NCBI Conserved Domain Search

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) and similar proteins; MRC1, also called MMR, C-type lectin domain family 13 member D (CLEC13D), C-type lectin domain family 13 member D-like (CLEC13DL), macrophage mannose receptor 1-like protein 1 (MRC1L1), or CD206, mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains. MRC1 acts as phagocytic receptor for bacteria, fungi and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467785 Cd Length: 123 Bit Score: 227.63 E-value: 4.28e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   23 RQFLIYNEDHKRCVDALSAISVQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWASVTLYACDSKSEYQKWEC 102
Cdd:cd23407     1 RSFLIYNEDHNRCVQARSSSSVTTATCNPNAESQKFRWVSGSQILSVAFKLCLGVPSKKDWVTVTLFPCNEKSELQKWEC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 341940970  103 KNDTLFGIKGTELYFNYGNRQEKNIKLYKGSGLWSRWKVYGTT 145
Cdd:cd23407    81 KNDTLLALKGEDLYFNYGNRQEKNVMLYKGSGLWSRWKIYGTT 123

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 130.80 E-value: 2.32e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   24 QFLIYNEDHKRCVDALSAIS-VQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWASVTLYACDSKSEYQKWEC 102
Cdd:cd23385     2 SFLIYNEDLGKCLAARSSSSkVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEDELQKWKC 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 341940970  103 KNDTLFGIKGTELYFNYgNRQEKNIKLYKGSGLWSRWK 140
Cdd:cd23385    82 SKDGLLLLKGLGLLLLY-DKSGKNVVVSKGSGLSSRWK 118

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 123.09 E-value: 1.42e-32

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    362 CPNQWWPYAGHCYRIHREEKKIQKyALQACRKEGGDLASIHSIEEFDFIFSQLG-YEPNDELWIGLNDIKIQMYFEWSDG 440
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWED-AQAFCQSLGGHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPDSNGSWQWSDG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 341940970    441 TP-VTFTKWLPGEPsheNNRQEDCVVMKGKDGYWADRACEQPLGYICK 487
Cdd:smart00034   80 SGpVSYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 117.34 E-value: 1.35e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  372 HCYRIHREEKKIQKyALQACRKEGGDLASIHSIEEFDFIFSQLGYEPNDELWIGLNDIKIQMYFEWSDGTP-VTFTKWLP 450
Cdd:cd00037     1 SCYKFSTEKLTWEE-AQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAP 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 341940970  451 GEPSheNNRQEDCVVMK-GKDGYWADRACEQPLGYICKM 488
Cdd:cd00037    80 GEPN--PGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 114.62 E-value: 1.52e-29

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    944 CKEGWHLYKNKCFKIFGfaneEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDST--FNAWTGLNDINAEHMFLW 1021
Cdd:smart00034    1 CPSGWISYGGKCYKFST----EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssDYYWIGLSDPDSNGSWQW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940970   1022 TAGQG-VHYTNWGKGYPGGRRSslsyedaDCVVVIGGNsreaGTWMDDTCDSKQGYICQ 1079
Cdd:smart00034   77 SDGSGpVSYSNWAPGEPNNSSG-------DCVVLSTSG----GKWNDVSCTSKLPFVCE 124

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 113.87 E-value: 1.74e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  659 CFKLYakgkHEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYHelFWLGLTYGSPSEGFTWSDGSP-VSYE 737
Cdd:cd00037     2 CYKFS----TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD--VWIGLNDLSSEGTWKWSDGSPlVDYT 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 341940970  738 NWAYGEPNNYQNvEYCGELKGDPGMSWNDINCEHLNNWICQI 779
Cdd:cd00037    76 NWAPGEPNPGGS-EDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 113.85 E-value: 2.22e-29

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   1229 CPESeqtaWIPFYGHCYYFeSSFTRSWGQASLECLRMGASLVSIETAAESSFLSYRVEPLKSKTNFWIGMFR-NVEGKWL 1307
Cdd:smart00034    1 CPSG----WISYGGKCYKF-STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDpDSNGSWQ 75

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 341940970   1308 WLN-DNPVSFVNWKTGDPSGERNDCVVLASSSGLWNNIHCSSYKGFICK 1355
Cdd:smart00034   76 WSDgSGPVSYSNWAPGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 111.92 E-value: 1.29e-28

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    802 DGWVIYKDYQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNGGQSPYFIGM-LISMDKKFIWMDGSK- 879
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLsDPDSNGSWQWSDGSGp 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 341940970    880 VDFVAWATGEPNFANddENCVTMYTNSGFWNDINCGYPNNFICQ 923
Cdd:smart00034   83 VSYSNWAPGEPNNSS--GDCVVLSTSGGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 110.38 E-value: 4.08e-28

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    646 CPENWgtTSKTSMCFKLYakgkHEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYHElFWLGLTYGSPSEG 725
Cdd:smart00034    1 CPSGW--ISYGGKCYKFS----TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY-YWIGLSDPDSNGS 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 341940970    726 FTWSDGSP-VSYENWAYGEPNNyqNVEYCGELKGDPGmSWNDINCEHLNNWICQ 778
Cdd:smart00034   74 WQWSDGSGpVSYSNWAPGEPNN--SSGDCVVLSTSGG-KWNDVSCTSKLPFVCE 124

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 105.37 E-value: 2.40e-26

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    504 CRKGWKRHGFYCYLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVG-LRPEKYFWTGLSDVQNKGTFRWT-VD 581
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPDSNGSWQWSdGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 341940970    582 EQVQFTHWNADMPGRKAG-CVAMKTGvaGGLWDVLSCEEKAKFVCK 626
Cdd:smart00034   81 GPVSYSNWAPGEPNNSSGdCVVLSTS--GGKWNDVSCTSKLPFVCE 124

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 103.71 E-value: 4.92e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   387 ALQACRKEGGDLASIHSIEEFDFIFSQLGyEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLPgePSHENNRQEDCVVM 466
Cdd:pfam00059    7 AREACRKLGGHLVSINSAEELDFLSSTLK-KSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP--EPNNNGENEDCVEL 83

                           90       100
                   ....*....|....*....|..
gi 341940970   467 KGKDGYWADRACEQPLGYICKM 488
Cdd:pfam00059   84 SSSSGKWNDENCNSKNPFVCEK 105

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 103.47 E-value: 8.81e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  810 YQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYInKNGGQSPYFIGM-LISMDKKFIWMDGSK-VDFVAWAT 887
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-KKSSSSDVWIGLnDLSSEGTWKWSDGSPlVDYTNWAP 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 341940970  888 GEPNFaNDDENCVTMYTNS-GFWNDINCGYPNNFICQR 924
Cdd:cd00037    80 GEPNP-GGSEDCVVLSSSSdGKWNDVSCSSKLPFICEK 116

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 102.31 E-value: 1.86e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  954 KCFKIFgfanEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRD-STFNAWTGLNDINAEHMFLWTAGQG-VHYTN 1031
Cdd:cd00037     1 SCYKFS----TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKsSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970 1032 WGKGYPGgrrsslSYEDADCVVViggNSREAGTWMDDTCDSKQGYICQ 1079
Cdd:cd00037    77 WAPGEPN------PGGSEDCVVL---SSSSDGKWNDVSCSSKLPFICE 115

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 101.23 E-value: 7.11e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1229 CPESeqtaWIPFYGHCYYFeSSFTRSWGQASLECLRMGASLVSIETAAESSFLSYRVEplkSKTNFWIGMF-RNVEGKWL 1307
Cdd:cd03590     1 CPTN----WKSFQSSCYFF-STEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS---GNRSYWIGLSdEETEGEWK 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940970 1308 WLNDNPV--SFVNWKTGDPS---GERNDCVVLASSSGLWNNIHCSSYKGFICKM 1356
Cdd:cd03590    73 WVDGTPLnsSKTFWHPGEPNnwgGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 98.32 E-value: 4.17e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  1252 TRSWGQASLECLRMGASLVSIETAAESSFLSYRVEplKSKTNFWIGM-FRNVEGKWLWLNDNPVSFVNW-KTGDPSGERN 1329
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLK--KSNKYFWIGLtDRKNEGTWKWVDGSPVNYTNWaPEPNNNGENE 78

                           90       100
                   ....*....|....*....|....*..
gi 341940970  1330 DCVVLASSSGLWNNIHCSSYKGFICKM 1356
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 98.20 E-value: 9.33e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  362 CPNQWWPYAGHCYRIHREEK-------KIQKYALQACRkegGDLASIHSIEEFDFIF----SQLGYEPNDELWIGLNDIK 430
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLtweeaelRCRSFSIPGLI---AHLVSIHSQEENDFVYdlfeSSRGPDTPYGLWIGLHDRT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940970  431 IQMYFEWSDGTPVTFTKWLPGEPSHENNrQEDCVVMK---GKDGYWADRACEQPLGYICKM 488
Cdd:cd03589    78 SEGPFEWTDGSPVDFTKWAGGQPDNYGG-NEDCVQMWrrgDAGQSWNDMPCDAVFPYICKM 137

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 97.76 E-value: 9.57e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  646 CPENWgtTSKTSMCFKLyakgKHEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYhelfWLGLTyGSPSEG 725
Cdd:cd03590     1 CPTNW--KSFQSSCYFF----STEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY----WIGLS-DEETEG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940970  726 -FTWSDGSPV--SYENWAYGEPNNYQNV-EYCGELKGDPGmSWNDINCEHLNNWICQ 778
Cdd:cd03590    70 eWKWVDGTPLnsSKTFWHPGEPNNWGGGgEDCAELVYDSG-GWNDVPCNLEYRWICE 125

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 97.38 E-value: 1.62e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  362 CPNQWWPYAGHCYRIHREEKKIQKyALQACRKEGGDLASIHSIEEFDFIFSQLGYepNDELWIGLNDIKIQMYFEWSDGT 441
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEE-SRQFCEDMGAHLVIINSQEEQEFISKILSG--NRSYWIGLSDEETEGEWKWVDGT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 341940970  442 PV--TFTKWLPGEPSHENNRQEDCVVMKGKDGYWADRACEQPLGYICKM 488
Cdd:cd03590    78 PLnsSKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 96.53 E-value: 2.43e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  234 SKSALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSG-LWIGLNSLSVRSGWQWAGGSP-FRYLNWLPGSPSSE 311
Cdd:cd00037     6 STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEPNPG 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 341940970  312 PGKSCVSLNPGKNAKWENLECVQKLGYICKK 342
Cdd:cd00037    86 GSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 94.99 E-value: 8.93e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1243 HCYYFeSSFTRSWGQASLECLRMGASLVSIETAAESSFLSYRVePLKSKTNFWIGMFR-NVEGKWLWLNDNP-VSFVNWK 1320
Cdd:cd00037     1 SCYKF-STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-KKSSSSDVWIGLNDlSSEGTWKWSDGSPlVDYTNWA 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 341940970 1321 TGDPSGERN-DCVVL-ASSSGLWNNIHCSSYKGFICKM 1356
Cdd:cd00037    79 PGEPNPGGSeDCVVLsSSSDGKWNDVSCSSKLPFICEK 116

