NCBI Conserved Domain Search

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) and similar proteins; MRC2, also called C-type mannose receptor 2, C-type lectin domain family 13 member E (CLEC13E), endocytic receptor 180 (Endo180), urokinase-type plasminogen activator receptor-associated protein (UPARAP), UPAR-associated protein, urokinase receptor-associated protein, or CD280, may play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). MRC2 contains an atypical ricin B-type lectin domain at the N-terminus. The typical ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. In contrast, the ninth, tenth and eleventh beta strands, comprising the gamma subdomain, are missing in the ricin B-type lectin domain of MRC2.

Pssm-ID: 467786 Cd Length: 124 Bit Score: 202.71 E-value: 1.91e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   42 NVFLIFSHGLQGCLEAQGGQVRVTPACNTSLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTT-ASLGMYECDREALNLR 120
Cdd:cd23408     1 DVFLIYSDGAQGCLEVRDSVVRLSPACNTSSPAQQWKWVSRNRLFNLGSMQCLGVSGPNGSGTsATLGTYECDRESVNMR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 110624774  121 WHCRTLGDQLSLLLGARTSNiSKPGTLERGDQTRSGQWRIYGSEE 165
Cdd:cd23408    81 WHCRTLGEQLSQHLGARTAN-GNPSTLERGDQARSSQWRIYGSEQ 124

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 133.11 E-value: 4.99e-36

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774    382 CEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEV--EELWIGLNDLKLQMNFEWSDGS 459
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 110624774    460 -LVSFTHWHPFEPNNFRdslEDCVTIWGPEGRWNDSPCNQSLPSICK 505
Cdd:smart00034   81 gPVSYSNWAPGEPNNSS---GDCVVLSTSGGKWNDVSCTSKLPFVCE 124

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 126.65 E-value: 8.49e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  382 CEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEvEELWIGLNDLKLQMNFEWSDGS-- 459
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGN-RSYWIGLSDEETEGEWKWVDGTpl 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 110624774  460 LVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKK 506
Cdd:cd03590    80 NSSKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 121.19 E-value: 5.64e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  247 SCYQFnFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLL-TGYSSTLWIGLNDLDTSGGWQWSDNSP-LKYLNWES 324
Cdd:cd00037     1 SCYKF-STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAP 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 110624774  325 DQPDNPSEENCGVIRTESSGGWQNRDCSIALPYVCKK 361
Cdd:cd00037    80 GEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 120.42 E-value: 9.26e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  392 HCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIK-QEVEELWIGLNDLKLQMNFEWSDGS-LVSFTHWHPF 469
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLSSEGTWKWSDGSpLVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 110624774  470 EPNNFRDslEDCVTIW-GPEGRWNDSPCNQSLPSICKK 506
Cdd:cd00037    81 EPNPGGS--EDCVVLSsSSDGKWNDVSCSSKLPFICEK 116

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 115.00 E-value: 1.04e-29

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774    235 CETFWDkdQLTDSCYQFnFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSST--LWIGLNDLDTSGGWQWS 312
Cdd:smart00034    1 CPSGWI--SYGGKCYKF-STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWS 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 110624774    313 DNSPL-KYLNWESDQPDNpSEENCGVIRTeSSGGWQNRDCSIALPYVCK 360
Cdd:smart00034   78 DGSGPvSYSNWAPGEPNN-SSGDCVVLST-SGGKWNDVSCTSKLPFVCE 124

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 114.21 E-value: 1.80e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  382 CEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKqevEELWIGLNDLKLQMNFEWSDGSLV 461
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQ---DYQWIGLNDRTIEGDFRWSDGHPL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 110624774  462 SFTHWHPFEPNNFRDSLEDCVT-IWGPEGRWNDSPCNQSLPSICKK 506
Cdd:cd03588    78 QFENWRPNQPDNFFATGEDCVVmIWHEEGEWNDVPCNYHLPFTCKK 123

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.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 109.37 E-value: 1.32e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  382 CEPSWQPFQGHCYRLQAEKRSWQESKKACL-----RGGGDLVSIHSMAELEFITKQIKQ-----EVEELWIGLNDLKLQM 451
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVYDLFESsrgpdTPYGLWIGLHDRTSEG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 110624774  452 NFEWSDGSLVSFTHWHPFEPNNfRDSLEDCVTIW---GPEGRWNDSPCNQSLPSICK 505
Cdd:cd03589    81 PFEWTDGSPVDFTKWAGGQPDN-YGGNEDCVQMWrrgDAGQSWNDMPCDAVFPYICK 136

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 107.56 E-value: 2.56e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   400 KRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNNfrDSLE 479
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*..
gi 110624774   480 DCVTIWGPEGRWNDSPCNQSLPSICKK 506
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 107.69 E-value: 3.09e-27

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774    521 CRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLI-YNWEGEYFWTALQDLNSTGSFFWLSGD 599
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLkNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 110624774    600 E-VMYTHWNRDQPGYSRGGCVALATGSamGLWEVKNCTSFRaRYIC 644
Cdd:smart00034   81 GpVSYSNWAPGEPNNSSGDCVVLSTSG--GKWNDVSCTSKL-PFVC 123

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 106.14 E-value: 1.12e-26

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774    829 WLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSraQEQHWWIGLHTSESDGRFRWTDGS-I 907
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSG--SSDYYWIGLSDPDSNGSWQWSDGSgP 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 110624774    908 INFISWAPGKPRPVGKDkkCVYMTASREDWGDQRCLTALPYICK 951
Cdd:smart00034   83 VSYSNWAPGEPNNSSGD--CVVLSTSGGKWNDVSCTSKLPFVCE 124

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 102.70 E-value: 1.50e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  837 YKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRaqeQHWWIGLHTSESDGRFRWTDGS-IINFISWAP 915
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSS---SDVWIGLNDLSSEGTWKWSDGSpLVDYTNWAP 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 110624774  916 GKPRPvGKDKKCVYMTASRED-WGDQRCLTALPYICKR 952
Cdd:cd00037    80 GEPNP-GGSEDCVVLSSSSDGkWNDVSCSSKLPFICEK 116

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 101.79 E-value: 2.41e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   256 TLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEENC 335
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENEDC 80

                           90       100
                   ....*....|....*....|....*.
gi 110624774   336 GVIRTeSSGGWQNRDCSIALPYVCKK 361
Cdd:pfam00059   81 VELSS-SSGKWNDENCNSKNPFVCEK 105

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 100.00 E-value: 1.47e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  531 SCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGEYFWTALQDLNSTGSFFWLSGDEVM-YTHWNRD 609
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVdYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 110624774  610 QPGYSRGG-CVALATGSAmGLWEVKNCTSfRARYIC 644
Cdd:cd00037    81 EPNPGGSEdCVVLSSSSD-GKWNDVSCSS-KLPFIC 114

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 99.21 E-value: 2.78e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   42 NVFLIFSHGLQGCLEAQGGQVRVTPA-CNTSLPAQRWKWVSRNRLFNLGTMQCLGTgwPGTNTTASLGMYECDREALNLR 120
Cdd:cd23385     1 DSFLIYNEDLGKCLAARSSSSKVSLStCNPNSPNQQWKWTSGHRLFNVGTGKCLGV--SSSSPSSPLRLFECDSEDELQK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 110624774  121 WHCRTLGDQLSLLLGARTS-NISKPGTLERGDQTRSGQWRI 160
Cdd:cd23385    79 WKCSKDGLLLLKGLGLLLLyDKSGKNVVVSKGSGLSSRWKI 119

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 98.06 E-value: 8.24e-24

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774    669 CPQGWASDTKlrYCYKVFSserlqDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIFGesepeiheQHWFWIGL 748
Cdd:smart00034    1 CPSGWISYGG--KCYKFST-----EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGS--------SDYYWIGL 65

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110624774    749 NRRDPRGgqSWRWSDGVG-FSYHNFDRSrHDDDDIRGCAVLDLASLQWVAMQCDTQLDWICK 809
Cdd:smart00034   66 SDPDSNG--SWQWSDGSGpVSYSNWAPG-EPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 96.51 E-value: 3.14e-23

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774    972 CPSDWIQFLNKCFQVQGQEpqsrVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVT--FDLWIGLHA--SQRDFQW 1047
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEK----KTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssDYYWIGLSDpdSNGSWQW 76

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110624774   1048 VEQEPLM-YANWAPGEPSGPSPapsgnkptSCAVVLHSpsahfTGRWDDRSCTEEtHGFICQ 1108
Cdd:smart00034   77 SDGSGPVsYSNWAPGEPNNSSG--------DCVVLSTS-----GGKWNDVSCTSK-LPFVCE 124

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 95.06 E-value: 1.12e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  235 CETFWDkdQLTDSCYQFNfQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTlWIGLNDLDTSGGWQWSDN 314
Cdd:cd03590     1 CPTNWK--SFQSSCYFFS-TEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY-WIGLSDEETEGEWKWVDG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110624774  315 SPL--KYLNWESDQPDN--PSEENCGVIRTeSSGGWQNRDCSIALPYVCKK 361
Cdd:cd03590    77 TPLnsSKTFWHPGEPNNwgGGGEDCAELVY-DSGGWNDVPCNLEYRWICEK 126

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.

