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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    39 WTYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPK-NPTYYWIGIRKIGKTWTWVGTNKTLTkEAENWGTG 117
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKyNLGYYWIDGNDINNEGTWVDTDKKEL-EYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 400181   118 EPNNKKSkEDCVEIYIKrerDSGKWNDDACHKRKAALCYT 157
Cdd:cd03592  80 EPNNGRN-ENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115

EEV Host range protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    217 FSFQSQCAFNCSEGS-----ELLGNAKTECGASGNWTYLEPICQVIQCMpLAAPDLGTMECSHPLANFSFTSACTFTCSE 291
Cdd:PHA02817  42 YNIGSNVTFFCGNNTrgvryTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKP 120

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 400181    292 ETDLIGERKTVCRSSGSWSSPSPICQKTKRSFSKI 326
Cdd:PHA02817 121 GFVLIGTKYSVCGINSSWIPKVPICSRDNITYNKI 155

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    39 WTYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPK-NPTYYWIGIRKIGKTWTWVGTNKTLTkEAENWGTG 117
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKyNLGYYWIDGNDINNEGTWVDTDKKEL-EYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 400181   118 EPNNKKSkEDCVEIYIKrerDSGKWNDDACHKRKAALCYT 157
Cdd:cd03592  80 EPNNGRN-ENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181       33 HHGTHCwtYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPK--NPTYYWIGIRKIGKTWTWVGTNKTLTKE 110
Cdd:smart00034   7 SYGGKC--YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSDPDSNGSWQWSDGSGPVS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 400181      111 AENWGTGEPNNkkSKEDCVEIYikreRDSGKWNDDACHKRKAALC 155
Cdd:smart00034  85 YSNWAPGEPNN--SSGDCVVLS----TSGGKWNDVSCTSKLPFVC 123

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 400181      197 CEPLKAPELGTMNCIHplGDFSFQSQCAFNCSEGSELLGNAKTECGASGNWTYLEPIC 254
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

EEV Host range protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    217 FSFQSQCAFNCSEGS-----ELLGNAKTECGASGNWTYLEPICQVIQCMpLAAPDLGTMECSHPLANFSFTSACTFTCSE 291
Cdd:PHA02817  42 YNIGSNVTFFCGNNTrgvryTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKP 120

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 400181    292 ETDLIGERKTVCRSSGSWSSPSPICQKTKRSFSKI 326
Cdd:PHA02817 121 GFVLIGTKYSVCGINSSWIPKVPICSRDNITYNKI 155

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.

                          10        20
                  ....*....|....*....|..
gi 400181     165 CNRHGECVETINNNTCICDPGY 186
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPGY 22

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    39 WTYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPK-NPTYYWIGIRKIGKTWTWVGTNKTLTkEAENWGTG 117
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKyNLGYYWIDGNDINNEGTWVDTDKKEL-EYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 400181   118 EPNNKKSkEDCVEIYIKrerDSGKWNDDACHKRKAALCYT 157
Cdd:cd03592  80 EPNNGRN-ENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    39 WTYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPK-NPTYYWIGIRKIGKTWTWVGTNKTLTKEAENWGTG 117
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKsSSSDVWIGLNDLSSEGTWKWSDGSPLVDYTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 400181   118 EPNNKKSkEDCVEIYIkreRDSGKWNDDACHKRKAALCY 156
Cdd:cd00037  81 EPNPGGS-EDCVVLSS---SSDGKWNDVSCSSKLPFICE 115

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181       33 HHGTHCwtYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPK--NPTYYWIGIRKIGKTWTWVGTNKTLTKE 110
Cdd:smart00034   7 SYGGKC--YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSDPDSNGSWQWSDGSGPVS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 400181      111 AENWGTGEPNNkkSKEDCVEIYikreRDSGKWNDDACHKRKAALC 155
Cdd:smart00034  85 YSNWAPGEPNN--SSGDCVVLS----TSGGKWNDVSCTSKLPFVC 123

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    41 YHYSER-SMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPKNPTYYWIGIRKIGKTWTWV-GTNKTLTkeAENWGTGE 118
Cdd:cd03591   3 IFVTNGeEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVyLDGGPLT--YTNWKPGE 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 400181   119 PNNKKSKEDCVEIYikrerDSGKWNDDACHKRKAALC 155
Cdd:cd03591  81 PNNAGGGEDCVEMY-----TSGKWNDVACNLTRLFVC 112