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 94.47 E-value: 9.35e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   670 KKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYhelFWLGLTYGSPSEGFTWSDGSPVSYENWAyGEPNNYQN 749
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDRKNEGTWKWVDGSPVNYTNWA-PEPNNNGE 76

                           90       100
                   ....*....|....*....|....*....
gi 341940970   750 VEYCGELKGDPGmSWNDINCEHLNNWICQ 778
Cdd:pfam00059   77 NEDCVELSSSSG-KWNDENCNSKNPFVCE 104

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 94.22 E-value: 1.28e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  514 YCYLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVGLRPEKYFWTGLSDVQNKGTFRWTV-DEQVQFTHWNAD 592
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDgSPLVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 341940970  593 MP--GRKAGCVAMKTGVAGGlWDVLSCEEKAKFVCKH 627
Cdd:cd00037    81 EPnpGGSEDCVVLSSSSDGK-WNDVSCSSKLPFICEK 116

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 93.31 E-value: 2.33e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   966 KKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTFNAWTGLNDINAEHMFLWTAGQGVHYTNWgkgypgGRRSSLS 1045
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNW------APEPNNN 74

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 341940970  1046 YEDADCVVViggnSREAGTWMDDTCDSKQGYICQT 1080
Cdd:pfam00059   75 GENEDCVEL----SSSSGKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 91.10 E-value: 1.96e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  362 CPNQWWPYAGHCYRiHREEKKIQKYALQACRKEGGDLASIHSIEEFDFIFSQlgyePNDELWIGLNDIKIQMYFEWSDGT 441
Cdd:cd03588     1 CEEGWDKFQGHCYR-HFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN----AQDYQWIGLNDRTIEGDFRWSDGH 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970  442 PVTFTKWLPGEPSHENNRQEDCVVMKGKD-GYWADRACEQPLGYICKM 488
Cdd:cd03588    76 PLQFENWRPNQPDNFFATGEDCVVMIWHEeGEWNDVPCNYHLPFTCKK 123

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.

Pssm-ID: 128373 Cd Length: 49 Bit Score: 87.74 E-value: 4.04e-21

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 341940970    161 GNANGAVCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDKDKLFGFC 209
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 88.12 E-value: 1.66e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  812 YYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNGGQSpyFIGMlISMDK--KFIWMDGSKVDFVAWATGE 889
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYA--FIGI-TDLETegQFVYLDGGPLTYTNWKPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 341940970  890 PNFANDDENCVTMYTnSGFWNDINCGYPNNFICQ 923
Cdd:cd03591    81 PNNAGGGEDCVEMYT-SGKWNDVACNLTRLFVCE 113

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 86.27 E-value: 1.09e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  362 CPNQWWPYAGHCYRIHREEKKIQKyALQACRK--EGGDLASIHSIEEFDFIFSQL-GYEPNDE-LWIGLNDIKIQMYFEW 437
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSD-AELFCQKygPGAHLASIHSPAEAAAIASLIsSYQKAYQpVWIGLHDPQQSRGWEW 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940970  438 SDGTPVTFTKWLPGEPShenNRQEDCVVMKGKDGY--WADRACEQPLGYICK 487
Cdd:cd03594    80 SDGSKLDYRSWDRNPPY---ARGGYCAELSRSTGFlkWNDANCEERNPFICK 128

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 85.73 E-value: 1.50e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    234 SKSALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSG--LWIGLNSLSVRSGWQWAGGSP-FRYLNWLPGSPSS 310
Cdd:smart00034   16 STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGSGpVSYSNWAPGEPNN 95

                            90       100       110
                    ....*....|....*....|....*....|.
gi 341940970    311 EPGkSCVSLNpGKNAKWENLECVQKLGYICK 341
Cdd:smart00034   96 SSG-DCVVLS-TSGGKWNDVSCTSKLPFVCE 124

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 86.26 E-value: 1.69e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  646 CPENWgtTSKTSMCFKLYAkgkhEKKTWFESRDFCKAIG-----GELASIKSKDEQQVIWRLITSSGSYHELF--WLGLt 718
Cdd:cd03589     1 CPTFW--TAFGGYCYRFFG----DRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPDTPYglWIGL- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940970  719 YGSPSEG-FTWSDGSPVSYENWAYGEPNNYQNVEYCGEL--KGDPGMSWNDINCEHLNNWICQI 779
Cdd:cd03589    74 HDRTSEGpFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMwrRGDAGQSWNDMPCDAVFPYICKM 137

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 85.82 E-value: 1.88e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  802 DGWVIYKDYQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNGGqspYFIGML-ISMDKKFIWMDGSKV 880
Cdd:cd03590     3 TNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS---YWIGLSdEETEGEWKWVDGTPL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 341940970  881 --DFVAWATGEP-NFANDDENCVTMYTNSGFWNDINCGYPNNFICQR 924
Cdd:cd03590    80 nsSKTFWHPGEPnNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 84.96 E-value: 2.85e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   1096 DGFVTYGKSSYSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAFAW--MKMHPFNVPIWIALNSNLTNNEYTWTDRW-R 1172
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGSgP 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 341940970   1173 VRYTNWGADEPKLKSA-CVYMDVD-GYWRTSYCNESFYFLCK 1212
Cdd:smart00034   83 VSYSNWAPGEPNNSSGdCVVLSTSgGKWNDVSCTSKLPFVCE 124

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.

Pssm-ID: 238019 Cd Length: 48 Bit Score: 81.97 E-value: 4.74e-19

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970  162 NANGAVCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDKDKLFGFC 209
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 83.05 E-value: 1.12e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1106 YSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAFAWMKMHPF-NVPIWIALNSNLTNNEYTWTDRWR-VRYTNWGADEP 1183
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSsSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEP 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 341940970 1184 KLKSA--CVYMDV--DGYWRTSYCNESFYFLCKK 1213
Cdd:cd00037    83 NPGGSedCVVLSSssDGKWNDVSCSSKLPFICEK 116

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 82.79 E-value: 2.52e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  944 CKEGWHLYKNKCFKIFGfaneEKKSWQDARQACK-----GLKGNLVSIENAQEQAFVtYHM------RDSTFNAWTGLND 1012
Cdd:cd03589     1 CPTFWTAFGGYCYRFFG----DRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFV-YDLfessrgPDTPYGLWIGLHD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940970 1013 INAEHMFLWTAGQGVHYTNWGKGYPGGRrsslsYEDADCVVVIGGNSREaGTWMDDTCDSKQGYICQT 1080
Cdd:cd03589    76 RTSEGPFEWTDGSPVDFTKWAGGQPDNY-----GGNEDCVQMWRRGDAG-QSWNDMPCDAVFPYICKM 137

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 81.37 E-value: 2.84e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   818 KETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNGgqSPYFIGML-ISMDKKFIWMDGSKVDFVAWAtGEPNFANDD 896
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN--KYFWIGLTdRKNEGTWKWVDGSPVNYTNWA-PEPNNNGEN 77

                           90       100
                   ....*....|....*....|....*...
gi 341940970   897 ENCVTMYTNSGFWNDINCGYPNNFICQR 924
Cdd:pfam00059   78 EDCVELSSSSGKWNDENCNSKNPFVCEK 105

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 81.37 E-value: 3.49e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   237 ALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSGLWIGLNSLSVRSGWQWAGGSPFRYLNWLPGSPSSEPGKSC 316
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENEDC 80

                           90       100
                   ....*....|....*....|....*.
gi 341940970   317 VSLNPgKNAKWENLECVQKLGYICKK 342
Cdd:pfam00059   81 VELSS-SSGKWNDENCNSKNPFVCEK 105

Fibronectin type II domain;

Pssm-ID: 459645 Cd Length: 42 Bit Score: 77.61 E-value: 1.29e-17

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 341940970   168 CAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDKDKLFGFC 209
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 79.65 E-value: 1.74e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  668 HEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYhelFWLGLTyGSPSEG-FTWSDGSPVSYENWAYGEPNN 746
Cdd:cd03591     8 GEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTY---AFIGIT-DLETEGqFVYLDGGPLTYTNWKPGEPNN 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 341940970  747 YQNVEYCGELKGDPGmsWNDINCEHLNNWICQI 779
Cdd:cd03591    84 AGGGEDCVEMYTSGK--WNDVACNLTRLFVCEF 114

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 78.18 E-value: 9.40e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  646 CPENWgtTSKTSMCFKLYAKgkheKKTWFESRDFCKAI--GGELASIKSKDEQQVIWRLITSSGSYHELFWLGLTYGSPS 723
Cdd:cd03594     1 CPKGW--LPYKGNCYGYFRQ----PLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQS 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940970  724 EGFTWSDGSPVSYENWAYGEPnnYQNVEYCGELKGDPG-MSWNDINCEHLNNWICQ 778
Cdd:cd03594    75 RGWEWSDGSKLDYRSWDRNPP--YARGGYCAELSRSTGfLKWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 77.62 E-value: 1.07e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  944 CKEGWHLYKNKCFKIFgfanEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTfnaWTGLNDINAEHMFLWTA 1023
Cdd:cd03588     1 CEEGWDKFQGHCYRHF----PDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940970 1024 GQGVHYTNWGKGYPggrrSSLSYEDADCVVVIGgnsREAGTWMDDTCDSKQGYICQ 1079
Cdd:cd03588    74 GHPLQFENWRPNQP----DNFFATGEDCVVMIW---HEEGEWNDVPCNYHLPFTCK 122

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 77.13 E-value: 1.09e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   524 TFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVGLRPeKYFWTGLSDVQNKGTFRWTVDEQVQFTHW--NADMPGRKAGCV 601
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTWKWVDGSPVNYTNWapEPNNNGENEDCV 81

                           90       100
                   ....*....|....*....|....*.
gi 341940970   602 AMKTgvAGGLWDVLSCEEKAKFVCKH 627
Cdd:pfam00059   82 ELSS--SSGKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 77.73 E-value: 1.10e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  944 CKEGWHLYKNKCFkifgFANEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRdSTFNAWTGLNDINAEHMFLWTA 1023
Cdd:cd03590     1 CPTNWKSFQSSCY----FFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLSDEETEGEWKWVD 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940970 1024 GQGVH--YTNWGKGYPggrrSSLSYEDADCVVVIGgnsrEAGTWMDDTCDSKQGYICQT 1080
Cdd:cd03590    76 GTPLNssKTFWHPGEP----NNWGGGGEDCAELVY----DSGGWNDVPCNLEYRWICEK 126