Pssm-ID: 128373 Cd Length: 49 Bit Score: 90.44 E-value: 4.29e-22

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 110624774    180 GNSHGKPCTIPFKYDNQWFHGCTSTGREDGHLWCATTQDYGKDERWGFC 228
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 91.91 E-value: 8.15e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  681 YCYKVFSserlqDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKifgesepeiHEQHWFWIGLNRRDPRGgqSWR 760
Cdd:cd00037     1 SCYKFST-----EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK---------SSSSDVWIGLNDLSSEG--TWK 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 110624774  761 WSDGVG-FSYHNFDRSRHDDDDIRGCAVLDLASL-QWVAMQCDTQLDWICKI 810
Cdd:cd00037    65 WSDGSPlVDYTNWAPGEPNPGGSEDCVVLSSSSDgKWNDVSCSSKLPFICEK 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.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 89.74 E-value: 8.58e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  382 CEPSWQPFQGHCYRLQAEKRSWQESKKAC--LRGGGDLVSIHSMAELEFITKQIKQ---EVEELWIGLNDLKLQMNFEWS 456
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISSyqkAYQPVWIGLHDPQQSRGWEWS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110624774  457 DGSLVSFTHWHPFEPNNFRdslEDCVTIWGPEG--RWNDSPCNQSLPSICK 505
Cdd:cd03594    81 DGSKLDYRSWDRNPPYARG---GYCAELSRSTGflKWNDANCEERNPFICK 128

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.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 89.72 E-value: 9.05e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  829 WLRFQEAEYKFFEHHSTWAQAQRICTWF-----QAELTSVHSQAELDFLsHNLQKFSRAQEQHW--WIGLHTSESDGRFR 901
Cdd:cd03589     5 WTAFGGYCYRFFGDRLTWEEAELRCRSFsipglIAHLVSIHSQEENDFV-YDLFESSRGPDTPYglWIGLHDRTSEGPFE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110624774  902 WTDGSIINFISWAPGKPRPVGKDKKCVYMtASRED----WGDQRCLTALPYICK 951
Cdd:cd03589    84 WTDGSPVDFTKWAGGQPDNYGGNEDCVQM-WRRGDagqsWNDMPCDAVFPYICK 136

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.

Pssm-ID: 238019 Cd Length: 48 Bit Score: 85.43 E-value: 2.30e-20

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 110624774  181 NSHGKPCTIPFKYDNQWFHGCTSTGREDGHLWCATTQDYGKDERWGFC 228
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 86.90 E-value: 5.51e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  982 KCFQVQGQepqsRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNV-TFDLWIGLH--ASQRDFQWVEQEPLM-YAN 1057
Cdd:cd00037     1 SCYKFSTE----KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSsSSDVWIGLNdlSSEGTWKWSDGSPLVdYTN 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 110624774 1058 WAPGEpsgpspaPSGNKPTSCAVVLHSPsahfTGRWDDRSCTeETHGFICQK 1109
Cdd:cd00037    77 WAPGE-------PNPGGSEDCVVLSSSS----DGKWNDVSCS-SKLPFICEK 116

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 86.09 E-value: 1.36e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  235 CETFWDKDQltDSCYQFnFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSstlWIGLNDLDTSGGWQWSDN 314
Cdd:cd03588     1 CEEGWDKFQ--GHCYRH-FPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 110624774  315 SPLKYLNWESDQPDN--PSEENCGVIRTESSGGWQNRDCSIALPYVCKK 361
Cdd:cd03588    75 HPLQFENWRPNQPDNffATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKK 123

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

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 85.43 E-value: 1.77e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  394 YRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNN 473
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNN 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 110624774  474 FRDSlEDCVTIWGpEGRWNDSPCNQSLPSIC 504
Cdd:cd03591    84 AGGG-EDCVEMYT-SGKWNDVACNLTRLFVC 112

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 85.34 E-value: 2.30e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   1261 CPQGladsaWIPFREHCYSFHMELLlGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGQSRgAWLGMNFNPKGGT 1340
Cdd:smart00034    1 CPSG-----WISYGGKCYKFSTEKK-TWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY-YWIGLSDPDSNGS 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 110624774   1341 LVWQDNT-AVNYSNWGPpglGPSMLSHNSCYWIQSNSGLWRPGACTNiTMGVVCK 1394
Cdd:smart00034   74 WQWSDGSgPVSYSNWAP---GEPNNSSGDCVVLSTSGGKWNDVSCTS-KLPFVCE 124

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.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 84.73 E-value: 4.03e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  669 CPQGWaSDTKlRYCYKVFSSErlqdkKSWVQAQGACQEL--GAQLLSLASYEEEHFVANMLNKIFGESEPeiheqhwFWI 746
Cdd:cd03594     1 CPKGW-LPYK-GNCYGYFRQP-----LSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAYQP-------VWI 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110624774  747 GLNrrDPRGGQSWRWSDGVGFSYhnfdRSRHDDDDIRG---CAVLDLAS--LQWVAMQCDTQLDWICK 809
Cdd:cd03594    67 GLH--DPQQSRGWEWSDGSKLDY----RSWDRNPPYARggyCAELSRSTgfLKWNDANCEERNPFICK 128

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 81.76 E-value: 2.65e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   845 TWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSraqeQHWWIGLHTSESDGRFRWTDGSIINFISWAPgKPRPVGKD 924
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN----KYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGEN 77

                           90       100
                   ....*....|....*....|....*...
gi 110624774   925 KKCVYMTASREDWGDQRCLTALPYICKR 952
Cdd:pfam00059   78 EDCVELSSSSGKWNDENCNSKNPFVCEK 105

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.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 82.41 E-value: 3.30e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  235 CETFWDkdQLTDSCYQFnFQSTLSWREAWASCEQQG-----ADLLSITEIHEQTYINGLLTGYSST-----LWIGLNDLD 304
Cdd:cd03589     1 CPTFWT--AFGGYCYRF-FGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPdtpygLWIGLHDRT 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110624774  305 TSGGWQWSDNSPLKYLNWESDQPDN-PSEENCGVIRTESSGG--WQNRDCSIALPYVCK 360
Cdd:cd03589    78 SEGPFEWTDGSPVDFTKWAGGQPDNyGGNEDCVQMWRRGDAGqsWNDMPCDAVFPYICK 136

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. Ly-75 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467789 Cd Length: 116 Bit Score: 79.01 E-value: 2.99e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   42 NVFLIFSHGLQGCLEAQGGQVRVTpACNTSLPAQRWKWVSRNRLFNLGTMQCLGTGwpGTNTTASLGMYECDREALNLRW 121
Cdd:cd23411     3 DIFTIQHENSGKCLKVENSQISAV-DCKQSSESLQWKWVSEHRLFNLGSKQCLGLD--ITKPSNTLKMFECDSKSVMLWW 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 110624774  122 HCR------TLGDQLSLLLGARTSNISKPGTLERGD 151
Cdd:cd23411    80 RCEggslygASQYRLAVKNGSVTASIDSNDTWKKGG 115

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 78.77 E-value: 4.36e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  829 WLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSraqeqhwWIGLHTSESDGRFRWTDGSII 908
Cdd:cd03588     5 WDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-------WIGLNDRTIEGDFRWSDGHPL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 110624774  909 NFISWAPGKPRP---VGKDkkCVYMTASRE-DWGDQRCLTALPYICKR 952
Cdd:cd03588    78 QFENWRPNQPDNffaTGED--CVVMIWHEEgEWNDVPCNYHLPFTCKK 123

Fibronectin type II domain;