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    33 HHGTHCwtYHYSERSMNWENARKFCK-----HNYTDLVAIQNKRE----IEYLEKTLPKNPTY-YWIGI--RKIGKTWTW 100
Cdd:cd03589   7 AFGGYC--YRFFGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEEndfvYDLFESSRGPDTPYgLWIGLhdRTSEGPFEW 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 400181   101 V-GTNKTLTKeaenWGTGEPNNKKSKEDCVEIYiKRERDSGKWNDDACHKRKAALC 155
Cdd:cd03589  85 TdGSPVDFTK----WAGGQPDNYGGNEDCVQMW-RRGDAGQSWNDMPCDAVFPYIC 135

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    40 TYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPKNpTYYWIGIRKIGKTWTWV---GTNKTLTkeaeNWGT 116
Cdd:cd03603   2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKwsdGEESTYT----NWGS 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 400181   117 GEP-NNKKSKEDCVEIYIKRErDSGKWNDDA 146
Cdd:cd03603  77 GEPhNNGGGNEDYAAINHFPG-ISGKWNDLA 106

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    37 HCWTYHYSERSmnWENARKFCKHNYTDLVAIQNKREIEYLEKtlpKNPTYYWIGI--RKIGKTWTWVGTNKTLTkeaENW 114
Cdd:cd03588  11 HCYRHFPDRET--WEDAERRCREQQGHLSSIVTPEEQEFVNN---NAQDYQWIGLndRTIEGDFRWSDGHPLQF---ENW 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 400181   115 GTGEPNNK-KSKEDCVeIYIKRERdsGKWNDDACH 148
Cdd:cd03588  83 RPNQPDNFfATGEDCV-VMIWHEE--GEWNDVPCN 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    34 HGTHCWTYHYSERSmnWENARKFCK--HNYTDLVAIQNKREI----EYLEKTLPKNpTYYWIGIR--KIGKTWTWVGTNK 105
Cdd:cd03594   8 YKGNCYGYFRQPLS--WSDAELFCQkyGPGAHLASIHSPAEAaaiaSLISSYQKAY-QPVWIGLHdpQQSRGWEWSDGSK 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 400181   106 TLTKeaeNWGTGEPNNkkSKEDCVEIyikrERDSG--KWNDDACHKRKAALC 155
Cdd:cd03594  85 LDYR---SWDRNPPYA--RGGYCAEL----SRSTGflKWNDANCEERNPFIC 127

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    41 YHYSERSMNWENARKFCKHNYTDLVAIQNKRE---IEYLEKTLPKNPTYYWIGIRKIGKTWTWVGTNKTLTKEAE----- 112
Cdd:cd03595  18 FQDSRRRLNFEEARQACREDGGELLSIESENEqklIERFIQTLRASDGDFWIGLRRSSQYNVTSSACSSLYYWLDgsist 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 400181   113 --NWGTGEPNNkkSKEDCVEIYIKRERDSG-------KWNDDACHKRKAALC 155
Cdd:cd03595  98 frNWYVDEPSC--GSEVCVVMYHQPSAPAGqggpylfQWNDDNCNMKNNFIC 147

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    214 LGDFSFQSQCAFNCSEGSELLGNAKTEC--GASGN--WTYLEPICQVIQCMplAAPDLGTMECSHPLANFSFTSACTFTC 289
Cdd:PHA02927  99 IGGVDFGSSITYSCNSGYQLIGESKSYCelGSTGSmvWNPEAPICESVKCQ--SPPSISNGRHNGYEDFYTDGSVVTYSC 176

                         90
                 ....*....|....
gi 400181    290 SEETDLIGERKTVC 303
Cdd:PHA02927 177 NSGYSLIGNSGVLC 190

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400181    49 NWENARKFCKHNYTDLVAIQNKREIEYLEKTLPKNPTYY-----WIGIRKIGKT-WTWVG----TNKTLtkeaeNWGTGE 118
Cdd:cd03597  21 SYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKqkltpWVGLRKINVSyWCWEDmspfTNTTL-----QWLPGE 95

                ...
gi 400181   119 PNN 121
Cdd:cd03597  96 PSD 98