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 21553093 189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL-ANVLSWMGLTDQN--GPWRWVDGTDFD 265
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21553093 266 KGFKNWRPLQPDNWHghmlGGGEDCAHFSYD-GRWNDDVCQRHYHWICET 314
Cdd:cd03590  81 SSKTFWHPGEPNNWG----GGGEDCAELVYDsGGWNDVPCNLEYRWICEK 126

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 21553093 189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL-ANVLSWMGLTDQN--GPWRWVDGTDFD 265
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21553093 266 KGFKNWRPLQPDNWHghmlGGGEDCAHFSYD-GRWNDDVCQRHYHWICET 314
Cdd:cd03590  81 SSKTFWHPGEPNNWG----GGGEDCAELVYDsGGWNDVPCNLEYRWICEK 126

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 21553093    189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS----WMGLTD--QNGPWRWVDGT 262
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDpdSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 21553093    263 DFDKgFKNWRPLQPDNwhghmlgGGEDCAHFSYD-GRWNDDVCQRHYHWICE 313
Cdd:smart00034  81 GPVS-YSNWAPGEPNN-------SSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093  189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLSWMGLTDQ--NGPWRWVDGTDFDK 266
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNREssNHPWKWADNSNYNA 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 21553093  267 GFknwrplqpdnwhghMLGGGEDCAHFSyDGRWNDDVCQRHYHWIC 312
Cdd:PHA02642 168 SF--------------VITGTGECAYLN-DIRISSSRVYANRKWIC 198

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093 100 QSLDSRADNFEKGISSLKVDVEDHRQELQAgrdLSQKVTSLESTLEKreqaLKTDLSDLTDHVQQLETDLKALTCQLANL 179
Cdd:COG1579  13 QELDSELDRLEHRLKELPAELAELEDELAA---LEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGNV 85

                ...
gi 21553093 180 KNN 182
Cdd:COG1579  86 RNN 88

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 21553093 189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL-ANVLSWMGLTDQN--GPWRWVDGTDFD 265
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21553093 266 KGFKNWRPLQPDNWHghmlGGGEDCAHFSYD-GRWNDDVCQRHYHWICET 314
Cdd:cd03590  81 SSKTFWHPGEPNNWG----GGGEDCAELVYDsGGWNDVPCNLEYRWICEK 126

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 21553093    189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS----WMGLTD--QNGPWRWVDGT 262
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDpdSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 21553093    263 DFDKgFKNWRPLQPDNwhghmlgGGEDCAHFSYD-GRWNDDVCQRHYHWICE 313
Cdd:smart00034  81 GPVS-YSNWAPGEPNN-------SSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093 189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRL-----ENSHLVVVNSLEEQNFLQNRLANVLS-------WMGLTD--QNG 254
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRGpdtpyglWIGLHDrtSEG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21553093 255 PWRWVDGTDFDkgFKNWRPLQPDNWhghmlGGGEDCAHFSY----DGRWNDDVCQRHYHWIC 312
Cdd:cd03589  81 PFEWTDGSPVD--FTKWAGGQPDNY-----GGNEDCVQMWRrgdaGQSWNDMPCDAVFPYIC 135

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093   208 KSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL--ANVLSWMGLTDQ--NGPWRWVDGTDFDkgFKNWRPLQPDNwhghm 283
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRknEGTWKWVDGSPVN--YTNWAPEPNNN----- 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 21553093   284 lGGGEDCAHFSY-DGRWNDDVCQRHYHWICET 314
Cdd:pfam00059  75 -GENEDCVELSSsSGKWNDENCNSKNPFVCEK 105

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 21553093 201 YWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS---WMGLTDQNGPWRWVDGTDFDKGFKNWRPLQPD 277
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21553093 278 NwhghmlGGGEDCAHFSY--DGRWNDDVCQRHYHWICET 314
Cdd:cd03592  83 N------GRNENCLEIYIkdNGKWNDEPCSKKKSAICYT 115

