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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112 107 CPKDWKPFDSNCYFPSTDSvESWMESEEKCSGIGAHLVVIHSQEEQDFLPRILDTHAAYFIGLSDP-GHRQWQWVDQTPY 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 54312112 186 NGNATFWHEGEPSS---DNEQCVIINHHEntgWGWSDSSCSDKQKLVCQ 231
Cdd:cd03590  80 NSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWICE 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112 107 CPKDWKPFDSNCYFPSTDSvESWMESEEKCSGIGAHLVVIHSQEEQDFLPRILDTHAAYFIGLSDP-GHRQWQWVDQTPY 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 54312112 186 NGNATFWHEGEPSS---DNEQCVIINHHEntgWGWSDSSCSDKQKLVCQ 231
Cdd:cd03590  80 NSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWICE 125

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112   127 ESWMESEEKCSGIGAHLVVIHSQEEQDFLPRIL-DTHAAYFIGLSDPGH-RQWQWVDQTPYngNATFWH-EGEPSSDNEQ 203
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLkKSNKYFWIGLTDRKNeGTWKWVDGSPV--NYTNWApEPNNNGENED 79

                          90       100
                  ....*....|....*....|....*...
gi 54312112   204 CVIINHhenTGWGWSDSSCSDKQKLVCQ 231
Cdd:pfam00059  80 CVELSS---SSGKWNDENCNSKNPFVCE 104

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112 107 CPKDWKPFDSNCYFPSTDSvESWMESEEKCSGIGAHLVVIHSQEEQDFLPRILDTHAAYFIGLSDP-GHRQWQWVDQTPY 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 54312112 186 NGNATFWHEGEPSS---DNEQCVIINHHEntgWGWSDSSCSDKQKLVCQ 231
Cdd:cd03590  80 NSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWICE 125

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 54312112 117 NCYFPSTDSVeSWMESEEKCSGIGAHLVVIHSQEEQDFLPRIL--DTHAAYFIGLSDPGH-RQWQWVDQTPYNgNATFWH 193
Cdd:cd00037   1 SCYKFSTEKL-TWEEAQEYCRSLGGHLASIHSEEENDFLASLLkkSSSSDVWIGLNDLSSeGTWKWSDGSPLV-DYTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 54312112 194 EGEPSSD-NEQCVIINHheNTGWGWSDSSCSDKQKLVCQV 232
Cdd:cd00037  79 PGEPNPGgSEDCVVLSS--SSDGKWNDVSCSSKLPFICEK 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112 107 CPKDWKPFDSNCY--FPSTdsvESWMESEEKC--SGIGAHLVVIHSQEEQDFLPR-ILDTHAAY---FIGLSDPGH-RQW 177
Cdd:cd03594   1 CPKGWLPYKGNCYgyFRQP---LSWSDAELFCqkYGPGAHLASIHSPAEAAAIASlISSYQKAYqpvWIGLHDPQQsRGW 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 54312112 178 QWVDQTPYNGNAtfWHEGEPSSDNEQCVIINhhENTGW-GWSDSSCSDKQKLVCQ 231
Cdd:cd03594  78 EWSDGSKLDYRS--WDRNPPYARGGYCAELS--RSTGFlKWNDANCEERNPFICK 128

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112   127 ESWMESEEKCSGIGAHLVVIHSQEEQDFLPRIL-DTHAAYFIGLSDPGH-RQWQWVDQTPYngNATFWH-EGEPSSDNEQ 203
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLkKSNKYFWIGLTDRKNeGTWKWVDGSPV--NYTNWApEPNNNGENED 79

                          90       100
                  ....*....|....*....|....*...
gi 54312112   204 CVIINHhenTGWGWSDSSCSDKQKLVCQ 231
Cdd:pfam00059  80 CVELSS---SSGKWNDENCNSKNPFVCE 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112 107 CPKDWKPFDSNCYFPSTDSvESWMESEEKCSGIGAHLVVIHSQEEQDFLPRilDTHAAYFIGLSDPG-HRQWQWVDQTPY 185
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDR-ETWEDAERRCREQQGHLSSIVTPEEQEFVNN--NAQDYQWIGLNDRTiEGDFRWSDGHPL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 54312112 186 NGNAtfWHEGEPSS---DNEQCVIINHHENTgwGWSDSSCSDKQKLVCQ 231
Cdd:cd03588  78 QFEN--WRPNQPDNffaTGEDCVVMIWHEEG--EWNDVPCNYHLPFTCK 122

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112  107 CPKDWKPFDSNCYFPSTDSvESWMESEEKCSGIGAHLVVIHSQEEQDFLPRILDThAAYFIGLS-DPGHRQWQWVDQTPY 185
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDS-KNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDS-SDHWIGLNrESSNHPWKWADNSNY 165

                         90
                 ....*....|....*..
gi 54312112  186 NGNATFWHEGEPSSDNE 202
Cdd:PHA02642 166 NASFVITGTGECAYLND 182

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 54312112 119 YFPSTDSVESWMESEEKCSGIGAHLVVIHSQEEQDFLPRILDTHAA----YFIGLSDPGHR---------QWQWVDQTPy 185
Cdd:cd03595  17 YFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRAsdgdFWIGLRRSSQYnvtssacssLYYWLDGSI- 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 54312112 186 ngnATF--WHEGEPSSDNEQCVIINHHENTGWG--------WSDSSCSDKQKLVCQ 231
Cdd:cd03595  96 ---STFrnWYVDEPSCGSEVCVVMYHQPSAPAGqggpylfqWNDDNCNMKNNFICK 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312112 115 DSNCY--FPSTdsvESWMESEEKCSGIGAHLVVIHSQEEQDFLPRIL--------DTHAAYFIGLS-DPGH--------R 175
Cdd:cd03600   3 SDACYtlHPQK---LTFLEAQRSCIELGGNLATVRSGEEADVVSLLLaagpgrhgRGSLRLWIGLQrEPRQcsdpslplR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 54312112 176 QWQWV--DQtpyNGNATFWH-EGEPSSDNEQCVIINHHENTG--WGWSDSSCS 223
Cdd:cd03600  80 GFSWVtgDQ---DTDFSNWLqEPAGTCTSPRCVALSAAGSTPdnLKWKDGPCS 129