Pssm-ID: 459645 Cd Length: 42 Bit Score: 75.68 E-value: 6.63e-17

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 110624774   187 CTIPFKYDNQWFHGCTSTGREDGHLWCATTQDYGKDERWGFC 228
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 77.52 E-value: 8.35e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   539 QVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNwEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRGG- 617
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK-SNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENEd 79

                           90       100
                   ....*....|....*....|....*....
gi 110624774   618 CVALAtgSAMGLWEVKNCTSfRARYICRQ 646
Cdd:pfam00059   80 CVELS--SSSGKWNDENCNS-KNPFVCEK 105

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 77.34 E-value: 1.75e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  972 CPSDWIQFLNKCFQVqgqepqSRVK--WSEAQFSCEQQEAQLVTITNPLEQAFITASLpNVTFDLWIGLHASQRD--FQW 1047
Cdd:cd03590     1 CPTNWKSFQSSCYFF------STEKksWEESRQFCEDMGAHLVIINSQEEQEFISKIL-SGNRSYWIGLSDEETEgeWKW 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110624774 1048 VEQEPLM--YANWAPGEPSgpSPAPSGNKptsCAVVLHSpsahfTGRWDDRSCTEETHgFICQK 1109
Cdd:cd03590    74 VDGTPLNssKTFWHPGEPN--NWGGGGED---CAELVYD-----SGGWNDVPCNLEYR-WICEK 126

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 76.22 E-value: 3.11e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  235 CETFWDKDQltDSCYQFnFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSStlWIGLNDLDTSGGWQWSDN 314
Cdd:cd03593     1 CPKDWICYG--NKCYYF-SMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWIDG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 110624774  315 SPLKylNWESDQPDNPSeENCGVIrteSSGGWQNRDCSIALPYVCKK 361
Cdd:cd03593    76 SPLN--NLFNIRGSTKS-GNCAYL---SSTGIYSEDCSTKKRWICEK 116

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 76.01 E-value: 3.70e-16

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774     46 IFSHGLQGCLEAQGGQVRV-TPACNTSLPAQRWKWVSRNRLFNLGTMQCLGTGWpgtNTTASLGMYECDREALNLRWHCR 124
Cdd:smart00458    1 IISGNTGKCLDVNGNKNPVgLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANG---NTGSTVTLYSCDGTNDNQYWEVN 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 110624774    125 TLGD----QLSLLLGARTSNISKPGTLERGDQTRSGQWRIY 161
Cdd:smart00458   78 KDGTirnpDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 118

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 75.80 E-value: 4.04e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  260 REAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNP-SEENCGVI 338
Cdd:cd03591    14 DDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNAgGGEDCVEM 93

                          90       100
                  ....*....|....*....|.
gi 110624774  339 rtESSGGWQNRDCSIALPYVC 359
Cdd:cd03591    94 --YTSGKWNDVACNLTRLFVC 112

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 75.21 E-value: 4.53e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   997 WSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQR--DFQWVEQEPLMYANWAPgEPSGPSPAPsgnk 1074
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNegTWKWVDGSPVNYTNWAP-EPNNNGENE---- 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 110624774  1075 ptSCAVVLHSPsahftGRWDDRSCTEEtHGFICQK 1109
Cdd:pfam00059   79 --DCVELSSSS-----GKWNDENCNSK-NPFVCEK 105

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.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 75.49 E-value: 7.32e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  247 SCYQFnFQSTLSWREAWASCEQ--QGADLLSITEIHEQTYINGLLTGY---SSTLWIGLNDLDTSGGWQWSDNSPLKYLN 321
Cdd:cd03594    11 NCYGY-FRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYqkaYQPVWIGLHDPQQSRGWEWSDGSKLDYRS 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110624774  322 WESDQPdNPSEENCGVIRTESS-GGWQNRDCSIALPYVCK 360
Cdd:cd03594    90 WDRNPP-YARGGYCAELSRSTGfLKWNDANCEERNPFICK 128

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 74.72 E-value: 9.33e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  255 STLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGY-SSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEE 333
Cdd:cd03592     8 EKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYnLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPNNGRNE 87

                          90       100
                  ....*....|....*....|....*.
gi 110624774  334 NCGVIRTESSGGWQNRDCSIALPYVC 359
Cdd:cd03592    88 NCLEIYIKDNGKWNDEPCSKKKSAIC 113

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 72.79 E-value: 4.37e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  394 YRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEEL-WIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPN 472
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 110624774  473 NFRDslEDCVTIW-GPEGRWNDSPCNQSLPSIC 504
Cdd:cd03592    83 NGRN--ENCLEIYiKDNGKWNDEPCSKKKSAIC 113

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 72.75 E-value: 5.10e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  828 EWLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRaqeqhwWIGLHTSESDGRFRWTDGSI 907
Cdd:cd03593     4 DWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY------WIGLSREKSEKPWKWIDGSP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 110624774  908 INFIswapGKPRPVGKDKKCVYMTASREDwgDQRCLTALPYICKR 952
Cdd:cd03593    78 LNNL----FNIRGSTKSGNCAYLSSTGIY--SEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 72.75 E-value: 5.25e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  382 CEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQevEELWIGLNDLKLQMNFEWSDGSlv 461
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGS-- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 110624774  462 SFTHWhpFEPNNFRDSlEDCVTIWGpeGRWNDSPCNQSLPSICKK 506
Cdd:cd03593    77 PLNNL--FNIRGSTKS-GNCAYLSS--TGIYSEDCSTKKRWICEK 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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 72.65 E-value: 6.10e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1276 HCYSFHMELLlGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGQSrgAWLGMNFNPKGGTLVWQDNT-AVNYSNW 1354
Cdd:cd00037     1 SCYKFSTEKL-TWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD--VWIGLNDLSSEGTWKWSDGSpLVDYTNW 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 110624774 1355 GPPglGPSMLSHNSCYWIQSNS-GLWRPGACTNiTMGVVCK 1394
Cdd:cd00037    78 APG--EPNPGGSEDCVVLSSSSdGKWNDVSCSS-KLPFICE 115

ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor (PLA2R1) and similar proteins; PLA2R1, also called PLA2-R, PLA2R, 180 kDa secretory phospholipase A2 receptor, C-type lectin domain family 13 member C (CLEC13C), or M-type receptor, is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine production during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. PLA2R1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467788 Cd Length: 118 Bit Score: 72.47 E-value: 6.13e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   41 PNVFLIFSHGLQGCLEAQGGQVRVTpACNTSLPAQRWKWVSRNRLFNLGTMQCLgtgwpGTNTTA---SLGMYECDREAL 117
Cdd:cd23410     1 KGMFILESESLKKCISADKSGLFLE-NCDQPSDSMLWKWVSRHRLFNLGSSMCL-----GLNLSYpqqPLGLFECDSTLR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 110624774  118 NLRWHCrtLGDqlsLLLGARTSNISKPGTLERGDQTRSGQWRIYGSEED 166
Cdd:cd23410    75 TLWWRC--NGK---MLIGADQYKLTAVGSKVVASRQSSHKWKPYGSQDE 118

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.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 72.40 E-value: 8.02e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  823 PQGrreWLRFQEAEYKFFEHHSTWAQAQRICTWFQ--AELTSVHSQAELDFLSHNLQKFSRAqEQHWWIGLHTSESDGRF 900
Cdd:cd03594     2 PKG---WLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYQKA-YQPVWIGLHDPQQSRGW 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110624774  901 RWTDGSIINFISWaPGKPrPVGKDKKCVYMTASRE--DWGDQRCLTALPYICK 951
Cdd:cd03594    78 EWSDGSKLDYRSW-DRNP-PYARGGYCAELSRSTGflKWNDANCEERNPFICK 128

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 70.58 E-value: 1.99e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   694 KKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIfGESepeiheqhwFWIGLNRRDPrgGQSWRWSDGVGFSYHNFD 773
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS-NKY---------FWIGLTDRKN--EGTWKWVDGSPVNYTNWA 68

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 110624774   774 RSRHDDDDIRGCAVLDLASLQWVAMQCDTQLDWICK 809
Cdd:pfam00059   69 PEPNNNGENEDCVELSSSSGKWNDENCNSKNPFVCE 104

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 69.71 E-value: 4.13e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  257 LSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLndLDTSGGWQWSDNSPLKYLNWESDQPDNpsEENCG 336
Cdd:cd03602    10 KTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQPFG--QGDCA 85

                          90       100
                  ....*....|....*....|...
gi 110624774  337 VIRteSSGGWQNRDCSIALPYVC 359
Cdd:cd03602    86 TMY--SSGRWYAALCSALKPFIC 106