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093 189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRL--ENSHLVVVNSLEEQNFL-------QNRLANVlsWMGLTD--QNGPWR 257
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIaslissyQKAYQPV--WIGLHDpqQSRGWE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21553093 258 WVDGTDFDkgFKNWRPLQPdnwhghmLGGGEDCAHFSYDG---RWNDDVCQRHYHWICE 313
Cdd:cd03594  79 WSDGSKLD--YRSWDRNPP-------YARGGYCAELSRSTgflKWNDANCEERNPFICK 128

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093 207 EKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS--WMGLTDQNGPWRWVDGTDFDKGFKNWRPLQPDNWhghml 284
Cdd:cd03591  10 EKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTyaFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNA----- 84

                        90       100
                ....*....|....*....|....*....
gi 21553093 285 GGGEDCAHFSYDGRWNDDVCQRHYHWICE 313
Cdd:cd03591  85 GGGEDCVEMYTSGKWNDVACNLTRLFVCE 113

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 21553093 200 CYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS-----WMGLTDQNGPWRWVDGTDFDKGFKNWR-- 272
Cdd:cd03596  11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPgnwevWLGINDMVAEGKWVDVNGSPISYFNWEre 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 21553093 273 -PLQPDNwhghmlGGGEDCAHFS--YDGRWNDDVCQRHYHWICE 313
Cdd:cd03596  91 iTAQPDG------GKRENCVALSssAQGKWFDEDCRREKPYVCE 128

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093  189 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLSWMGLTDQNGpwrwvdgtDFDKGF 268
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKKG--------DDDDRE 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 21553093  269 KNWRPLQPDnwhghmlgGGEDCAhFSYDGRWNDDVCQRHYHWICETEL 316
Cdd:PHA03097 118 VLDKVVKPP--------KSGKCA-YLKDKTIISSNCNATKGWICFDRL 156

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 21553093 196 HEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS---------WMGL-------TDQNGPWR-- 257
Cdd:cd03600   2 VSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGrhgrgslrlWIGLqreprqcSDPSLPLRgf 81

                        90
                ....*....|....*
gi 21553093 258 -WVDGtDFDKGFKNW 271
Cdd:cd03600  82 sWVTG-DQDTDFSNW 95

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093 202 WFSESEKSWPEADKYCRLENSHLVVVNsLEEQNFLQNRLANVLS-----WMGLTD-QNGPWR--WVDGTDFDKGFKNWRP 273
Cdd:cd03601   4 LCSDETMNYAKAGAFCRSRGMRLASLA-MRDSEMRDAILAFTLVkghgyWVGADNlQDGEYDflWNDGVSLPTDSDLWAP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21553093 274 LQPDNWHGHmlgggEDCAHFSYD-GRWNDDVCQRHYHWICE 313
Cdd:cd03601  83 NEPSNPQSR-----QLCVQLWSKyNLLDDEYCGRAKRVICE 118

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093  70 IGSQNSQLRRDLGTLRAILDNTTSKI---KAEFQSLDSRADNFEKGISSLKVDVEDHRQELQA----GRDLSQKVTSLES 142
Cdd:COG4372  43 LQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQEELESlqeeAEELQEELEELQK 122

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 21553093 143 ---TLEKREQALKTDLSDLTDHVQQLETDLKALTCQLANLKNN 182
Cdd:COG4372 123 erqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165

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 21553093 197 EGSCY---WFSESEK--SWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS-----WMGL----------TDQNGPW 256
Cdd:cd03595   9 EKPCYkiaYFQDSRRrlNFEEARQACREDGGELLSIESENEQKLIERFIQTLRAsdgdfWIGLrrssqynvtsSACSSLY 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21553093 257 RWVDGTDfdKGFKNWRPLQPDnwhghmlGGGEDCAHFSYDG------------RWNDDVCQRHYHWICE 313
Cdd:cd03595  89 YWLDGSI--STFRNWYVDEPS-------CGSEVCVVMYHQPsapagqggpylfQWNDDNCNMKNNFICK 148

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21553093  96 KAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAGRDLSQKVTSLESTLEKREQALKTDLSDLTDHVQQLETDLKALTCQ 175
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                ....
gi 21553093 176 LANL 179
Cdd:COG4942 106 LAEL 109