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 209977023 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLgrlettnevidSDFETRNFWIGLTYKTAKDSFRWATGEH 389
Cdd:cd00037    2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-----------KKSSSSDVWIGLNDLSSEGTWKWSDGSP 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 209977023 390 QA-FTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd00037   71 LVdYTNWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLgrlettnevidSDFETRNFWIGLTYKTAKDSFRWATGEH 389
Cdd:cd00037    2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-----------KKSSSSDVWIGLNDLSSEGTWKWSDGSP 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 209977023 390 QA-FTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd00037   71 LVdYTNWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

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 209977023   310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILafylgrlettNEVIDSDFETRNFWIGLTYKTAKDSFRWATG-E 388
Cdd:smart00034  12 CYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFV----------ASLLKNSGSSDYYWIGLSDPDSNGSWQWSDGsG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 209977023   389 HQAFTSFAFGQPDNHGfGNCVELQASAAFnWNDQRCKTRNRYICQ 433
Cdd:smart00034  82 PVSYSNWAPGEPNNSS-GDCVVLSTSGGK-WNDVSCTSKLPFVCE 124

SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein represent functional links between plant defense systems and human immune system. This family has no known function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023    51 LLSLHNRLRS------WVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPagLVSFVEVV 124
Cdd:smart00198   6 ILDAHNKLRSqvaggfLAAPAASNMLKLTWDCELASSAQNWANQCPFGHSTPRPGYGENLAWWSSSTALP--DTYASAAV 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209977023   125 SLWFAEGQRYSHAAGECA-RNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSP 184
Cdd:smart00198  84 QLWYDEFQDYGYSSNTCKdTNGKIGHYTQVVWAKTYKVGCGVANCPDGTKKKTVVVCNYDP 144

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 209977023 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLgrlettnevidSDFETRNFWIGLTYKTAKDSFRWATGEH 389
Cdd:cd00037    2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-----------KKSSSSDVWIGLNDLSSEGTWKWSDGSP 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 209977023 390 QA-FTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd00037   71 LVdYTNWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of glioma pathogenesis-related protein 1 and similar proteins; Glioma pathogenesis-related protein 1 (GLIPR1) is also called related to testes-specific, vespid, and pathogenesis protein 1 (RTVP-1). The GLIPR1 gene has been identified as a p53 target gene and was shown to be methylated and down-regulated in prostate cancer. It is a novel broad-spectrum tumor suppressor whose proapoptotic properties are exerted in part through ROS-JNK signaling. GLIPR1 is composed of a signal peptide that directs its secretion, a CAP domain, and a transmembrane domain. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023  52 LSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC-GTPTPSL--ASGLWRTLQ-VGWNMQLLPAGLVSFVEVVSLW 127
Cdd:cd05385    7 VRIHNELRSKVSPPAANMRYMSWDKALAKTARAWARKCkFSHNICLkePGKCHPNFTtLGENIWLGSIFSFSVESAITSW 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209977023 128 FAEGQRYSHAAGECARnaTCTHYTQLVWATSSQLGCGRHLCSAG-------QAAIeaFVCAYSPRG 186
Cdd:cd05385   87 YNEVKDYNFKTNSCSR--VCGHYTQVVWADSYKVGCAVHVCPNGggffsgsSSAI--FVCNYGPAG 148

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory proteins; Cysteine-rich secretory proteins (CRISPs) are two-domain proteins with an evolutionary diverse and structurally conserved N-terminal CAP domain and a C-terminal cysteine-rich domain, which is comprised of a hinge and an ICR (ion channel regulator) region. CRISPs are involved in response to pathogens, fertilization, and sperm maturation. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. CRISP-1 has been shown to mediate gamete fusion by binding to the egg surface. Other members of the CRISP family secreted in the testis (CRISP2), epididymis (CRISP3-4), or during ejaculation (CRISP3), are also involved in sperm-egg interaction, supporting the existence of a functional redundancy and cooperation between homolog proteins ensuring the success of fertilization. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1) and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023  44 NRKEsflLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCgTPTPSLASGLWRT-LQVGWNMqLLPAGLVSFVE 122
Cdd:cd05383    2 VQQE---IVDLHNALRRSVNPPASNMLKMSWNPEAAENAQRWANRC-NFTHSPPNGRTIPgIRCGENI-FMSSYPASWSE 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977023 123 VVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSP 184
Cdd:cd05383   77 VIQAWYDEYKDFKYGVGAKPPGSVTGHYTQVVWYSSYLVGCAVAYCPSQGSLKYFYVCQYCP 138