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 77.03 E-value: 1.30e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  812 YYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNgGQSPYFIGMLiSMDKKFIWMDGSKVDFVA--WATGE 889
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKY-NLGYYWIDGN-DINNEGTWVDTDKKELEYknWAPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 341940970  890 PNfANDDENCVTMY-TNSGFWNDINCGYPNNFICQR 924
Cdd:cd03592    81 PN-NGRNENCLEIYiKDNGKWNDEPCSKKKSAICYT 115

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 76.63 E-value: 3.49e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  804 WVIYKDYQYYFSKEKETMDNARAFCKK-----NFGDLATIKSESEKKFLWKYINKNGGQSPYFiGMLISMDKK-----FI 873
Cdd:cd03589     5 WTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRGPDTPY-GLWIGLHDRtsegpFE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940970  874 WMDGSKVDFVAWATGEPNFANDDENCVTMYTNS---GFWNDINCGYPNNFIC 922
Cdd:cd03589    84 WTDGSPVDFTKWAGGQPDNYGGNEDCVQMWRRGdagQSWNDMPCDAVFPYIC 135

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 75.03 E-value: 6.21e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  374 YRIHREEKKIQKyALQACRKEGGDLASIHSIEE----FDFIFSQLGYepndeLWIGLNDIKIQMYFEWSDGTPVTFTKWL 449
Cdd:cd03591     4 FVTNGEEKNFDD-AQKLCSEAGGTLAMPRNAAEnaaiASYVKKGNTY-----AFIGITDLETEGQFVYLDGGPLTYTNWK 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 341940970  450 PGEPsheNNR--QEDCVVMKgKDGYWADRACEQPLGYIC 486
Cdd:cd03591    78 PGEP---NNAggGEDCVEMY-TSGKWNDVACNLTRLFVC 112

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 75.10 E-value: 1.02e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1237 WIPFYGHCY-YFesSFTRSWGQASLECLRMGAS--LVSIETAAESSFL-SYRVEPLKSKTNFWIGMFRNVEGK-WLWLND 1311
Cdd:cd03594     5 WLPYKGNCYgYF--RQPLSWSDAELFCQKYGPGahLASIHSPAEAAAIaSLISSYQKAYQPVWIGLHDPQQSRgWEWSDG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 341940970 1312 NPVSFVNWKTGDPSGERNDCVVLASSSG--LWNNIHCSSYKGFICK 1355
Cdd:cd03594    83 SKLDYRSWDRNPPYARGGYCAELSRSTGflKWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 73.00 E-value: 9.38e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  659 CFKL-YAKGKHEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYHELFWLGL--------TYGSPSEGFTWS 729
Cdd:cd03595    12 CYKIaYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLrrssqynvTSSACSSLYYWL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940970  730 DGSPVSYENWAYGEPNNyqNVEYCGEL---------KGDPGM-SWNDINCEHLNNWICQ 778
Cdd:cd03595    92 DGSISTFRNWYVDEPSC--GSEVCVVMyhqpsapagQGGPYLfQWNDDNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 71.62 E-value: 2.31e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1229 CPeseqTAWIPFYGHCY-YFESSFTrsWGQASLECLRMG-----ASLVSIETAAESSFLSYRVEPLKSK---TNFWIGMF 1299
Cdd:cd03589     1 CP----TFWTAFGGYCYrFFGDRLT--WEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPdtpYGLWIGLH 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940970 1300 -RNVEGKWLWLNDNPVSFVNWKTGDPS--GERNDCVVL---ASSSGLWNNIHCSSYKGFICKM 1356
Cdd:cd03589    75 dRTSEGPFEWTDGSPVDFTKWAGGQPDnyGGNEDCVQMwrrGDAGQSWNDMPCDAVFPYICKM 137

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 70.30 E-value: 4.41e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1237 WIPFYGHCY-YFESSftRSWGQASLECLRMGASLVSIETAAESSFLSYRVEPLKsktnfWIGMF-RNVEGKWLWLNDNPV 1314
Cdd:cd03588     5 WDKFQGHCYrHFPDR--ETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-----WIGLNdRTIEGDFRWSDGHPL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970 1315 SFVNWKTGDP-----SGErnDCVVLA-SSSGLWNNIHCSSYKGFICKM 1356
Cdd:cd03588    78 QFENWRPNQPdnffaTGE--DCVVMIwHEEGEWNDVPCNYHLPFTCKK 123

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 69.04 E-value: 7.08e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  1112 KLPWHEAETYCKDHTSLLASILDPYSNAFAWMKMHPFNVPIWIALNSNLTNNEYTWTDRWRVRYTNWGA--DEPKLKSAC 1189
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPepNNNGENEDC 80

                           90       100
                   ....*....|....*....|....*
gi 341940970  1190 VYMD-VDGYWRTSYCNESFYFLCKK 1213
Cdd:pfam00059   81 VELSsSSGKWNDENCNSKNPFVCEK 105

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 69.08 E-value: 1.01e-13

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970     27 IYNEDHKRCVDALSAIS-VQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWaSVTLYACDSKSEYQKWECKND 105
Cdd:smart00458    1 IISGNTGKCLDVNGNKNpVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANGNTGS-TVTLYSCDGTNDNQYWEVNKD 79

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 341940970    106 TLFGIKGTELYFN-YGNRQEKNIKLYKGSG-LWSRWKVY 142
Cdd:smart00458   80 GTIRNPDSGKCLDvKDGNTGTKVILWTCSGnPNQKWIFE 118

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 68.17 E-value: 2.05e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1246 YFESSFTRSWGQASLECLRMGASLVSIETAAESSFLSYRVEPLKSKTnFWIGMF-RNVEGKWLWLNDNPVSFVNWKTGDP 1324
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGY-YWIDGNdINNEGTWVDTDKKELEYKNWAPGEP 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 341940970 1325 SGERN-DCVVLA-SSSGLWNNIHCSSYKGFIC 1354
Cdd:cd03592    82 NNGRNeNCLEIYiKDNGKWNDEPCSKKKSAIC 113

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 67.99 E-value: 2.81e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  646 CPENWgtTSKTSMCFKLYakgkHEKKTWFESRDFCKAIGGELASIKSKDEQQVIwrlitsSGSYHELFWLGLTYGSPSEG 725
Cdd:cd03588     1 CEEGW--DKFQGHCYRHF----PDRETWEDAERRCREQQGHLSSIVTPEEQEFV------NNNAQDYQWIGLNDRTIEGD 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940970  726 FTWSDGSPVSYENWAYGEPNNY-QNVEYCGELKGDPGMSWNDINCEHLNNWICQ 778
Cdd:cd03588    69 FRWSDGHPLQFENWRPNQPDNFfATGEDCVVMIWHEEGEWNDVPCNYHLPFTCK 122

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 68.38 E-value: 4.41e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1239 PFYGHCYYFESSFTRSWGQASLECLRMGASLVSIETAAESSFLSYRVEPLK-SKTNFWIGMFRNVEG---------KWLW 1308
Cdd:cd03595    11 PCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRaSDGDFWIGLRRSSQYnvtssacssLYYW 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940970 1309 LNDNPVSFVNWKTGDPSGERNDCVVL----ASSSGL-------WNNIHCSSYKGFICK 1355
Cdd:cd03595    91 LDGSISTFRNWYVDEPSCGSEVCVVMyhqpSAPAGQggpylfqWNDDNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 67.02 E-value: 4.68e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  668 HEKKTWFESRDFCKAIGGELASIKSKDEQQVI--WRLITSSGSYhelfWLGLTygSPSEGFTW--SDGSPVSYENWAYGE 743
Cdd:cd03592     7 TEKMTFNEAVKYCKSRGTDLVAIQNAEENALLngFALKYNLGYY----WIDGN--DINNEGTWvdTDKKELEYKNWAPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 341940970  744 PNNYQNvEYCGE-LKGDPGMsWNDINCEHLNNWICQ 778
Cdd:cd03592    81 PNNGRN-ENCLEiYIKDNGK-WNDEPCSKKKSAICY 114

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 66.97 E-value: 5.20e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  803 GWVIYKDYQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYInkngGQSPYFIGMLIS-MDKKFIWMDGSKVD 881
Cdd:cd03593     4 DWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQI----GSSSYWIGLSREkSEKPWKWIDGSPLN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 341940970  882 fvawATGEPNFANDDENCVtmYTNSGFWNDINCGYPNNFICQR 924
Cdd:cd03593    80 ----NLFNIRGSTKSGNCA--YLSSTGIYSEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 66.59 E-value: 7.10e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  646 CPENWgttsktsMCF--KLYAKGKhEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGsyhelFWLGLTYGSPS 723
Cdd:cd03593     1 CPKDW-------ICYgnKCYYFSM-EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS-----YWIGLSREKSE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 341940970  724 EGFTWSDGSPVSyeNWayGEPNNYQNVEYCGELKGDpgmSWNDINCEHLNNWICQ 778
Cdd:cd03593    68 KPWKWIDGSPLN--NL--FNIRGSTKSGNCAYLSST---GIYSEDCSTKKRWICE 115

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 66.63 E-value: 1.04e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  803 GWVIYKDYQY-YFSKEKeTMDNARAFCKKNF--GDLATIKSESEKKFLWKYINK-NGGQSPYFIGML-ISMDKKFIWMDG 877
Cdd:cd03594     4 GWLPYKGNCYgYFRQPL-SWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSyQKAYQPVWIGLHdPQQSRGWEWSDG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970  878 SKVDFVAWATGEPnfANDDENCVTMYTNSGF--WNDINCGYPNNFICQ 923
Cdd:cd03594    83 SKLDYRSWDRNPP--YARGGYCAELSRSTGFlkWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 65.47 E-value: 1.55e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  234 SKSALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSGL-WIGLNSLSVRSGWQWAGGSPFRYLNWLPGSPSSEP 312
Cdd:cd03592     6 STEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPNNGR 85

                          90       100
                  ....*....|....*....|....*...
gi 341940970  313 GKSCVSLNPGKNAKWENLECVQKLGYIC 340
Cdd:cd03592    86 NENCLEIYIKDNGKWNDEPCSKKKSAIC 113

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 64.70 E-value: 2.63e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  387 ALQACRKEGGDLASIHSIEEFDFIfSQLGYEPNDELWIGLndIKIQMYFEWSDGTPVTFTKWLPGEPShennRQEDCVVM 466
Cdd:cd03602    15 AQQYCRENYTDLATVQNQEDNALL-SNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQPF----GQGDCATM 87