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 69.76 E-value: 6.01e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  249 YQFnFQSTLSWREAWASCEQQGADLLSITEIHEQTYInGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPD 328
Cdd:cd03603     3 YKF-VDGGMTWEAAQTLAESLGGHLVTINSAEENDWL-LSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80

                          90       100
                  ....*....|....*....|..
gi 110624774  329 NPSEENCGVIRTES----SGGW 346
Cdd:cd03603    81 NNGGGNEDYAAINHfpgiSGKW 102

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.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 69.69 E-value: 1.01e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  972 CPSDWIQFLNKCFQVQGqepqSRVKWSEAQFSCEQ-----QEAQLVTITNPLEQAFI-----TASLPNVTFDLWIGLH-- 1039
Cdd:cd03589     1 CPTFWTAFGGYCYRFFG----DRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVydlfeSSRGPDTPYGLWIGLHdr 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110624774 1040 ASQRDFQWVEQEPLMYANWAPGEPSgpspapSGNKPTSCAVVLHSPSAhfTGRWDDRSCTEEtHGFIC 1107
Cdd:cd03589    77 TSEGPFEWTDGSPVDFTKWAGGQPD------NYGGNEDCVQMWRRGDA--GQSWNDMPCDAV-FPYIC 135

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 69.26 E-value: 1.19e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  521 CRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYnwEGEYFWTALQDLNSTGSFFWLSGD- 599
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS--GNRSYWIGLSDEETEGEWKWVDGTp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 110624774  600 -EVMYTHWNRDQPGYSRGG---CVALatGSAMGLWEVKNCTsFRARYIC 644
Cdd:cd03590    79 lNSSKTFWHPGEPNNWGGGgedCAEL--VYDSGGWNDVPCN-LEYRWIC 124

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 68.10 E-value: 2.69e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  828 EWLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKfsraqEQHWWIGLHTSESDGRFRWTDGS- 906
Cdd:cd03590     4 NWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSG-----NRSYWIGLSDEETEGEWKWVDGTp 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 110624774  907 -IINFISWAPGKP---RPVGKDkkCVYMTASREDWGDQRCLTALPYICKR 952
Cdd:cd03590    79 lNSSKTFWHPGEPnnwGGGGED--CAELVYDSGGWNDVPCNLEYRWICEK 126

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.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 67.09 E-value: 4.29e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  837 YKFFEHHSTWAQAQRICT-WFQAELTSVHSQAeldfLSHNLQKFSRAQEQ-HWWIGLHTSESDG--RFRWTDGSIINFIS 912
Cdd:cd03598     4 YRFVKSPRTFRDAQVICRrCYRGNLASIHSFA----FNYRVQRLVSTLNQaQVWIGGIITGKGRcrRFSWVDGSVWNYAY 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 110624774  913 WAPGKPRPvgKDKKCVYMTASREDWGDQRCLTALPYIC 950
Cdd:cd03598    80 WAPGQPGN--RRGHCVELCTRGGHWRRAHCKLRRPFIC 115

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 66.68 E-value: 6.00e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  533 YWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGeyFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPG 612
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGA--SWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80


                  ....*
gi 110624774  613 YSRGG 617
Cdd:cd03603    81 NNGGG 85

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 65.86 E-value: 9.18e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  399 EKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEELWIGLndLKLQMNFEWSDGSLVSFTHWHPFEPnnfrDSL 478
Cdd:cd03602     8 ESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQP----FGQ 81

                          90       100
                  ....*....|....*....|....*.
gi 110624774  479 EDCVTIwGPEGRWNDSPCNQSLPSIC 504
Cdd:cd03602    82 GDCATM-YSSGRWYAALCSALKPFIC 106

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 66.10 E-value: 9.80e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1137 FRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLT-QAARGLRTPLWIGLAGEEGSRRYSWVSEEP-LNYVGWQDGEP 1214
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAsLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEP 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 110624774 1215 --QQPGGCTYVDV--DGAWRTTSCDTKLqGAVCGV 1245
Cdd:cd00037    83 npGGSEDCVVLSSssDGKWNDVSCSSKL-PFICEK 116

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.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 66.26 E-value: 1.18e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  248 CYqFNFQSTLSWREAWASCEQQGADLLSITEIHE----QTYINGLLtGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWE 323
Cdd:cd03596    11 CY-LVSEETKHYHEASEDCIARGGTLATPRDSDEndalRDYVKASV-PGNWEVWLGINDMVAEGKWVDVNGSPISYFNWE 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 110624774  324 ---SDQPDNPSEENCGVIRTESSGGWQNRDCSIALPYVC 359
Cdd:cd03596    89 reiTAQPDGGKRENCVALSSSAQGKWFDEDCRREKPYVC 127

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.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 66.24 E-value: 1.40e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  521 CRKGWTWHSPSCYWLGEDQVTYSEARRLCTDH--GSQLVTITNRFEQAFVSSLI--YNWEGEYFWTALQDLNSTGSFFWL 596
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLIssYQKAYQPVWIGLHDPQQSRGWEWS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 110624774  597 SGDEVMYTHWNRDQPGYSRGGCVALATGSAMGLWEVKNCTSfRARYICR 645
Cdd:cd03594    81 DGSKLDYRSWDRNPPYARGGYCAELSRSTGFLKWNDANCEE-RNPFICK 128

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 66.08 E-value: 1.45e-12

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   1131 SYLNGTFRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGL--RTPLWIGLAGEEGSRRYSWVS-EEPLNYV 1207
Cdd:smart00034    7 SYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgsSDYYWIGLSDPDSNGSWQWSDgSGPVSYS 86

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 110624774   1208 GWQDGEPQQPGG-CTYVDVD-GAWRTTSCDTKLqGAVC 1243
Cdd:smart00034   87 NWAPGEPNNSSGdCVVLSTSgGKWNDVSCTSKL-PFVC 123

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 63.12 E-value: 1.00e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  669 CPQGWasdtkLRY---CYKVFSserlqDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIFgesepeiheqhwFW 745
Cdd:cd03593     1 CPKDW-----ICYgnkCYYFSM-----EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS------------YW 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110624774  746 IGLNRRDPrgGQSWRWSDGvGFSYHNFDRSRHDDDDirGCAVLDLASLQwvAMQCDTQLDWICK 809
Cdd:cd03593    59 IGLSREKS--EKPWKWIDG-SPLNNLFNIRGSTKSG--NCAYLSSTGIY--SEDCSTKKRWICE 115

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) and similar proteins; MRC1, also called MMR, C-type lectin domain family 13 member D (CLEC13D), C-type lectin domain family 13 member D-like (CLEC13DL), macrophage mannose receptor 1-like protein 1 (MRC1L1), or CD206, mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains. MRC1 acts as phagocytic receptor for bacteria, fungi and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467785 Cd Length: 123 Bit Score: 63.15 E-value: 1.18e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   42 NVFLIFSHGLQGCLEAQGGQVRVTPACNTSLPAQRWKWVSRNRLFNLGTMQCLGTgwPGTNTTASLGMYECDREALNLRW 121
Cdd:cd23407     1 RSFLIYNEDHNRCVQARSSSSVTTATCNPNAESQKFRWVSGSQILSVAFKLCLGV--PSKKDWVTVTLFPCNEKSELQKW 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 110624774  122 HCR--TL----GDQLSLLLGARTSNISKpgtLERGDQTRSgQWRIYGS 163
Cdd:cd23407    79 ECKndTLlalkGEDLYFNYGNRQEKNVM---LYKGSGLWS-RWKIYGT 122

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 63.12 E-value: 1.30e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  521 CRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNwegEYFWTALQDLNSTGSFFWLSGDE 600
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS---SSYWIGLSREKSEKPWKWIDGSP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 110624774  601 vmYTHWNRDQPGYSRGGCVALATGSAMGlwevKNCTSfRARYICRQ 646
Cdd:cd03593    78 --LNNLFNIRGSTKSGNCAYLSSTGIYS----EDCST-KKRWICEK 116

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 61.72 E-value: 2.66e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  1290 EARQRCQRAGGAVLSILDEMENVFVWEHLQSYegqSRGAWLGMNFNPKGGTLVWQDNTAVNYSNWGPPGLGPSmlSHNSC 1369
Cdd:pfam00059    6 EAREACRKLGGHLVSINSAEELDFLSSTLKKS---NKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENEDC 80