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogenesis-related protein 1 (PR-1) family proteins; Members of pathogenesis-related protein 1 (PR-1) family are among the most abundantly produced proteins in plants on pathogen attack. They are considered hallmarks of hypersensitive response/defense pathways and may act as anti-fungal agents or be involved in cell wall loosening.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 107 GWNMQLLPAGLVSFVEVVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIeaFVCAYSPRG 186
Cdd:cd05381   51 GENLFWGSGDNWSPADAVKSWVDEKPYYDYASNTCVGGKMCGHYTQVVWRNSTRLGCARVVCDNNGGTF--VICNYDPPG 128

                 ...
gi 209977023 187 NWE 189
Cdd:cd05381  129 NYI 131

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor R3HDML; Peptidase inhibitor R3HDML, also called cysteine-rich secretory protein R3HDML, is a putative serine protease inhibitor. The R3HDML gene may be associated with clinical dimensions of schizophrenia. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023  50 LLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCgtptpSLASGLWRTLQ-VGWNMQLLPAGLVSFVEVVSLWF 128
Cdd:cd18815    3 ALLDYHNRVRSQVFPPAANMEYMVWDERLAKSAEAWAAQC-----VWEHGPPQLMRyIGQNLSIHSGRYRSIVDLVKSWY 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 209977023 129 AEGQRYSHAAG-EC-------ARNATCTHYTQLVWATSSQLGCGRHLCS 169
Cdd:cd18815   78 DERQHYSFPHPrECnprcpskCSGAVCSHYTQMVWASSNRIGCAVHTCS 126

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 304 LRIDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNevidsdfetRNFWIGLTYKTAKDSFR 383
Cdd:cd03596    5 TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGN---------WEVWLGINDMVAEGKWV 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 209977023 384 WATGehQAFTSFAF-----GQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd03596   76 DVNG--SPISYFNWereitAQPDGGKRENCVALSSSAQGKWFDEDCRREKPYVCEF 129

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15 and similar proteins; This family is composed of peptidase inhibitor 15 (PI15), peptidase inhibitor R3HDML, cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1), and cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2). PI15 is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. R3HDML is a putative serine protease inhibitor, whose gene may be associated with clinical dimensions of schizophrenia. CRISPLD1 may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. plays a role in the etiology of NSCLP and is required for neural crest cell migration and cell viability during craniofacial development. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023  51 LLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC---GTPTPSLASglwrtlqVGWNMQLLPAGLVSFVEVVSLW 127
Cdd:cd18812    4 ILDYHNKLRGQVYPPAANMEYMVWDKELARSAEAWATQCiweHGPSSLLRS-------IGQNLSAHWGRYRSPVFLVKSW 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 128 FAEGQRYSHAA-GEC-------ARNATCTHYTQLVWATSSQLGCGRHLCSA----GQAAIEA--FVCAYS 183
Cdd:cd18812   77 YDEVKDYLFPYpRDCnphcpwrCSGPMCTHYTQMVWATSNRIGCAIHTCSNmnvwGNVWHRAvyLVCNYA 146

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 2; Cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2) is also called cysteine-rich secretory protein 11 (CRSIP-11), LCCL domain-containing cysteine-rich secretory protein 2 (LCRISP2), or CAP and LCCL domain containing protein 2 (CAPLD2). It plays a role in the etiology of NSCLP (non-syndromic cleft lip with or without cleft palate). It is required for neural crest cell migration and cell viability during craniofacial development. The CRISPLD2 gene has been identified a glucocorticoid responsive gene that modulates cytokine function in airway smooth muscle cells. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023  51 LLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC---GTPTPSLASgLWRTLQVGWNMQLLPAGLVSfvevvsLW 127
Cdd:cd18816    4 ILQLHNKLRGQVYPSASNMEYMTWDDELERSAEAWAQQCiweHGPTSLLPS-IGQNLAVHWGRYRSPAFHVQ------SW 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 128 FAEGQRYSHA-AGEC-------ARNATCTHYTQLVWATSSQLGCGRHLCSA----GQAAIEA--FVCAYS 183
Cdd:cd18816   77 YDEVKDYTYPyPHECnpwcperCSGPMCTHYTQIVWATTNKVGCAVNVCRRmnvwGEIWENAvyLVCNYS 146

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 1; Cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1) is also called cysteine-rich secretory protein 10 (CRISP-10), CocoaCrisp, LCCL domain-containing cysteine-rich secretory protein 1 (LCRISP1), or CAP and LCCL domain containing protein 1 (CAPLD1). CRISPLD1 is clearly distinct from CRISPs because they do not contain the 10 absolutely conserved cysteines or the ICR (ion channel regulator) domain of the CRISPs. It may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023  50 LLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC--GTPTPSLASGLWRTLQVGWNMQLLPAGLVSfvevvsLW 127
Cdd:cd18813    3 LILDLHNKLRGQVYPPASNMEYMTWDVELERSAEAWAETClwEHGPAHLLPSIGQNLGAHWGRYRPPTFHVQ------AW 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 128 FAEGQRYSHA-AGEC-------ARNATCTHYTQLVWATSSQLGCGRHLCSA----GQAAIEA--FVCAYS 183
Cdd:cd18813   77 YDEVRDFSYPyPQECnpycpfrCSGPVCTHYTQVVWATSNRIGCAINLCHNmnvwGQIWPKAiyLVCNYS 146