                          90       100
                  ....*....|....*....|
gi 341940970  467 kGKDGYWADRACEQPLGYIC 486
Cdd:cd03602    88 -YSSGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 64.39 E-value: 3.53e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  812 YYFSKEKETMDNARAFCKKNF-GDLATIKSESEKKFLWKYInKNGGQSPYFIGMLI---SMDKKFIWMDGSKVDFVAWAT 887
Cdd:cd03598     4 YRFVKSPRTFRDAQVICRRCYrGNLASIHSFAFNYRVQRLV-STLNQAQVWIGGIItgkGRCRRFSWVDGSVWNYAYWAP 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 341940970  888 GEPnfANDDENCVTMYTNSGFWNDINCGYPNNFICQ 923
Cdd:cd03598    83 GQP--GNRRGHCVELCTRGGHWRRAHCKLRRPFICS 116

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 63.89 E-value: 6.44e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1229 CPESeqtaWIPFYGHCYYFeSSFTRSWGQASLECLRMGASLVSIETAAESSFLSYRVEPLksktNFWIGM-FRNVEGKWL 1307
Cdd:cd03593     1 CPKD----WICYGNKCYYF-SMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS----SYWIGLsREKSEKPWK 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970 1308 WLNDNPVSfvNWKTGDPSGERNDCVVLaSSSGLwNNIHCSSYKGFICK 1355
Cdd:cd03593    72 WIDGSPLN--NLFNIRGSTKSGNCAYL-SSTGI-YSEDCSTKKRWICE 115

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 64.14 E-value: 6.63e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  199 DYDKDKLFGFCPLHFEGSErlwnkdpltgilyqinsksalTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSsglW 278
Cdd:cd03588     2 EEGWDKFQGHCYRHFPDRE---------------------TWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---W 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940970  279 IGLNSLSVRSGWQWAGGSPFRYLNWLPGSPSS--EPGKSCVSLNPGKNAKWENLECVQKLGYICKKG 343
Cdd:cd03588    58 IGLNDRTIEGDFRWSDGHPLQFENWRPNQPDNffATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 63.51 E-value: 8.45e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  362 CPNQWWPYAGHCYRIHREEKKIQKyALQACRKEGGDLASIHSIEEFDFIFSQLGyepNDELWIGLNDIKIQMYFEWSDGT 441
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNE-SKEACSSKNSSLLKIDDEEELEFLQSQIG---SSSYWIGLSREKSEKPWKWIDGS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 341940970  442 PvtFTKWLpgePSHENNRQEDCVVMKGKDGYWADraCEQPLGYICK 487
Cdd:cd03593    77 P--LNNLF---NIRGSTKSGNCAYLSSTGIYSED--CSTKKRWICE 115

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 63.55 E-value: 8.63e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  387 ALQACRKEGGDLASIHSIEEFDFIFSQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLPGEPSheNNRQEDCVVM 466
Cdd:cd03592    15 AVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN--NGRNENCLEI 92

                          90       100
                  ....*....|....*....|.
gi 341940970  467 -KGKDGYWADRACEQPLGYIC 486
Cdd:cd03592    93 yIKDNGKWNDEPCSKKKSAIC 113

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 63.08 E-value: 9.23e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  957 KIFgFANEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTFNAWTGLNDINAEHMFLWTAGQGVHYTNWGKGY 1036
Cdd:cd03591     2 KIF-VTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 341940970 1037 PGGRrsslsYEDADCVVVIGGnsreaGTWMDDTCDSKQGYICQ 1079
Cdd:cd03591    81 PNNA-----GGGEDCVEMYTS-----GKWNDVACNLTRLFVCE 113

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 63.75 E-value: 9.77e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  803 GWVIYKDYQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLwkyinKNGGQSPYFIGMLISM-DKKFIWMDGSKVD 881
Cdd:cd03588     4 GWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV-----NNNAQDYQWIGLNDRTiEGDFRWSDGHPLQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 341940970  882 FVAWATGEP-NFANDDENCVTM-YTNSGFWNDINCGYPNNFICQR 924
Cdd:cd03588    79 FENWRPNQPdNFFATGEDCVVMiWHEEGEWNDVPCNYHLPFTCKK 123

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 63.54 E-value: 1.08e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  944 CKEGWHLYKNKCFKIFGfaneEKKSWQDARQACKGLK--GNLVSIENAQEQAFVT-----YHMRDStfNAWTGLNDINAE 1016
Cdd:cd03594     1 CPKGWLPYKGNCYGYFR----QPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIAslissYQKAYQ--PVWIGLHDPQQS 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940970 1017 HMFLWTAGQGVHYTNWGKGYPGGRRSSlsyedadCVVViggnSREAG--TWMDDTCDSKQGYICQ 1079
Cdd:cd03594    75 RGWEWSDGSKLDYRSWDRNPPYARGGY-------CAEL----SRSTGflKWNDANCEERNPFICK 128

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 62.78 E-value: 1.25e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  810 YQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNGGQSpyFIGMLISMDkKFIWMDGSKVDFVAWATGE 889
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAA--WIGLYRDVD-SWRWSDGSESSFRNWNTFQ 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 341940970  890 PnFANDDenCVTMYTNsGFWNDINCGYPNNFIC 922
Cdd:cd03602    78 P-FGQGD--CATMYSS-GRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 63.37 E-value: 1.95e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  807 YKDYQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNG-GQSPYFIGMLISMDK---------KFIWMD 876
Cdd:cd03595    13 YKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRaSDGDFWIGLRRSSQYnvtssacssLYYWLD 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940970  877 GSKVDFVAWATGEPNFANddENCVTMY----TNSGF-------WNDINCGYPNNFICQ 923
Cdd:cd03595    93 GSISTFRNWYVDEPSCGS--EVCVVMYhqpsAPAGQggpylfqWNDDNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 62.41 E-value: 3.18e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  504 CRKGWKRHGfYCYLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLV--GLRPEKYFWTGLSDVQNKGTFRWTVD 581
Cdd:cd03596     1 CLKGTKIHK-KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVkaSVPGNWEVWLGINDMVAEGKWVDVNG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 341940970  582 EQVQFTHWNADMP-----GRKAGCVAMKTGVAGGLWDVlSCEEKAKFVC 625
Cdd:cd03596    80 SPISYFNWEREITaqpdgGKRENCVALSSSAQGKWFDE-DCRREKPYVC 127

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 62.38 E-value: 3.63e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  504 CRKGWKRHGFYCYLIGSTLSTFTDANHTCTN-----EKAYLTTVEDRYEQAFLT----SLVGLRPEKYFWTGLSDVQNKG 574
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYdlfeSSRGPDTPYGLWIGLHDRTSEG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940970  575 TFRWTVDEQVQFTHWNADMP---GRKAGCVAM-KTGVAGGLWDVLSCEEKAKFVCKH 627
Cdd:cd03589    81 PFEWTDGSPVDFTKWAGGQPdnyGGNEDCVQMwRRGDAGQSWNDMPCDAVFPYICKM 137

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 61.70 E-value: 4.04e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  371 GHCYRIHREEKKIQKyALQACRK-EGGDLASIHSiEEFDFIFSQLGYEPND-ELWIG--LNDIKIQMYFEWSDGTPVTFT 446
Cdd:cd03598     1 GRCYRFVKSPRTFRD-AQVICRRcYRGNLASIHS-FAFNYRVQRLVSTLNQaQVWIGgiITGKGRCRRFSWVDGSVWNYA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 341940970  447 KWLPGEPShenNRQEDCVVMKGKDGYWADRACEQPLGYIC 486
Cdd:cd03598    79 YWAPGQPG---NRRGHCVELCTRGGHWRRAHCKLRRPFIC 115

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 61.29 E-value: 4.93e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  387 ALQACRKEGGDLASIHSIEEFDFIFSQLGYepNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLPGEPSHENNRQEDCVVM 466
Cdd:cd03603    15 AQTLAESLGGHLVTINSAEENDWLLSNFGG--YGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNNGGGNEDYAAI 92

                          90
                  ....*....|....
gi 341940970  467 ---KGKDGYWADRA 477
Cdd:cd03603    93 nhfPGISGKWNDLA 106

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 60.01 E-value: 1.60e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  504 CRKGWKRHGFYCYLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLvgLRPEKYFWTGLSDVQNKGTFRWtVD-- 581
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKI--LSGNRSYWIGLSDEETEGEWKW-VDgt 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940970  582 -EQVQFTHWNADMPGRKAG----CVAMKTgvAGGLWDVLSCEEKAKFVCK 626
Cdd:cd03590    78 pLNSSKTFWHPGEPNNWGGggedCAELVY--DSGGWNDVPCNLEYRWICE 125

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 59.70 E-value: 1.91e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  961 FANEEKKSWQDARQACKGLKGNLVSIENAQEQAFVtyHMRDSTFNA---WTGLNDINAEHMFLWTAGQGVHYTNWGKGYP 1037
Cdd:cd03592     4 HYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALL--NGFALKYNLgyyWIDGNDINNEGTWVDTDKKELEYKNWAPGEP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 341940970 1038 GGRRSSlsyedaDCVVvigGNSREAGTWMDDTCDSKQGYICQT 1080
Cdd:cd03592    82 NNGRNE------NCLE---IYIKDNGKWNDEPCSKKKSAICYT 115

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 60.08 E-value: 1.98e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  504 CRKGWKRHGFYCYLIGSTLSTFTDANHTCTNEK--AYLTTVEDRYEQAFLTSLVG--LRPEKYFWTGLSDVQNKGTFRWT 579
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISsyQKAYQPVWIGLHDPQQSRGWEWS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970  580 VDEQVQFTHWNADMPGRKAG-CVAMKTGVAGGLWDVLSCEEKAKFVCK 626
Cdd:cd03594    81 DGSKLDYRSWDRNPPYARGGyCAELSRSTGFLKWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 59.71 E-value: 2.20e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  944 CKEGWHLYKnKCFKIFgfanEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTFNA---WTGLNDINAEHMFL 1020
Cdd:cd03596     1 CLKGTKIHK-KCYLVS----EETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNwevWLGINDMVAEGKWV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940970 1021 WTAGQGVHYTNWGKGYP----GGRRSSlsyedadCVVViggNSREAGTWMDDTCDSKQGYICQ 1079
Cdd:cd03596    76 DVNGSPISYFNWEREITaqpdGGKREN-------CVAL---SSSAQGKWFDEDCRREKPYVCE 128

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 58.85 E-value: 2.87e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1262 CLRMGASLVSIETAAESSFLSYRVEplKSKTNFWIGMF-RNVEGKWLWLNDNPVSFVNWKTGDPSGERN--DCVVLAsSS 1338
Cdd:cd03591    20 CSEAGGTLAMPRNAAENAAIASYVK--KGNTYAFIGITdLETEGQFVYLDGGPLTYTNWKPGEPNNAGGgeDCVEMY-TS 96

                          90
                  ....*....|....*.
gi 341940970 1339 GLWNNIHCSSYKGFIC 1354
Cdd:cd03591    97 GKWNDVACNLTRLFVC 112

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) and similar proteins; MRC2, also called C-type mannose receptor 2, C-type lectin domain family 13 member E (CLEC13E), endocytic receptor 180 (Endo180), urokinase-type plasminogen activator receptor-associated protein (UPARAP), UPAR-associated protein, urokinase receptor-associated protein, or CD280, may play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). MRC2 contains an atypical ricin B-type lectin domain at the N-terminus. The typical ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. In contrast, the ninth, tenth and eleventh beta strands, comprising the gamma subdomain, are missing in the ricin B-type lectin domain of MRC2.