                           90       100
                   ....*....|....*....|....*
gi 110624774  1370 YWIQSNSGLWRPGACTNITmGVVCK 1394
Cdd:pfam00059   81 VELSSSSGKWNDENCNSKN-PFVCE 104

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 61.34 E-value: 3.53e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  1146 WHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGEEGSRRYSWVSEEPLNYVGWQD--GEPQQPGGC-TY 1222
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPepNNNGENEDCvEL 83

                           90       100
                   ....*....|....*....|.
gi 110624774  1223 VDVDGAWRTTSCDTKLqGAVC 1243
Cdd:pfam00059   84 SSSSGKWNDENCNSKN-PFVC 103

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 61.67 E-value: 4.17e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  997 WSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFdLWIGL--HASQRDFQWVEQEPLMYANWAPGEPSGPSPAPSGNK 1074
Cdd:cd03603    12 WEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGA-SWIGAsdAATEGTWKWSDGEESTYTNWGSGEPHNNGGGNEDYA 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 110624774 1075 PTscavvlhSPSAHFTGRWDDRSCTEETHGFI 1106
Cdd:cd03603    91 AI-------NHFPGISGKWNDLANSYNTLGYV 115

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 61.17 E-value: 6.75e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  669 CPQGWASDTklRYCYkVFSSErlqdKKSWVQAQGACQELGAQLLSLASYEEEHFVanmlNKIFGESEpeiheqhWFWIGL 748
Cdd:cd03590     1 CPTNWKSFQ--SSCY-FFSTE----KKSWEESRQFCEDMGAHLVIINSQEEQEFI----SKILSGNR-------SYWIGL 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110624774  749 NrrDPRGGQSWRWSDG--VGFSYHNFDRSRHDDDDIRG--CAVLDLASLQWVAMQCDTQLDWICK 809
Cdd:cd03590    63 S--DEETEGEWKWVDGtpLNSSKTFWHPGEPNNWGGGGedCAELVYDSGGWNDVPCNLEYRWICE 125

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 59.90 E-value: 1.85e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  972 CPSDWIQFLNKCFQvqgqEPQSRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTfdlWIGLH--ASQRDFQWVE 1049
Cdd:cd03588     1 CEEGWDKFQGHCYR----HFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNdrTIEGDFRWSD 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110624774 1050 QEPLMYANWAPGEPSgpSPAPSGNkptSCAVVLhspsAHFTGRWDDRSCTEEThGFICQKG 1110
Cdd:cd03588    74 GHPLQFENWRPNQPD--NFFATGE---DCVVMI----WHEEGEWNDVPCNYHL-PFTCKKG 124

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.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 59.71 E-value: 2.17e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  521 CRKGWTWHSpSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFV-----SSLIYNWEgeyFWTALQDLNSTGSFFW 595
Cdd:cd03596     1 CLKGTKIHK-KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALrdyvkASVPGNWE---VWLGINDMVAEGKWVD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110624774  596 LSGDEVMYTHWNRDQPGYSRGG----CVALAtGSAMGLWEVKNCTSfRARYIC 644
Cdd:cd03596    77 VNGSPISYFNWEREITAQPDGGkrenCVALS-SSAQGKWFDEDCRR-EKPYVC 127

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 59.23 E-value: 2.70e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  981 NKCFQVQGQEpqsrVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQR--DFQWVEQEPLMYANW 1058
Cdd:cd03591     1 EKIFVTNGEE----KNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETegQFVYLDGGPLTYTNW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 110624774 1059 APGEPSGPSPApsgnkpTSCAVVLHSpsahftGRWDDRSCtEETHGFICQ 1108
Cdd:cd03591    77 KPGEPNNAGGG------EDCVEMYTS------GKWNDVAC-NLTRLFVCE 113

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 58.59 E-value: 4.04e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  392 HCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEvEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEP 471
Cdd:cd03603     1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKWSDGEESTYTNWGSGEP 79

                          90       100
                  ....*....|....*....|....*..
gi 110624774  472 NNFRDSLEDCV---TIWGPEGRWNDSP 495
Cdd:cd03603    80 HNNGGGNEDYAainHFPGISGKWNDLA 106

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.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 59.52 E-value: 5.09e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  389 FQGHCYRLQ-----AEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQI---KQEVEELWIGL--------NDLKLQMN 452
Cdd:cd03595     8 TEKPCYKIAyfqdsRRRLNFEEARQACREDGGELLSIESENEQKLIERFIqtlRASDGDFWIGLrrssqynvTSSACSSL 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110624774  453 FEWSDGSLVSFTHWHPFEPNNfrdSLEDCVTIW----GPEG-------RWNDSPCNQSLPSICK 505
Cdd:cd03595    88 YYWLDGSISTFRNWYVDEPSC---GSEVCVVMYhqpsAPAGqggpylfQWNDDNCNMKNNFICK 148

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.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 58.91 E-value: 5.10e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  669 CPQGWASDTKlrYCYKVFSserlqDKKSWVQAQGACQELG-----AQLLSLASYEEEHFVANMLNKIFGESEPEIHeqhw 743
Cdd:cd03589     1 CPTFWTAFGG--YCYRFFG-----DRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPDTPYGL---- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110624774  744 fWIGLNrrDPRGGQSWRWSDGVGFSYHNFDRSRHDD-DDIRGCAVL---DLASLQWVAMQCDTQLDWICKI 810
Cdd:cd03589    70 -WIGLH--DRTSEGPFEWTDGSPVDFTKWAGGQPDNyGGNEDCVQMwrrGDAGQSWNDMPCDAVFPYICKM 137

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 58.11 E-value: 5.92e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  972 CPSDWIQFLNKCFQVqGQEPQSrvkWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFdlWIGLHASQRDFQWVeqe 1051
Cdd:cd03593     1 CPKDWICYGNKCYYF-SMEKKT---WNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWK--- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110624774 1052 plmyanWAPGEPSGPSPAPSGNKPTSCAVVLHSPSAHFTgrwddrSCtEETHGFICQK 1109
Cdd:cd03593    72 ------WIDGSPLNNLFNIRGSTKSGNCAYLSSTGIYSE------DC-STKKRWICEK 116

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 58.08 E-value: 6.74e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  845 TWAQAQRICTWFQAELTSVHSQAE----LDFLShnlQKFSRAqeqhwWIGLHTSESDGRFRWTDGSIINFISWAPGKPRP 920
Cdd:cd03591    12 NFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVK---KGNTYA-----FIGITDLETEGQFVYLDGGPLTYTNWKPGEPNN 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 110624774  921 VGKDKKCVYMTASREdWGDQRCLTALPYIC 950
Cdd:cd03591    84 AGGGEDCVEMYTSGK-WNDVACNLTRLFVC 112

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 57.00 E-value: 1.32e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  835 AEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAQeqhwWIGLHTSESDgrFRWTDGSIINFISWA 914
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAA----WIGLYRDVDS--WRWSDGSESSFRNWN 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 110624774  915 PGkprPVGKDKKCVYMTASReDWGDQRCLTALPYIC 950
Cdd:cd03602    75 TF---QPFGQGDCATMYSSG-RWYAALCSALKPFIC 106

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 57.00 E-value: 1.78e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  993 SRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDL-WIGLHASQRDFQWV--EQEPLMYANWAPGEPSGpspa 1069
Cdd:cd03592     8 EKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDINNEGTWVdtDKKELEYKNWAPGEPNN---- 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 110624774 1070 pSGNKptSCAVVLHSPsahfTGRWDDRSCT 1099
Cdd:cd03592    84 -GRNE--NCLEIYIKD----NGKWNDEPCS 106

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.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 56.29 E-value: 4.85e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  981 NKCFQVQGQepqsRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFD-------LWIGLHASQ----------R 1043
Cdd:cd03600     4 DACYTLHPQ----KLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRhgrgslrLWIGLQREPrqcsdpslplR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110624774 1044 DFQWVE-QEPLMYANWaPGEPSGPSPAPSgnkptsCAVVLHSPSAHFTGRWDDRSCTEETHGFICQ 1108
Cdd:cd03600    80 GFSWVTgDQDTDFSNW-LQEPAGTCTSPR------CVALSAAGSTPDNLKWKDGPCSARADGYLCK 138