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15; Peptidase inhibitor 15 (PI15) is also called 25 kDa trypsin inhibitor (p25TI), cysteine-rich secretory protein 8 (CRISP-8), or SugarCrisp. It is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. PI15 may also participate in the regulation of drug resistance in ovarian cancer and serve as a potential target in targeted therapies. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023  51 LLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC-GTPTPSLasgLWRTLqvGWNMQLLPAGLVSFVEVVSLWFA 129
Cdd:cd18814    4 ILDYHNQVRGKVFPPAANMEYMVWDENLAKSAEAWAATCiWDHGPSY---LLRFL--GQNLSVRTGRYRSILQLVKPWYD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 209977023 130 EGQRYSHA-AGEC-------ARNATCTHYTQLVWATSSQLGCGRHLC 168
Cdd:cd18814   79 EVKDYAFPyPQDCnprcplrCYGPMCTHYTQMVWATSNRIGCAIHTC 125

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 311 FMVSSEADTYYRARMKCQRKGGVLAQIKSqkvqdilafylgrlETTNEVIDS---DFETRNFwIGLTYKTAKDSFRWATG 387
Cdd:cd03591    4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRN--------------AAENAAIASyvkKGNTYAF-IGITDLETEGQFVYLDG 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 209977023 388 EHQAFTSFAFGQPDNHGFG-NCVELQASAafNWNDQRCKTRNRYICQF 434
Cdd:cd03591   69 GPLTYTNWKPGEPNNAGGGeDCVEMYTSG--KWNDVACNLTRLFVCEF 114

Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organizms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilization. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how Swiss:Q91055 blocks the Ca++ transporting ryanodine receptors.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023   52 LSLHNRLRswvqpPAADMRRLDWSDS------LAQLAQARAALCGTPTPSLASGLWRTLQVGWNmqLLPAGLVSFVEVVS 125
Cdd:pfam00188   1 LDLHNEYR-----AAAGLPPLSWDNElaaaaqDHAKYCADNGSHNHRSPYGGNIYARVVAAGYA--LGDAGPDSAEDAVD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 209977023  126 LWFAEGQRYShaagecarnatCTHYTQLVWATSSQLGCGRHLCSAGQaaIEAFVCAY 182
Cdd:pfam00188  74 GWYDSPGTYN-----------CGHRTNLLWPKSTKVGCAVAKCGDGG--TYYFVCNY 117

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 308 GDCFMVSSEADTYYRARMKCQR-KGGVLAQIKSQKVQDILAFYLGRLETTNevidsdfetrnFWIG--LTYKTAKDSFRW 384
Cdd:cd03598    1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQ-----------VWIGgiITGKGRCRRFSW 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 209977023 385 ATGEHQAFTSFAFGQPDNhGFGNCVELQASAAFnWNDQRCKTRNRYICQF 434
Cdd:cd03598   70 VDGSVWNYAYWAPGQPGN-RRGHCVELCTRGGH-WRRAHCKLRRPFICSY 117

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977023 306 IDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNEVIDsdfetRNFWIGLTYKTAKDS---- 381
Cdd:cd03600    2 VSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRHGRGS-----LRLWIGLQREPRQCSdpsl 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209977023 382 ----FRWATG-EHQAFTSFAFGQPDNHGFGNCVELQASAA----FNWNDQRCKTR-NRYICQFA 435
Cdd:cd03600   77 plrgFSWVTGdQDTDFSNWLQEPAGTCTSPRCVALSAAGStpdnLKWKDGPCSARaDGYLCKFS 140

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of Golgi-associated plant pathogenesis-related protein 1 and similar proteins; Golgi-associated plant pathogenesis related protein 1 (GAPR1), also called Golgi-associated PR-1 protein or glioma pathogenesis-related protein 2 (GLIPR-2), forms amyloid-like fibrils in the presence of liposomes containing acidic phospholipids. It has been identified in mice as an up-regulated protein in kidney fibrosis, and is involved in epithelial to mesenchymal transition and in generating a pool of myofibroblasts contributing to fibrosis. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209977023 122 EVVSLWFAEGQRY-------SHAAGecarnatctHYTQLVWATSSQLGCGRhlcsAGQAAIEAFVCA-YSPRGNW 188
Cdd:cd05382   71 EAVDSWYNEIKNYnfnkpgfQSGTG---------HFTQVVWKSSTELGVGV----AKSKDGCVYVVArYSPAGNV 132