Pssm-ID: 467786 Cd Length: 124 Bit Score: 58.65 E-value: 5.18e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   25 FLIYNEDHKRCVDALSAISVQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVP---SKTDWASVTLYACDSKSEYQKWE 101
Cdd:cd23408     3 FLIYSDGAQGCLEVRDSVVRLSPACNTSSPAQQWKWVSRNRLFNLGSMQCLGVSgpnGSGTSATLGTYECDRESVNMRWH 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940970  102 CKN--DTLfgikgtELYFNYGNRQEKNIKLYKGSGLWS-RWKVYGTTD 146
Cdd:cd23408    83 CRTlgEQL------SQHLGARTANGNPSTLERGDQARSsQWRIYGSEQ 124

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 58.47 E-value: 5.44e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  234 SKSALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSgLWIGLNSLSVRSGWQWAGGSPFR--YLNWLPGSPSS- 310
Cdd:cd03590    16 STEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEETEGEWKWVDGTPLNssKTFWHPGEPNNw 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 341940970  311 -EPGKSCVSLNPGKNAkWENLECVQKLGYICKK 342
Cdd:cd03590    95 gGGGEDCAELVYDSGG-WNDVPCNLEYRWICEK 126

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 57.77 E-value: 6.04e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1245 YYFESSfTRSWGQASLECLRMGASLVSIETAAESSFLSYRVEplKSKTNFWIGMFRNVEGkWLWLNDNPVSFVNWKTGDP 1324
Cdd:cd03602     3 FYLVNE-SKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSR--VSNSAAWIGLYRDVDS-WRWSDGSESSFRNWNTFQP 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 341940970 1325 SGeRNDCVVLaSSSGLWNNIHCSSYKGFIC 1354
Cdd:cd03602    79 FG-QGDCATM-YSSGRWYAALCSALKPFIC 106

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 57.77 E-value: 6.10e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1106 YSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAfAWMKMHPF-NVPIWIALNSnlTNNEYTWTDRWRVRYTNWGADEPK 1184
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNA-LLSNLSRVsNSAAWIGLYR--DVDSWRWSDGSESSFRNWNTFQPF 79

                          90       100
                  ....*....|....*....|....*..
gi 341940970 1185 LKSACVYMDVDGYWRTSYCNESFYFLC 1211
Cdd:cd03602    80 GQGDCATMYSSGRWYAALCSALKPFIC 106

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 58.20 E-value: 6.27e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  668 HEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSyhelFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNY 747
Cdd:cd03603     7 DGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGA----SWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNN 82

                          90       100
                  ....*....|....*....|...
gi 341940970  748 Q----NVEYCGELKGDPGmSWND 766
Cdd:cd03603    83 GggneDYAAINHFPGISG-KWND 104

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 58.36 E-value: 6.49e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  504 CRKGWKRHGFYCYLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVglrpEKYFWTGLSDVQNKGTFRWTVDEQ 583
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNA----QDYQWIGLNDRTIEGDFRWSDGHP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 341940970  584 VQFTHWNADMPGR--KAG--CVAMkTGVAGGLWDVLSCEEKAKFVCK 626
Cdd:cd03588    77 LQFENWRPNQPDNffATGedCVVM-IWHEEGEWNDVPCNYHLPFTCK 122

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 57.82 E-value: 7.32e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  964 EEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTfNAWTGLNDINAEHMFLWTAGQGVHYTNWGKGYPGGrrSS 1043
Cdd:cd03603     7 DGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHN--NG 83

                          90       100
                  ....*....|....*....|....
gi 341940970 1044 LSYEDadcVVVIGGNSREAGTWMD 1067
Cdd:cd03603    84 GGNED---YAAINHFPGISGKWND 104

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 57.85 E-value: 8.52e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1242 GHCYYFESSfTRSWGQASLECLRM-GASLVSIEtaaeSSFLSYRVEPLKSKTN---FWIGMFRNVEGK---WLWLNDNPV 1314
Cdd:cd03598     1 GRCYRFVKS-PRTFRDAQVICRRCyRGNLASIH----SFAFNYRVQRLVSTLNqaqVWIGGIITGKGRcrrFSWVDGSVW 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 341940970 1315 SFVNWKTGDPSGERNDCVVLASSSGLWNNIHCSSYKGFIC 1354
Cdd:cd03598    76 NYAYWAPGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFIC 115

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose receptor (MRC)-like proteins; The subfamily corresponds to a group of uncharacterized ricin B-type lectin beta-trefoil domain-containing proteins from Gnathostomata. They show high sequence similarity with macrophage mannose receptor (MRC) family proteins.

Pssm-ID: 467790 Cd Length: 127 Bit Score: 58.18 E-value: 8.53e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   21 DARQFLIYNEDHKRC--VDALSAISVQTATCNPEAESQKFRWVSDSQ-IMSVAFKLCLGVPSKTDWASVTLYACDSKsEY 97
Cdd:cd23412     1 EVQGFMIRNVQLEKCiqVDHGESERVSLAECKPHSEHQQWSWDPETRaLSSLHTGECLTVLKIQEFGSVRLEPCGSR-EP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 341940970   98 QKWECKNDTLFGIKGTELYFNyGNRQEKNIKLYKGSGLWSRWK 140
Cdd:cd23412    80 QAWSCSKKGHLTLQGLGLHLS-ARHSSHKVFVSKEKGKFSKWK 121

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 58.17 E-value: 8.96e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1246 YFESSFTRSWGQASLECLRMGASLVSIETAAESSFLS-YRVEPLKSKTNFWIGMFRNV-EGKWLWLNDNPVSFVNWKTGD 1323
Cdd:cd03596    12 YLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdYVKASVPGNWEVWLGINDMVaEGKWVDVNGSPISYFNWEREI 91

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 341940970 1324 PS----GERNDCVVLASSS-GLWNNIHCSSYKGFIC 1354
Cdd:cd03596    92 TAqpdgGKRENCVALSSSAqGKWFDEDCRREKPYVC 127

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 57.34 E-value: 1.22e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  944 CKEGWHLYKNKCFKIFgfanEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTFnaWTGLNDINAEHMFLWTa 1023
Cdd:cd03593     1 CPKDWICYGNKCYYFS----MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWI- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940970 1024 gQGVHYTNWGKgypggrrSSLSYEDADCVVViggnsreAGTWMDDT-CDSKQGYICQ 1079
Cdd:cd03593    74 -DGSPLNNLFN-------IRGSTKSGNCAYL-------SSTGIYSEdCSTKKRWICE 115

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 57.38 E-value: 1.57e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  238 LTWHQARASCKQ--QNADLLSVTEIHEQMYLTGLTSSL---SSGLWIGLNSLSVRSGWQWAGGSPFRYLNWlPGSPSSEP 312
Cdd:cd03594    20 LSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYqkaYQPVWIGLHDPQQSRGWEWSDGSKLDYRSW-DRNPPYAR 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 341940970  313 GKSCVSLNPGKN-AKWENLECVQKLGYICK 341
Cdd:cd03594    99 GGYCAELSRSTGfLKWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.

Pssm-ID: 153071 Cd Length: 119 Bit Score: 56.77 E-value: 2.08e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  810 YQYYFSKEKETMDNARAFCKKNFGDLATIK---SESEKKFLWKYINKNGGqspYFIGM--LISMDKKFIWMDGSKV--DF 882
Cdd:cd03601     1 YEILCSDETMNYAKAGAFCRSRGMRLASLAmrdSEMRDAILAFTLVKGHG---YWVGAdnLQDGEYDFLWNDGVSLptDS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 341940970  883 VAWATGEPNFANDDENCVTMYTNSGFWNDINCGYPNNFICQ 923
Cdd:cd03601    78 DLWAPNEPSNPQSRQLCVQLWSKYNLLDDEYCGRAKRVICE 118

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 56.15 E-value: 3.23e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1106 YSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAFAWMKMHPFNVPIWIALNSNLTNNEYTWTDRWRVRYTNWGADEP-- 1183
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPnn 83

                          90       100
                  ....*....|....*....|....*....
gi 341940970 1184 -KLKSACVYMDVDGYWRTSYCNESFYFLC 1211
Cdd:cd03591    84 aGGGEDCVEMYTSGKWNDVACNLTRLFVC 112

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 56.82 E-value: 3.67e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  373 CYRI---HREEKKIQ-KYALQACRKEGGDLASIHSIEEFDFI--FSQLGYEPNDELWIGL--------NDIKIQMYFEWS 438
Cdd:cd03595    12 CYKIayfQDSRRRLNfEEARQACREDGGELLSIESENEQKLIerFIQTLRASDGDFWIGLrrssqynvTSSACSSLYYWL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  439 DGTPVTFTKWLPGEPSHENnrqEDCVVM-------KGKDGY----WADRACEQPLGYICK 487
Cdd:cd03595    92 DGSISTFRNWYVDEPSCGS---EVCVVMyhqpsapAGQGGPylfqWNDDNCNMKNNFICK 148

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 55.51 E-value: 5.10e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  516 YLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVGLRpeKYFWTGLSDVQNKGTFRWTVDEQVQFTHWNADMPG 595
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY--GASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80


                  .
gi 341940970  596 R 596
Cdd:cd03603    81 N 81

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 56.21 E-value: 5.50e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  238 LTWHQARASCKQ-----QNADLLSVTEIHEQMYLTGLTSSLS-----SGLWIGLNSLSVRSGWQWAGGSPFRYLNWLPGS 307
Cdd:cd03589    20 LTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRgpdtpYGLWIGLHDRTSEGPFEWTDGSPVDFTKWAGGQ 99

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 341940970  308 PSSEPG-KSCVSLNPGKNA--KWENLECVQKLGYICK 341
Cdd:cd03589   100 PDNYGGnEDCVQMWRRGDAgqSWNDMPCDAVFPYICK 136

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 55.07 E-value: 5.55e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  238 LTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSGLWIGLnsLSVRSGWQWAGGSPFRYLNWLPGSPSsePGKSCV 317
Cdd:cd03602    10 KTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQPF--GQGDCA 85