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.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 55.46 E-value: 6.57e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1261 CPQGladsaWIPFREHCYSFHMELLlGHKEARQRCQR--AGGAVLSILDEMENVFVWEHLQSYEGQSRGAWLGMNFNPKG 1338
Cdd:cd03594     1 CPKG-----WLPYKGNCYGYFRQPL-SWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQS 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 110624774 1339 GTLVWQDNTAVNYSNWGPpglGPSMLSHNSCYWIQSNSG--LWRPGACTN 1386
Cdd:cd03594    75 RGWEWSDGSKLDYRSWDR---NPPYARGGYCAELSRSTGflKWNDANCEE 121

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.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 55.09 E-value: 9.46e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  393 CYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEV---EELWIGLNDLKLQMNFEWSDGSLVSFTHWH-- 467
Cdd:cd03596    11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVpgnWEVWLGINDMVAEGKWVDVNGSPISYFNWEre 90

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 110624774  468 -PFEPNNFRdsLEDCVTIWG-PEGRWNDSPCNQSLPSIC 504
Cdd:cd03596    91 iTAQPDGGK--RENCVALSSsAQGKWFDEDCRREKPYVC 127

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 60.10 E-value: 1.13e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774   388 PFQGHCYRLQAEKRSWQESKKACL-RGGGDLVSIHSMAELEFITKQIKQEVEE-LWIGLNDLKL--QMNFEWSDG-SLVS 462
Cdd:TIGR00864  326 EENGHCFQIVPEEAAWLDAQEQCLaRAGAALAIVDNDALQNFLARKVTHSLDRgVWIGFSDVNGaeKGPAHQGEAfEAEE 405

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110624774   463 FTHWHPFEPNNFRDSLedCVTIwGPEGRWNDSPCNQSLPSICK--------KAGQLSQGAAEED 518
Cdd:TIGR00864  406 CEEGLAGEPHPARAEH--CVRL-DPRGQCNSDLCNAPHAYVCElnpggpvpDAENFAMGAASFD 466

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 54.12 E-value: 2.31e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  521 CRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYnwegEYFWTALQDLNSTGSFFWLSGDE 600
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQ----DYQWIGLNDRTIEGDFRWSDGHP 76

                          90
                  ....*....|.
gi 110624774  601 VMYTHWNRDQP 611
Cdd:cd03588    77 LQFENWRPNQP 87

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 53.45 E-value: 2.45e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1290 EARQRCQRAGGAVLSILDEMENvfvwEHLQSYEGQ-SRGAWLGMNFNPKGGTLVWQDNTAVNYSNWG---PPGLGpsmlS 1365
Cdd:cd03591    15 DAQKLCSEAGGTLAMPRNAAEN----AAIASYVKKgNTYAFIGITDLETEGQFVYLDGGPLTYTNWKpgePNNAG----G 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 110624774 1366 HNSCYWIQSnSGLWRPGACtNITMGVVCKL 1395
Cdd:cd03591    87 GEDCVEMYT-SGKWNDVAC-NLTRLFVCEF 114

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

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 53.53 E-value: 3.11e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  972 CPSDWIQFLNKCFQVQGQePQSrvkWSEAQFSCEQ--QEAQLVTITNPLEQAFIT---ASLPNVTFDLWIGLHASQ--RD 1044
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQ-PLS---WSDAELFCQKygPGAHLASIHSPAEAAAIAsliSSYQKAYQPVWIGLHDPQqsRG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110624774 1045 FQWVEQEPLMYANWAPGEPSgpspapsgNKPTSCAvVLHSPSAhFTgRWDDRSCTEETHgFICQ 1108
Cdd:cd03594    77 WEWSDGSKLDYRSWDRNPPY--------ARGGYCA-ELSRSTG-FL-KWNDANCEERNP-FICK 128

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.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 53.22 E-value: 3.17e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  391 GHCYRLQAEKRSWQESKKACLR-GGGDLVSIHSMAELEFITKQIKQ-EVEELWIG--LNDLKLQMNFEWSDGSLVSFTHW 466
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTlNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 110624774  467 HPFEPNNFRdslEDCVTIWGPEGRWNDSPCNQSLPSIC 504
Cdd:cd03598    81 APGQPGNRR---GHCVELCTRGGHWRRAHCKLRRPFIC 115

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 52.96 E-value: 4.46e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  669 CPQGWasDTKLRYCYKVFsserlQDKKSWVQAQGACQELGAQLLSLASYEEEHFVANmlnkifgesepeiHEQHWFWIGL 748
Cdd:cd03588     1 CEEGW--DKFQGHCYRHF-----PDRETWEDAERRCREQQGHLSSIVTPEEQEFVNN-------------NAQDYQWIGL 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110624774  749 NRRDPRGgqSWRWSDGVGFSYHNFDRSRHDDDDIRG--CAVLDL-ASLQWVAMQCDTQLDWICK 809
Cdd:cd03588    61 NDRTIEG--DFRWSDGHPLQFENWRPNQPDNFFATGedCVVMIWhEEGEWNDVPCNYHLPFTCK 122

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.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 52.97 E-value: 7.62e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  989 QEPQSRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTF---DLWIGLHASQR----------DFQWVEQEPLMY 1055
Cdd:cd03595    19 QDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRAsdgDFWIGLRRSSQynvtssacssLYYWLDGSISTF 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110624774 1056 ANWAPGEPSGPSPApsgnkptsCAVVLHSPSA------HFTGRWDDRSCtEETHGFICQ 1108
Cdd:cd03595    99 RNWYVDEPSCGSEV--------CVVMYHQPSApagqggPYLFQWNDDNC-NMKNNFICK 148

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 51.27 E-value: 1.75e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  837 YKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLshnLQKFSRAQEQhwWIGLHTSESDGRFRWTDGSIINFISWAPG 916
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWL---LSNFGGYGAS--WIGASDAATEGTWKWSDGEESTYTNWGSG 77


                  ....*.
gi 110624774  917 KPRPVG 922
Cdd:cd03603    78 EPHNNG 83

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.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 51.20 E-value: 2.52e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1261 CPQgladsAWIPFREHCYSFhMELLLGHKEARQRCQ-----RAGGAVLSILDEMENVFVWEHLQSYEGQSR--GAWLGMN 1333
Cdd:cd03589     1 CPT-----FWTAFGGYCYRF-FGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVYDLFESSRGPDTpyGLWIGLH 74

                          90       100
                  ....*....|....*....|...
gi 110624774 1334 FNPKGGTLVWQDNTAVNYSNWGP 1356
Cdd:cd03589    75 DRTSEGPFEWTDGSPVDFTKWAG 97

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 50.37 E-value: 2.77e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  540 VTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIyNWEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRGG-- 617
Cdd:cd03591    11 KNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV-KKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNAGGGed 89

                          90       100
                  ....*....|....*....|..
gi 110624774  618 CVALATGsamGLWEVKNCTSFR 639
Cdd:cd03591    90 CVEMYTS---GKWNDVACNLTR 108

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.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 50.82 E-value: 3.24e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  521 CRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGS-----QLVTITNRFEQAFVSSLiynWEG-------EYFWTALQDLN 588
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIpgliaHLVSIHSQEENDFVYDL---FESsrgpdtpYGLWIGLHDRT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  589 STGSFFWLSGDEVMYTHWNRDQP--GYSRGGCVALA-TGSAMGLWEVKNCTSfRARYICR 645
Cdd:cd03589    78 SEGPFEWTDGSPVDFTKWAGGQPdnYGGNEDCVQMWrRGDAGQSWNDMPCDA-VFPYICK 136

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.

