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 26892293  35 SCYIFLQEAikvESIEDVRNQCTDHGADMISIHNEEENAFILDTLKKqwKGPDDILLGMFYDTDDASFKWFDNS-NMTFD 113
Cdd:cd00037   1 SCYKFSTEK---LTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWKWSDGSpLVDYT 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 26892293 114 KWTDQDDDEDLVDTCAFLHI-KTGEWKKGNCE 144
Cdd:cd00037  76 NWAPGEPNPGGSEDCVVLSSsSDGKWNDVSCS 107

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26892293   24 CPSStWIQFQDSCYIFlqeaikvesIEDVRNQ------CTDHGADMISIHNEEENAFIldtlkKQWKGPDDILLGMFYDT 97
Cdd:PHA02642  88 CPKG-WIGFGYKCFYF---------SEDSKNWtfgntfCTSLGATLVKVETEEELNFL-----KRYKDSSDHWIGLNRES 152

                         90
                 ....*....|..
gi 26892293   98 DDASFKWFDNSN 109
Cdd:PHA02642 153 SNHPWKWADNSN 164

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 26892293  35 SCYIFLQEAikvESIEDVRNQCTDHGADMISIHNEEENAFILDTLKKqwKGPDDILLGMFYDTDDASFKWFDNS-NMTFD 113
Cdd:cd00037   1 SCYKFSTEK---LTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWKWSDGSpLVDYT 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 26892293 114 KWTDQDDDEDLVDTCAFLHI-KTGEWKKGNCE 144
Cdd:cd00037  76 NWAPGEPNPGGSEDCVVLSSsSDGKWNDVSCS 107

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 26892293  24 CPSsTWIQFQDSCYIFLQEAIkveSIEDVRNQCTDHG-----ADMISIHNEEENAFILDTLKKQWKG--PDDILLGMFYD 96
Cdd:cd03589   1 CPT-FWTAFGGYCYRFFGDRL---TWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPdtPYGLWIGLHDR 76

                        90
                ....*....|....*....
gi 26892293  97 TDDASFKWFDNSNMTFDKW 115
Cdd:cd03589  77 TSEGPFEWTDGSPVDFTKW 95

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 26892293  29 WIQFQDSCYIFLQEAikvESIEDVRNQCTDHGADMISIHNEEENAFILDTLKK-QWKGPDDillgmfyDTDDASFKWFDN 107
Cdd:cd03588   5 WDKFQGHCYRHFPDR---ETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDyQWIGLND-------RTIEGDFRWSDG 74

                ....*...
gi 26892293 108 SNMTFDKW 115
Cdd:cd03588  75 HPLQFENW 82

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 26892293  24 CPSStWIQFQDSCY-IFLQEaikvESIEDVRNQCTDH--GADMISIHNEEENAFILDTLKKQWKGPDDILLGMFYDTDDA 100
Cdd:cd03594   1 CPKG-WLPYKGNCYgYFRQP----LSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSR 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26892293 101 SFKWFDNSNMTFDKWtDQDDDEDLVDTCAFLHIKTG--EWKKGNCEV 145
Cdd:cd03594  76 GWEWSDGSKLDYRSW-DRNPPYARGGYCAELSRSTGflKWNDANCEE 121

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26892293   24 CPSStWIQFQDSCYIFlqeaikvesIEDVRNQ------CTDHGADMISIHNEEENAFIldtlkKQWKGPDDILLGMFYDT 97
Cdd:PHA02642  88 CPKG-WIGFGYKCFYF---------SEDSKNWtfgntfCTSLGATLVKVETEEELNFL-----KRYKDSSDHWIGLNRES 152

                         90
                 ....*....|..
gi 26892293   98 DDASFKWFDNSN 109
Cdd:PHA02642 153 SNHPWKWADNSN 164