                          90       100
                  ....*....|....*....|...
gi 341940970  318 SLNPgkNAKWENLECVQKLGYIC 340
Cdd:cd03602    86 TMYS--SGRWYAALCSALKPFIC 106

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 55.07 E-value: 5.71e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  669 EKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYhelFWLGLTYGspSEGFTWSDGSPVSYENWAygePNNYQ 748
Cdd:cd03602     8 ESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSA---AWIGLYRD--VDSWRWSDGSESSFRNWN---TFQPF 79

                          90       100
                  ....*....|....*....|....*....
gi 341940970  749 NVEYCGELKGDPgmSWNDINCEHLNNWIC 777
Cdd:cd03602    80 GQGDCATMYSSG--RWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 55.86 E-value: 6.02e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  375 RIHR------EEKKIQKYALQACRKEGGDLASIHSIEEFDFI--FSQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFT 446
Cdd:cd03596     6 KIHKkcylvsEETKHYHEASEDCIARGGTLATPRDSDENDALrdYVKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYF 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 341940970  447 KW---LPGEPshENNRQEDCVVMKG-KDGYWADRACEQPLGYIC 486
Cdd:cd03596    86 NWereITAQP--DGGKRENCVALSSsAQGKWFDEDCRREKPYVC 127

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 55.51 E-value: 6.31e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1104 SSYSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAFAWMKMhPFNVPIWIALNSNLTNNEYTWTDRWRVRYTNWGADEP 1183
Cdd:cd03603     1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNF-GGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEP 79

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467338 [Multi-domain] Cd Length: 121 Bit Score: 55.14 E-value: 7.91e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   24 QFLIYNED-----HKRCVDALSAISVQTATCnpEAESQKFRWV---SDSQIMSVAFKLCLGVPSKTDwaSVTLYACDSKS 95
Cdd:cd23460    38 QFWMYTGDgqirqDHLCLTADEGNKVTLREC--ADQLPSQEWSydeKTGTIRHRSTGLCLTLDANND--VVILKECDSNS 113


                  ....*
gi 341940970   96 EYQKW 100
Cdd:cd23460   114 LWQKW 118

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 55.67 E-value: 1.03e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  944 CKEGwhlYKNKCFKIFGFANEEKK-SWQDARQACKGLKGNLVSIENAQEQAFV---TYHMRDSTFNAWTGL--------N 1011
Cdd:cd03595     4 CRRG---TEKPCYKIAYFQDSRRRlNFEEARQACREDGGELLSIESENEQKLIerfIQTLRASDGDFWIGLrrssqynvT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940970 1012 DINAEHMFLWTAGQGVHYTNWGKGYPggrrsSLSYEdaDCVVVIGGNSREAG-------TWMDDTCDSKQGYICQ 1079
Cdd:cd03595    81 SSACSSLYYWLDGSISTFRNWYVDEP-----SCGSE--VCVVMYHQPSAPAGqggpylfQWNDDNCNMKNNFICK 148

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 54.07 E-value: 1.86e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    23 RQFLIYNEDHKRCVDALSAIS----VQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWASVTLYACDSKSEYQ 98
Cdd:pfam00652    1 ATGRIRNRASGKCLDVPGGSSaggpVGLYPCHGSNGNQLWTLTGDGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQ 80


                   ....*...
gi 341940970    99 KWECKNDT 106
Cdd:pfam00652   81 RWRYDEDG 88

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.

Pssm-ID: 153071 Cd Length: 119 Bit Score: 53.69 E-value: 2.09e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  679 FCKAIGGELASIKSKDEQQVIWRLITSSGSYHElFWLGLTYGSPSEG-FTWSDGS--PVSYENWAYGEPNNYQNVEYCGE 755
Cdd:cd03601    18 FCRSRGMRLASLAMRDSEMRDAILAFTLVKGHG-YWVGADNLQDGEYdFLWNDGVslPTDSDLWAPNEPSNPQSRQLCVQ 96

                          90       100
                  ....*....|....*....|....
gi 341940970  756 LKGDPGMsWNDINCEHLNNWICQI 779
Cdd:cd03601    97 LWSKYNL-LDDEYCGRAKRVICEK 119

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 54.29 E-value: 2.29e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1101 YGKSSYSLMKLKLPWHEAETYCKDHTSL-----LASILDPYSNAFA---WMKMHPFNVP--IWIALNSNLTNNEYTWTDR 1170
Cdd:cd03589     8 FGGYCYRFFGDRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVydlFESSRGPDTPygLWIGLHDRTSEGPFEWTDG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 341940970 1171 WRVRYTNWGADEP---KLKSACVYM----DVDGYWRTSYCNESFYFLCK 1212
Cdd:cd03589    88 SPVDFTKWAGGQPdnyGGNEDCVQMwrrgDAGQSWNDMPCDAVFPYICK 136

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 53.58 E-value: 2.63e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1243 HCYYFeSSFTRSWGQASLECLRMGASLVSIETAAESSFLsyrVEPLKSKTNFWIGMFR-NVEGKWLWLNDNPVSFVNWKT 1321
Cdd:cd03603     1 HFYKF-VDGGMTWEAAQTLAESLGGHLVTINSAEENDWL---LSNFGGYGASWIGASDaATEGTWKWSDGEESTYTNWGS 76

                          90       100
                  ....*....|....*....|....*...
gi 341940970 1322 GDPS--GERNDCVV----LASSSGLWNN 1343
Cdd:cd03603    77 GEPHnnGGGNEDYAainhFPGISGKWND 104

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 54.36 E-value: 2.73e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  659 CFKLYakgkHEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYHE----LFWLGL--------TYGSPSEGF 726
Cdd:cd03600     6 CYTLH----PQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRHGrgslRLWIGLqreprqcsDPSLPLRGF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  727 TW-SDGSPVSYENWAyGEPNNYQNVEYCGELKGDPGMS----WNDINCE-HLNNWICQIQ 780
Cdd:cd03600    82 SWvTGDQDTDFSNWL-QEPAGTCTSPRCVALSAAGSTPdnlkWKDGPCSaRADGYLCKFS 140

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 52.72 E-value: 5.11e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  228 ILYQIN----SKSALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSglWIGLNSLSVRSGWQWAGGSPFRylNW 303
Cdd:cd03593     6 ICYGNKcyyfSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWIDGSPLN--NL 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 341940970  304 LpGSPSSEPGKSCVSLNpgkNAKWENLECVQKLGYICKK 342
Cdd:cd03593    82 F-NIRGSTKSGNCAYLS---STGIYSEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 53.14 E-value: 5.21e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1097 GFVTYGKSSYSLMKLKLPWHEAETYCKDH--TSLLASILDPYSNAFA---WMKMHPFNVPIWIALNSNLTNNEYTWTDRW 1171
Cdd:cd03594     4 GWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIaslISSYQKAYQPVWIGLHDPQQSRGWEWSDGS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 341940970 1172 RVRYTNWGADEPKL-KSACVYM-DVDGY--WRTSYCNESFYFLCK 1212
Cdd:cd03594    84 KLDYRSWDRNPPYArGGYCAELsRSTGFlkWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 52.58 E-value: 6.65e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1115 WHEAETYCKDHTSLLASILDPYSNAFAWMKMHPFNvpiWIALNSNLTNNEYTWTDRWRVRYTNWGADEPK----LKSACV 1190
Cdd:cd03588    22 WEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDGHPLQFENWRPNQPDnffaTGEDCV 98

                          90       100
                  ....*....|....*....|....*
gi 341940970 1191 YM--DVDGYWRTSYCNESFYFLCKK 1213
Cdd:cd03588    99 VMiwHEEGEWNDVPCNYHLPFTCKK 123

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 52.39 E-value: 9.38e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  659 CFKLYakgkHEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYHELFWLGLTyGSPSEGfTWSD--GSPVSY 736
Cdd:cd03596    11 CYLVS----EETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNWEVWLGIN-DMVAEG-KWVDvnGSPISY 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 341940970  737 ENW---AYGEPNNYQNvEYCGELKGDPGMSWNDINCEHLNNWICQ 778
Cdd:cd03596    85 FNWereITAQPDGGKR-ENCVALSSSAQGKWFDEDCRREKPYVCE 128

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 51.66 E-value: 1.24e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  810 YQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWkyiNKNGGQSPYFIGM-LISMDKKFIWMDGSKVDFVAWATG 888
Cdd:cd03603     1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLL---SNFGGYGASWIGAsDAATEGTWKWSDGEESTYTNWGSG 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 341940970  889 EPnFANDDENCVTMYTN-----SGFWNDINCGYPNNF 920
Cdd:cd03603    78 EP-HNNGGGNEDYAAINhfpgiSGKWNDLANSYNTLG 113

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 51.18 E-value: 1.79e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  504 CRKGWKRHGFYCYLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVGlrpEKYFWTGLSDVQNKGTFRWtVDEQ 583
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG---SSSYWIGLSREKSEKPWKW-IDGS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 341940970  584 VqFTHWNAD-MPGRKAGCVAM-KTGVAGGlwdvlSCEEKAKFVCKH 627
Cdd:cd03593    77 P-LNNLFNIrGSTKSGNCAYLsSTGIYSE-----DCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.

Pssm-ID: 153071 Cd Length: 119 Bit Score: 51.00 E-value: 2.30e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940970  423 WIGLNDIKIQMY-FEWSDGT--PVTFTKWLPGEPSHENNRQeDCVVMKGKDGYWADRACEQPLGYICK 487
Cdd:cd03601    52 WVGADNLQDGEYdFLWNDGVslPTDSDLWAPNEPSNPQSRQ-LCVQLWSKYNLLDDEYCGRAKRVICE 118

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 48.99 E-value: 9.46e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  679 FCKAI-GGELASIKSKDEQQVIWRLitSSGSYHELFWLG--LTYGSPSEGFTWSDGSPVSYENWAYGEPNNyqNVEYCGE 755
Cdd:cd03598    19 ICRRCyRGNLASIHSFAFNYRVQRL--VSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYWAPGQPGN--RRGHCVE 94

                          90       100
                  ....*....|....*....|...
gi 341940970  756 LKGDPGMsWNDINCEHLNNWICQ 778
Cdd:cd03598    95 LCTRGGH-WRRAHCKLRRPFICS 116

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

Pssm-ID: 153067 Cd Length: 129 Bit Score: 49.12 E-value: 1.16e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940970  944 CKEGWHLYKNKCFKIfgfaNEEKKSWQDARQACKGLKGNLVSIENAQEQAFV-----TYHMRDSTFNAWTGLNDIN 1014
Cdd:cd03597     1 CGEGWHLVGNSCLKI----NTARESYDNAKLYCRNLNAVLASLTTQKKVEFVlkelqKHQMTKQKLTPWVGLRKIN 72

ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor (PLA2R1) and similar proteins; PLA2R1, also called PLA2-R, PLA2R, 180 kDa secretory phospholipase A2 receptor, C-type lectin domain family 13 member C (CLEC13C), or M-type receptor, is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine production during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. PLA2R1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467788 Cd Length: 118 Bit Score: 48.97 E-value: 1.20e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   25 FLIYNEDHKRCVDALSAiSVQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWASVTLYACDSKSEYQKWECKN 104
Cdd:cd23410     4 FILESESLKKCISADKS-GLFLENCDQPSDSMLWKWVSRHRLFNLGSSMCLGLNLSYPQQPLGLFECDSTLRTLWWRCNG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 341940970  105 DTLFGIKGTELyfnygnrQEKNIKLYKGSGLWSRWKVYGTTDD 147
Cdd:cd23410    83 KMLIGADQYKL-------TAVGSKVVASRQSSHKWKPYGSQDE 118

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 52.78 E-value: 2.15e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   224 PLTGILYQINSK------SALTWHQARASCKQQ-NADLLSVTEIHEQMYLTG-LTSSLSSGLWIGL---NSLSVRSGWQW 292
Cdd:TIGR00864  319 PKDGEIFEENGHcfqivpEEAAWLDAQEQCLARaGAALAIVDNDALQNFLARkVTHSLDRGVWIGFsdvNGAEKGPAHQG 398

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940970   293 AGGSPFRYLNWLPGSPSSEPGKSCVSLNPgknAKWENLE-CVQKLGYICKkgnntLNPFI-IPSASDVPTGCP 363
Cdd:TIGR00864  399 EAFEAEECEEGLAGEPHPARAEHCVRLDP---RGQCNSDlCNAPHAYVCE-----LNPGGpVPDAENFAMGAA 463

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 48.73 E-value: 2.48e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  222 KDPLTGILYQINSKSALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSL--SSG-LWIGL--------NSLSVRSGW 290
Cdd:cd03595     9 EKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLraSDGdFWIGLrrssqynvTSSACSSLY 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940970  291 QWAGGSPFRYLNWLPGSPSSePGKSCV------SLNPGKNA----KWENLECVQKLGYICK 341
Cdd:cd03595    89 YWLDGSISTFRNWYVDEPSC-GSEVCVvmyhqpSAPAGQGGpylfQWNDDNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 48.58 E-value: 2.56e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  238 LTWHQARASCKQQNADLLSV--TEIHE--QMYLTGLTSSLSSG---LWIGLN------SLSVR--SGWQW-AGGSPFRYL 301
Cdd:cd03600    14 LTFLEAQRSCIELGGNLATVrsGEEADvvSLLLAAGPGRHGRGslrLWIGLQreprqcSDPSLplRGFSWvTGDQDTDFS 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 341940970  302 NWLPGSPSSEPGKSCVSLNP----GKNAKWENLECVQKL-GYICK 341
Cdd:cd03600    94 NWLQEPAGTCTSPRCVALSAagstPDNLKWKDGPCSARAdGYLCK 138

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 47.81 E-value: 4.46e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  373 CYRIHREEKKIQKyALQACRKEGGDLASIHSIEEFDFI---FSQLGYEPND---ELWIGLNDIKIQMY--------FEWS 438
Cdd:cd03600     6 CYTLHPQKLTFLE-AQRSCIELGGNLATVRSGEEADVVsllLAAGPGRHGRgslRLWIGLQREPRQCSdpslplrgFSWV 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940970  439 DGTPVT-FTKWLpgEPSHENNRQEDCVVM-----KGKDGYWADRACEQPL-GYICK 487
Cdd:cd03600    85 TGDQDTdFSNWL--QEPAGTCTSPRCVALsaagsTPDNLKWKDGPCSARAdGYLCK 138

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 46.98 E-value: 4.80e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1105 SYSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAFAWMKMHPFNVPI-WIALNSNltNNEYTW--TDRWRVRYTNWGAD 1181
Cdd:cd03592     2 TYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDI--NNEGTWvdTDKKELEYKNWAPG 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 341940970 1182 EP--KLKSACV--YMDVDGYWRTSYCNESFYFLC 1211
Cdd:cd03592    80 EPnnGRNENCLeiYIKDNGKWNDEPCSKKKSAIC 113

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 50.85 E-value: 7.80e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   362 CPN--QWWPYAGHCYRIHREEKKIQKYALQACRKEGGDLASIHSIEEFDFIFSQLGYEPNDELWIGLNDIKI--QMYFEW 437
Cdd:TIGR00864  318 CPKdgEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDVNGaeKGPAHQ 397

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 341940970   438 SDGTPV-TFTKWLPGEPSHEnnRQEDCVVMkGKDGYWADRACEQPLGYICKMVSQ 491
Cdd:TIGR00864  398 GEAFEAeECEEGLAGEPHPA--RAEHCVRL-DPRGQCNSDLCNAPHAYVCELNPG 449

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. Ly-75 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467789 Cd Length: 116 Bit Score: 46.27 E-value: 8.29e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   25 FLIYNEDHKRCVDALSAIsVQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWASVTLYACDSKSEYQKWECKN 104
Cdd:cd23411     5 FTIQHENSGKCLKVENSQ-ISAVDCKQSSESLQWKWVSEHRLFNLGSKQCLGLDITKPSNTLKMFECDSKSVMLWWRCEG 83

                          90
                  ....*....|....*.
gi 341940970  105 DTLFGIKGTELYFNYG 120
Cdd:cd23411    84 GSLYGASQYRLAVKNG 99

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 45.99 E-value: 1.37e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970    21 DARQFLIYNEDH-------KRCVDALSA---ISVQTATCNPEAESQKFRWVSD-SQIMSVAFKLCLGV-PSKTDWASVTL 88
Cdd:pfam00652   35 NGNQLWTLTGDGtirsvasDLCLDVGSTadgAKVVLWPCHPGNGNQRWRYDEDgTQIRNPQSGKCLDVsGAGTSNGKVIL 114

                           90
                   ....*....|..
gi 341940970    89 YACDSKSEYQKW 100
Cdd:pfam00652  115 WTCDSGNPNQQW 126

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 46.27 E-value: 1.63e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  953 NKCFKIFgfanEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTF-------NAWTGLN--------DINAEH 1017
Cdd:cd03600     4 DACYTLH----PQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGrhgrgslRLWIGLQreprqcsdPSLPLR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940970 1018 MFLWTAG-QGVHYTNWGKGYPGGRRSSLsyedadCVVV--IGGNSREAGtWMDDTCDSK-QGYICQ 1079
Cdd:cd03600    80 GFSWVTGdQDTDFSNWLQEPAGTCTSPR------CVALsaAGSTPDNLK-WKDGPCSARaDGYLCK 138

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

Pssm-ID: 153067 Cd Length: 129 Bit Score: 45.65 E-value: 1.79e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  362 CPNQWWPYAGHCYRIHREEKKIQKYALqACRKEGGDLASIHSIEEFDFIFSQLGYEPNDEL----WIGLNDIKIQmYFEW 437
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKL-YCRNLNAVLASLTTQKKVEFVLKELQKHQMTKQkltpWVGLRKINVS-YWCW 78

                          90
                  ....*....|....*....
gi 341940970  438 SDGTPVTFT--KWLPGEPS 454
Cdd:cd03597    79 EDMSPFTNTtlQWLPGEPS 97

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 45.06 E-value: 1.82e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  964 EEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTFNAWTGLNDINAEhmFLWTAGQGVHYTNWGKGYPGGrrss 1043
Cdd:cd03602     7 NESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDS--WRWSDGSESSFRNWNTFQPFG---- 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 341940970 1044 lsyeDADCVVViggnsREAGTWMDDTCDSKQGYIC 1078
Cdd:cd03602    81 ----QGDCATM-----YSSGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 44.36 E-value: 3.87e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  235 KSALTWHQARASCKQ-QNADLLSVTEIHEQMYLTGLTSSLSSG-LWIGlnslSVRSGW------QWAGGSPFRYLNWLPG 306
Cdd:cd03598     8 KSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAqVWIG----GIITGKgrcrrfSWVDGSVWNYAYWAPG 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 341940970  307 SPSSEPGkSCVSLNPgKNAKWENLECVQKLGYIC 340
Cdd:cd03598    84 QPGNRRG-HCVELCT-RGGHWRRAHCKLRRPFIC 115

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 44.30 E-value: 5.21e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  239 TWHQARASCKQQNADLLSVTEIHEQMYLTG-LTSSLSSG--LWIGLNSLSVRSGWQWAGGSPFRYLNW---LPGSPSSEP 312
Cdd:cd03596    20 HYHEASEDCIARGGTLATPRDSDENDALRDyVKASVPGNweVWLGINDMVAEGKWVDVNGSPISYFNWereITAQPDGGK 99

                          90       100
                  ....*....|....*....|....*...
gi 341940970  313 GKSCVSLNPGKNAKWENLECVQKLGYIC 340
Cdd:cd03596   100 RENCVALSSSAQGKWFDEDCRREKPYVC 127

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.

Pssm-ID: 153071 Cd Length: 119 Bit Score: 43.68 E-value: 7.29e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940970 1293 NFWIGM--FRNVEGKWLWLNDN--PVSFVNWKTGDPSG--ERNDCVVLASSSGLWNNIHCSSYKGFICK 1355
Cdd:cd03601    50 GYWVGAdnLQDGEYDFLWNDGVslPTDSDLWAPNEPSNpqSRQLCVQLWSKYNLLDDEYCGRAKRVICE 118

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 43.44 E-value: 7.34e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  524 TFTDANHTCTNEKAYLTTVEDRYEQAFLTSLV--GLRpekYFWTGLSDVQNKGTFRWTVDEQVQFTHWNADMPGRKAG-- 599
Cdd:cd03591    12 NFDDAQKLCSEAGGTLAMPRNAAENAAIASYVkkGNT---YAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNAGGge 88

                          90       100
                  ....*....|....*....|....*..
gi 341940970  600 -CVAMktgVAGGLWDVLSCEEKAKFVC 625
Cdd:cd03591    89 dCVEM---YTSGKWNDVACNLTRLFVC 112

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 45.11 E-value: 1.13e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1229 CPEseqtAWIPFYGHCYYFeSSFTRSWGQASLECLRMGASLVSIETAAESSFLsyrvEPLKSKTNFWIGMFRNVEGK-WL 1307
Cdd:PHA02642   88 CPK----GWIGFGYKCFYF-SEDSKNWTFGNTFCTSLGATLVKVETEEELNFL----KRYKDSSDHWIGLNRESSNHpWK 158

                          90
                  ....*....|....*...
gi 341940970 1308 WLNDNP--VSFVNWKTGD 1323
Cdd:PHA02642  159 WADNSNynASFVITGTGE 176