Pssm-ID: 153071 Cd Length: 119 Bit Score: 49.45 E-value: 7.25e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110624774  441 WIGLNDLKL-QMNFEWSDGSLVSFTH--WHPFEPNNfRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKK 506
Cdd:cd03601    52 WVGADNLQDgEYDFLWNDGVSLPTDSdlWAPNEPSN-PQSRQLCVQLWSKYNLLDDEYCGRAKRVICEK 119

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.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 49.89 E-value: 1.08e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  247 SCYQF-NFQST---LSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSST---LWIGL--------NDLDTSGGWQW 311
Cdd:cd03595    11 PCYKIaYFQDSrrrLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASdgdFWIGLrrssqynvTSSACSSLYYW 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110624774  312 SDNSPLKYLNWESDQPDNPSEEnCGVI--RTESSGG--------WQNRDCSIALPYVCK 360
Cdd:cd03595    91 LDGSISTFRNWYVDEPSCGSEV-CVVMyhQPSAPAGqggpylfqWNDDNCNMKNNFICK 148

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 48.96 E-value: 1.13e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  693 DKKSWVQAQGACQELGAQLLSLASYEEEHFVANMlnkiFGESEPeiheqhwFWIGLNRRDPRGgqSWRWSDGVGFSYHNF 772
Cdd:cd03603     8 GGMTWEAAQTLAESLGGHLVTINSAEENDWLLSN----FGGYGA-------SWIGASDAATEG--TWKWSDGEESTYTNW 74


                  ...
gi 110624774  773 DRS 775
Cdd:cd03603    75 GSG 77

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.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 48.22 E-value: 1.99e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  247 SCYQFnFQSTLSWREAWASCEQ-QGADLLSITEIHEQTYINGLLTGYSST-LWIGLNDLDTSGGWQ--WSDNSPLKYLNW 322
Cdd:cd03598     2 RCYRF-VKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAqVWIGGIITGKGRCRRfsWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 110624774  323 ESDQPdNPSEENCGVIRTEsSGGWQNRDCSIALPYVC 359
Cdd:cd03598    81 APGQP-GNRRGHCVELCTR-GGHWRRAHCKLRRPFIC 115

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.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 48.15 E-value: 2.80e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  837 YKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAqEQHWWIGLHTSESDGRFRWTDGSIINFISW--- 913
Cdd:cd03596    12 YLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPG-NWEVWLGINDMVAEGKWVDVNGSPISYFNWere 90

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 110624774  914 APGKPRPvGKDKKCVYMTASRE-DWGDQRCLTALPYIC 950
Cdd:cd03596    91 ITAQPDG-GKRENCVALSSSAQgKWFDEDCRREKPYVC 127

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 46.98 E-value: 3.95e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  997 WSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQRDFQWVEQEPLMYANWAPGEPSGPSpapsgnkpt 1076
Cdd:cd03602    12 WSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSDGSESSFRNWNTFQPFGQG--------- 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 110624774 1077 SCAVVLhspsahFTGRWDDRSCTEETHgFIC 1107
Cdd:cd03602    83 DCATMY------SSGRWYAALCSALKP-FIC 106

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 47.19 E-value: 5.51e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1267 DSAWIPFREHCYSfHMELLLGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEgqsrgaWLGMNFNPKGGTLVWQDN 1346
Cdd:cd03588     2 EEGWDKFQGHCYR-HFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ------WIGLNDRTIEGDFRWSDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 110624774 1347 TAVNYSNWGPPGLGPSMLSHNSC-YWIQSNSGLWRPGACtNITMGVVCK 1394
Cdd:cd03588    75 HPLQFENWRPNQPDNFFATGEDCvVMIWHEEGEWNDVPC-NYHLPFTCK 122

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.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 46.81 E-value: 1.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  680 RYCYKVFSSERLQDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIfGESEPEiheqhwFWIGLNRRDPRGGQS- 758
Cdd:cd03595    10 KPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTL-RASDGD------FWIGLRRSSQYNVTSs 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  759 -----WRWSDGVGFSYHNFdrsrHDDDDIRG---CAVL-----------DLASLQWVAMQCDTQLDWICK 809
Cdd:cd03595    83 acsslYYWLDGSISTFRNW----YVDEPSCGsevCVVMyhqpsapagqgGPYLFQWNDDNCNMKNNFICK 148

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 44.29 E-value: 3.38e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  533 YWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIyNWEGEYFWTALqdLNSTGSFFWLSGDEVMYTHWNRDQPG 612
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLS-RVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQPF 79

                          90       100
                  ....*....|....*....|....*..
gi 110624774  613 ySRGGCVALATGsamGLWEVKNCTSFR 639
Cdd:cd03602    80 -GQGDCATMYSS---GRWYAALCSALK 102

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 44.21 E-value: 4.34e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1137 FRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGEEGSRRYSWVSEEPLNYVGWQDGEPQQ 1216
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNN 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 110624774 1217 PGG---CTYVDVDGAWRTTSCDTKLQgAVC 1243
Cdd:cd03591    84 AGGgedCVEMYTSGKWNDVACNLTRL-FVC 112

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 43.95 E-value: 5.31e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1290 EARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGqsrgAWLGMNFNPKGGTLVWQDNTAVNYSNWG---PPGLGPSMLSH 1366
Cdd:cd03603    14 AAQTLAESLGGHLVTINSAEENDWLLSNFGGYGA----SWIGASDAATEGTWKWSDGEESTYTNWGsgePHNNGGGNEDY 89

                          90       100
                  ....*....|....*....|....*.
gi 110624774 1367 NSCYWIQSNSGLWRPGACTNITMGVV 1392
Cdd:cd03603    90 AAINHFPGISGKWNDLANSYNTLGYV 115

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 45.49 E-value: 8.11e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  668 SCPQGWasdtkLRYCYKVFSSErlQDKKSWVQAQGACQELGAQLLSLASYEEEHFVanmlnKIFGESEPEiheqhwfWIG 747
Cdd:PHA02642   87 TCPKGW-----IGFGYKCFYFS--EDSKNWTFGNTFCTSLGATLVKVETEEELNFL-----KRYKDSSDH-------WIG 147

                          90       100
                  ....*....|....*....|.
gi 110624774  748 LNRRDprGGQSWRWSDGVGFS 768
Cdd:PHA02642  148 LNRES--SNHPWKWADNSNYN 166

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.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 43.21 E-value: 1.09e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1137 FRLLQKPLRWHDALLLCES-RNASLAYVPDPYT-QAFLTQAARGLRTPLWIG--LAGEEGSRRYSWVSEEPLNYVGWQDG 1212
Cdd:cd03598     4 YRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFnYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYWAPG 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 110624774 1213 EP-QQPGGCTYVDV-DGAWRTTSCDtKLQGAVC 1243
Cdd:cd03598    84 QPgNRRGHCVELCTrGGHWRRAHCK-LRRPFIC 115

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 42.75 E-value: 1.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  845 TWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAqeqHWWIGLHTSESDGRFRWTDGSIINFISWAPGKPRPvGKD 924
Cdd:cd03592    11 TFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLG---YYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPNN-GRN 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 110624774  925 KKCV--YMTASREdWGDQRCLTALPYICKR 952
Cdd:cd03592    87 ENCLeiYIKDNGK-WNDEPCSKKKSAICYT 115

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.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 43.19 E-value: 2.02e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  246 DSCYQFNFQsTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTG-------YSSTLWIGLND-----LDTSG---GWQ 310
Cdd:cd03600     4 DACYTLHPQ-KLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAgpgrhgrGSLRLWIGLQReprqcSDPSLplrGFS 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110624774  311 W-SDNSPLKYLNWESDQPDNPSEENCGVIRTESSG----GWQNRDCSIALP-YVCK 360
Cdd:cd03600    83 WvTGDQDTDFSNWLQEPAGTCTSPRCVALSAAGSTpdnlKWKDGPCSARADgYLCK 138

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 41.98 E-value: 2.23e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1136 TFRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGEEGSrrYSWVSEEPLNYVGWQDGEPQ 1215
Cdd:cd03602     2 TFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDS--WRWSDGSESSFRNWNTFQPF 79

                          90
                  ....*....|....*....
gi 110624774 1216 QPGGCTYVDVDGAWRTTSC 1234
Cdd:cd03602    80 GQGDCATMYSSGRWYAALC 98

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 42.36 E-value: 2.33e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1142 KPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPL-WIGL--AGEEGsrrySWVS--EEPLNYVGWQDGEPQQ 1216
Cdd:cd03592     8 EKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGndINNEG----TWVDtdKKELEYKNWAPGEPNN 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 110624774 1217 PGG--C--TYVDVDGAWRTTSCDTKLqGAVC 1243
Cdd:cd03592    84 GRNenCleIYIKDNGKWNDEPCSKKK-SAIC 113

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.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 42.57 E-value: 3.54e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  521 CRKGWtwhSPSCYWLGEDQ-----VTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNW---EGEyFWTAL---QDLNS 589
Cdd:cd03595     4 CRRGT---EKPCYKIAYFQdsrrrLNFEEARQACREDGGELLSIESENEQKLIERFIQTLrasDGD-FWIGLrrsSQYNV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  590 TGS-----FFWLSGDEVMYTHWNRDQPGYSRGGCVAL---------ATGSAMGLWEVKNCTSfRARYICR 645
Cdd:cd03595    80 TSSacsslYYWLDGSISTFRNWYVDEPSCGSEVCVVMyhqpsapagQGGPYLFQWNDDNCNM-KNNFICK 148

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 43.57 E-value: 3.75e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  814 TDVREPD----DSPQGrreWLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFlshnLQKFSRAQEQhwWI 889
Cdd:PHA02642   76 SDTQEPTikyvTCPKG---WIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNF----LKRYKDSSDH--WI 146

                          90       100
                  ....*....|....*....|
gi 110624774  890 GLHTSESDGRFRWTDGSIIN 909
Cdd:PHA02642  147 GLNRESSNHPWKWADNSNYN 166

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 41.55 E-value: 4.39e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1261 CPQGladsaWIPFREHCYSFHMElLLGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGqsrgaWLGMNFNPKGGT 1340
Cdd:cd03593     1 CPKD-----WICYGNKCYYFSME-KKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY-----WIGLSREKSEKP 69

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 110624774 1341 LVWQDNTAvnYSNW-GPPGLGPSMlshnSCYWIQSN 1375
Cdd:cd03593    70 WKWIDGSP--LNNLfNIRGSTKSG----NCAYLSST 99

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.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 42.18 E-value: 5.22e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  848 QAQRICTWFQAELTSVHSQAELDFLSHNLQKfSRAQEQHWWIGLHTSESDG--------RFRWTDGSIINFISWAPGKPR 919
Cdd:cd03595    29 EARQACREDGGELLSIESENEQKLIERFIQT-LRASDGDFWIGLRRSSQYNvtssacssLYYWLDGSISTFRNWYVDEPS 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 110624774  920 pVGKDkKCVYM-----------TASREDWGDQRCLTALPYICK 951
Cdd:cd03595   108 -CGSE-VCVVMyhqpsapagqgGPYLFQWNDDNCNMKNNFICK 148

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 40.82 E-value: 5.39e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  690 RLQDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIFGEsepeiheqhwFWIGLNRrdprGGQSWRWSDGVGFSY 769
Cdd:cd03602     5 LVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSA----------AWIGLYR----DVDSWRWSDGSESSF 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110624774  770 HNFDRsrhDDDDIRG-CAVLDLASlQWVAMQCDTQLDWIC 808
Cdd:cd03602    71 RNWNT---FQPFGQGdCATMYSSG-RWYAALCSALKPFIC 106

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.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 41.28 E-value: 5.79e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  993 SRVKWSEAQFSCEQ-QEAQLVTITNPL--EQAFITASLPNVTfDLWIG----LHASQRDFQWVEQEPLMYANWAPGEPsg 1065
Cdd:cd03598     9 SPRTFRDAQVICRRcYRGNLASIHSFAfnYRVQRLVSTLNQA-QVWIGgiitGKGRCRRFSWVDGSVWNYAYWAPGQP-- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 110624774 1066 pspapsGNKPTSCAVVLHSpsahfTGRWDDRSCtEETHGFICQ 1108
Cdd:cd03598    86 ------GNRRGHCVELCTR-----GGHWRRAHC-KLRRPFICS 116

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 40.82 E-value: 6.70e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  540 VTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRG-GC 618
Cdd:cd03592    10 MTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPNNGRNeNC 89

                          90       100
                  ....*....|....*....|....*.
gi 110624774  619 VALATgSAMGLWEVKNCTSfRARYIC 644
Cdd:cd03592    90 LEIYI-KDNGKWNDEPCSK-KKSAIC 113

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 42.80 E-value: 7.32e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  380 VECEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQikQEVEELWIGLNDLKLQMNFEWSDGS 459
Cdd:PHA02642   86 VTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRY--KDSSDHWIGLNRESSNHPWKWADNS 163

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.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 40.82 E-value: 1.03e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1137 FRLLQKPLRWHDALLLCESRNAS--LAYVPDPYTQAFLTQAARGLRT---PLWIGLAGEEGSRRYSWVSEEPLNYVGWQD 1211
Cdd:cd03594    13 YGYFRQPLSWSDAELFCQKYGPGahLASIHSPAEAAAIASLISSYQKayqPVWIGLHDPQQSRGWEWSDGSKLDYRSWDR 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 110624774 1212 GEP-QQPGGCTYVDVDGA---WRTTSCDTKLQ 1239
Cdd:cd03594    93 NPPyARGGYCAELSRSTGflkWNDANCEERNP 124

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.

Pssm-ID: 153071 Cd Length: 119 Bit Score: 40.60 E-value: 1.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1032 FDLWIGLHASQR---DFQWVEQE--PLMYANWAPGEPSGPSpapsgnKPTSCAVVLHSPsahftGRWDDRSCtEETHGFI 1106
Cdd:cd03601    49 HGYWVGADNLQDgeyDFLWNDGVslPTDSDLWAPNEPSNPQ------SRQLCVQLWSKY-----NLLDDEYC-GRAKRVI 116


                  ...
gi 110624774 1107 CQK 1109
Cdd:cd03601   117 CEK 119

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.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 40.49 E-value: 1.39e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  528 HSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGEY------FWTALQ--------DLNSTGSF 593
Cdd:cd03600     2 VSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRHgrgslrLWIGLQreprqcsdPSLPLRGF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110624774  594 FWLSGDE-VMYTHWNRDQPGY-SRGGCVAL-ATGSAMGL--WEVKNCTSFRARYIC 644
Cdd:cd03600    82 SWVTGDQdTDFSNWLQEPAGTcTSPRCVALsAAGSTPDNlkWKDGPCSARADGYLC 137

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.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 39.74 E-value: 1.69e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  531 SCYWLGEDQVTYSEARRLCTD-HGSQLVTITNRFEQAFVSSLIYNWEGEYFWTALQDLNSTGS--FFWLSGDEVMYTHWN 607
Cdd:cd03598     2 RCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCrrFSWVDGSVWNYAYWA 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 110624774  608 RDQPGYSRGGCVALATGSamGLWEVKNCTSFRArYIC 644
Cdd:cd03598    82 PGQPGNRRGHCVELCTRG--GHWRRAHCKLRRP-FIC 115

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467318 [Multi-domain] Cd Length: 127 Bit Score: 39.67 E-value: 2.01e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 110624774   68 CNTSLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTTASLGMyeCD 113
Cdd:cd23440    75 CHGSGGSQQWRFKKDNRLYNPASGQCLAASKNGTSGYVTMDI--CS 118

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 39.21 E-value: 2.84e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774 1144 LRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTpLWIGLAGEEGSRRYSWVSEEPLN--YVGWQDGEPQQPGG-- 1219
Cdd:cd03590    20 KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEETEGEWKWVDGTPLNssKTFWHPGEPNNWGGgg 98

                          90       100
                  ....*....|....*....|....*..
gi 110624774 1220 --CTY-VDVDGAWRTTSCDTKLQgAVC 1243
Cdd:cd03590    99 edCAElVYDSGGWNDVPCNLEYR-WIC 124

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 38.17 E-value: 5.60e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110624774 1146 WHDALLLCESRNASLAYVPDPYTQAFLTQAARGlRTPLWIGLAGEEGSRRYSWVSEEPLNYVGWQDGEPQQPGG 1219
Cdd:cd03603    12 WEAAQTLAESLGGHLVTINSAEENDWLLSNFGG-YGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNNGG 84

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.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 38.57 E-value: 6.57e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624774  682 CYKVFSSerlqdKKSWVQAQGACQELGAQLLSLASYEEehfvANMLNKIFGESE-PEIHEQHWFWIGLNRR--------D 752
Cdd:cd03600     6 CYTLHPQ-----KLTFLEAQRSCIELGGNLATVRSGEE----ADVVSLLLAAGPgRHGRGSLRLWIGLQREprqcsdpsL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110624774  753 PRGGQSWRWSDGvGFSYHNFDRSRHDDDDIRGCAVLDLAS-----LQWVAMQCDTQLD-WICK 809
Cdd:cd03600    77 PLRGFSWVTGDQ-DTDFSNWLQEPAGTCTSPRCVALSAAGstpdnLKWKDGPCSARADgYLCK 138

C-type lectin-like protein; Provisional

Pssm-ID: 222982 [Multi-domain] Cd Length: 157 Bit Score: 38.69 E-value: 8.67e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110624774  521 CRKGWTWHSPSCYWLGED-QVTYSEARRlCTDHGSQLVTITNRFEQAFVSS 570
Cdd:PHA03097   46 CRSGWVGYNNKCYTFSENiTNKHLAIER-CADMDGILTLIDDQKEVLFVSR 95