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 42.76 E-value: 1.67e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  812 YYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKN-GGQSPYFIGML-ISMDKKFIWMDGSKVDFVAW---A 886
Cdd:cd03596    12 YLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASvPGNWEVWLGINdMVAEGKWVDVNGSPISYFNWereI 91

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 341940970  887 TGEPNfANDDENCVTMYTNS-GFWNDINCGYPNNFICQ 923
Cdd:cd03596    92 TAQPD-GGKRENCVALSSSAqGKWFDEDCRREKPYVCE 128

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 42.68 E-value: 1.82e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970 1101 YGKSSYSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAFAWMKMhPFNVPIWIALNSNLTNNEYTWTDR--WRVRYTNW 1178
Cdd:cd03590     8 FQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIL-SGNRSYWIGLSDEETEGEWKWVDGtpLNSSKTFW 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 341940970 1179 GADEP----KLKSACVYMD-VDGYWRTSYCNESFYFLCKK 1213
Cdd:cd03590    87 HPGEPnnwgGGGEDCAELVyDSGGWNDVPCNLEYRWICEK 126

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 42.95 E-value: 2.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  504 CRKGWKRHgfyCYLIG-----STLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLV-GLRP-EKYFWTGLSDVQNKGT- 575
Cdd:cd03595     4 CRRGTEKP---CYKIAyfqdsRRRLNFEEARQACREDGGELLSIESENEQKLIERFIqTLRAsDGDFWIGLRRSSQYNVt 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  576 -------FRWTVDEQVQFTHWNADMP--GRKAgCVAM------KTGVAGGL---WDVLSCEEKAKFVCKH 627
Cdd:cd03595    81 ssacsslYYWLDGSISTFRNWYVDEPscGSEV-CVVMyhqpsaPAGQGGPYlfqWNDDNCNMKNNFICKY 149

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467311 [Multi-domain] Cd Length: 127 Bit Score: 41.91 E-value: 3.14e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940970   35 CVDALSAIS-VQTATCNPEAESQKFRWVSDS-QIMSVAFKLCLGVPSKTDWASVTLYACDsKSEYQKWECKN 104
Cdd:cd23433    57 CLDASRKGGpVKLEKCHGMGGNQEWEYDKETkQIRHVNSGLCLTAPNEDDPNEPVLRPCD-GGPSQKWELEG 127

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 41.59 E-value: 3.39e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  516 YLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVGLRPEkYFWTGLSDVQnkGTFRWTVDEQVQFTHWNADMPG 595
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNS-AAWIGLYRDV--DSWRWSDGSESSFRNWNTFQPF 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 341940970  596 RKAGCVAMKTgvaGGLWDVLSCEEKAKFVC 625
Cdd:cd03602    80 GQGDCATMYS---SGRWYAALCSALKPFIC 106

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.

Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 41.65 E-value: 4.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   23 RQFLIYNEDHKRCVDALSAISVQTATCNPeAESQKFRWVSDS----QIMSVAFKLCLGVpskTDWASVTLYACDSkSEYQ 98
Cdd:cd23415     1 GTVRLRNVATGRCLDSNAGGNVYTGPCNG-GPYQRWTWSGVGdgtvTLRNAATGRCLDS---NGNGGVYTLPCNG-GSYQ 75


                  ...
gi 341940970   99 KWE 101
Cdd:cd23415    76 RWR 78

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 43.92 E-value: 1.16e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   643 EPKCPENWGTTSKTSMCFKLYAkgkhEKKTWFESRDFCKA-IGGELASIKSKDEQQVIWRLITSsgSYHELFWLGLT--Y 719
Cdd:TIGR00864  315 HPHCPKDGEIFEENGHCFQIVP----EEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTH--SLDRGVWIGFSdvN 388

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940970   720 GSPSEGFTWSDGSPV-SYENWAYGEPnNYQNVEYCGELkgDPGMSWNDINCEHLNNWICQIQKG 782
Cdd:TIGR00864  389 GAEKGPAHQGEAFEAeECEEGLAGEP-HPARAEHCVRL--DPRGQCNSDLCNAPHAYVCELNPG 449

C-type lectin-like protein; Provisional

Pssm-ID: 222982 [Multi-domain] Cd Length: 157 Bit Score: 41.00 E-value: 1.19e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  362 CPNQWWPYAGHCYRIhREEKKIQKYALQACRKEGGDLASIHSIEEFDFIFSQLGyepNDELWIGLNdikiqmyfewsdgt 441
Cdd:PHA03097   46 CRSGWVGYNNKCYTF-SENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKG---GQDLWIGIE-------------- 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 341940970  442 pvTFTKWLPGEPSHENNRQ----EDCVVMKGKDgyWADRACEQPLGYIC 486
Cdd:PHA03097  108 --KKKGDDDDREVLDKVVKppksGKCAYLKDKT--IISSNCNATKGWIC 152

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

Pssm-ID: 153067 Cd Length: 129 Bit Score: 40.26 E-value: 1.62e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  231 QINSkSALTWHQARASCKQQNADLLSVT----------EIHE-QMYLTGLTSslssglWIGLNSLSVrSGWQWAGGSPF- 298
Cdd:cd03597    14 KINT-ARESYDNAKLYCRNLNAVLASLTtqkkvefvlkELQKhQMTKQKLTP------WVGLRKINV-SYWCWEDMSPFt 85

                          90
                  ....*....|..
gi 341940970  299 -RYLNWLPGSPS 309
Cdd:cd03597    86 nTTLQWLPGEPS 97

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467312 [Multi-domain] Cd Length: 121 Bit Score: 40.00 E-value: 1.69e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940970   34 RCVDALSAI---SVQTATCNPEAESQKFRWVSDSQIMSVafKLCLGVPSKTDWASVTLYACDSKSEYQKWE 101
Cdd:cd23434    10 LCLDTLGHKaggTVGLYPCHGTGGNQEWSFTKDGQIKHD--DLCLTVVDRAPGSLVTLQPCREDDSNQKWE 78

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 39.74 E-value: 1.80e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  515 CYLIGSTLSTFTDANHTCTN-EKAYLTTVEDRYEQAFLTSLVGLRPEKYFWTGLSdVQNKG---TFRWTVDEQVQFTHWN 590
Cdd:cd03598     3 CYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGI-ITGKGrcrRFSWVDGSVWNYAYWA 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 341940970  591 ADMPGRKAG-CVAMKTgvAGGLWDVLSCEEKAKFVCKH 627
Cdd:cd03598    82 PGQPGNRRGhCVELCT--RGGHWRRAHCKLRRPFICSY 117

ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a putative sugar-binding pocket.

Pssm-ID: 467301 [Multi-domain] Cd Length: 119 Bit Score: 39.67 E-value: 2.16e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   13 IPVSVQLLDarqfliyneDHKRCVDALSAISVQTATCNPEAESQKFRWVSDSQIMSVAF-KLCLGVpskTDWASVTLYAC 91
Cdd:cd23423     3 RPVNLQSLS---------FNNRCLTVDNNGRVTLESCDSGDRNQSWILDSEGRYRSRVApDLCLDA---DDDGLLTLEQC 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940970   92 DSkSEYQKWECKNDTLF-GIKGTELYFNYGNRQEKNIKLYKGSGLWSRWK 140
Cdd:cd23423    71 SL-SLTQKWEWEGDRLKnRYLDTGWVLTHDAQGGLKLVPDSSEGNQTRWR 119

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 39.33 E-value: 2.27e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  230 YQInSKSALTWHQARASCKQQNADLLSVTEIHEQMYLtGLTSSLSSGLWIGLNSLSVRSGWQWAGGSPFRYLNWLPGSPS 309
Cdd:cd03603     3 YKF-VDGGMTWEAAQTLAESLGGHLVTINSAEENDWL-LSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80


                  ....
gi 341940970  310 SEPG 313
Cdd:cd03603    81 NNGG 84

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467315 [Multi-domain] Cd Length: 124 Bit Score: 39.20 E-value: 2.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   18 QL--LDARQFLIYNEdhkRCVDALSAIS-VQTATCNpEAESQKFRW-VSDSQIMSVAFKLCLGVPSKTDwaSVTLYACDS 93
Cdd:cd23437    40 QLfrLNEAGQLAVGE---QCLTASGSGGkVKLRKCN-LGETGKWEYdEATGQIRHKGTGKCLDLNEGTN--KLILQPCDS 113

                          90
                  ....*....|.
gi 341940970   94 KSEYQKWECKN 104
Cdd:cd23437   114 SSPSQKWEFNE 124

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 39.64 E-value: 2.73e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940970   44 VQTATCNPEAEsQKFRWVSDSQIMSVAFKLCLGVP--SKTDWASVTLYACDSKSEyQKW 100
Cdd:cd23418    72 VVIWPCNGGAN-QKWRFNSDGTIRNVNSGLCLDVAggGTANGTRLILWSCNGGSN-QRW 128

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 39.24 E-value: 3.17e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940970   34 RCVDALSAIS-----VQTATCNPEAeSQKFRWVSDSQIMSVAFKLCLGVP--SKTDWASVTLYACDSkSEYQKW 100
Cdd:cd23451    53 KCLDVSGGGTangtlVQLWDCNGTG-AQKWVPRADGTLYNPQSGKCLDAPggSTTDGTQLQLYTCNG-TAAQQW 124

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 38.59 E-value: 4.59e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970  953 NKCFKIFGFANeekkSWQDARQACKGL-KGNLVSIENaqeQAFvtyHMR----DSTFN---AWTG--LNDINAEHMFLWT 1022
Cdd:cd03598     1 GRCYRFVKSPR----TFRDAQVICRRCyRGNLASIHS---FAF---NYRvqrlVSTLNqaqVWIGgiITGKGRCRRFSWV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940970 1023 AGQGVHYTNWGKGYPGGRRSSlsyedadCVVViggnSREAGTWMDDTCDSKQGYICQ 1079
Cdd:cd03598    71 DGSVWNYAYWAPGQPGNRRGH-------CVEL----CTRGGHWRRAHCKLRRPFICS 116

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e and similar proteins; PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, R-PTP-beta, vascular endothelial protein tyrosine phosphatase, or VE-PTP, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells, which requires the presence of plakoglobin. The subfamily corresponds to PTPRB isoform e, which contains an extra ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467787 Cd Length: 117 Bit Score: 38.19 E-value: 6.19e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940970   25 FLIYNEDHKRCVDALSAISVqtATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWAS--VTLYACdskSEYQKWEC 102
Cdd:cd23409     4 FLILHVQKQQCLFGNKTVSV--GKCNATSPNQQWQWTEDGKLLHVKSGQCLGISNSSAFHSrrAILLDC---SQAPRWTC 78

                          90
                  ....*....|....*
gi 341940970  103 -KNDTLFGIKGTELY 116
Cdd:cd23409    79 hENEGLLEVANSSLF 93