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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 110 CRYLLVRTPKTFAEAQNVCSRCYGGNLVSIHDFNFNYRIQCCTSTVNQAQVWIGGNLRGWFLWKRFCWTDGSHWNFAYWS 189
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWVDGSVWNYAYWA 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 223633965 190 PGQPGNGQGSCVALCTKGGYWRRAQCDKQLPFVCSF 225
Cdd:cd03598   82 PGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFICSY 117

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 110 CRYLLVRTPKTFAEAQNVCSRCYGGNLVSIHDFNFNYRIQCCTSTVNQAQVWIGGNLRGWFLWKRFCWTDGSHWNFAYWS 189
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWVDGSVWNYAYWA 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 223633965 190 PGQPGNGQGSCVALCTKGGYWRRAQCDKQLPFVCSF 225
Cdd:cd03598   82 PGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFICSY 117

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965  118 PKTFAEAQNVCSRcYGGNLVSIHDFNFNYRIQcctSTVNQAQV--WIG----GNLRGWflwkrfCWTDGSHWNFAYWSPG 191
Cdd:pfam00059   1 SKTWDEAREACRK-LGGHLVSINSAEELDFLS---STLKKSNKyfWIGltdrKNEGTW------KWVDGSPVNYTNWAPE 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 223633965  192 QPGNGQ-GSCVALCTKGGYWRRAQCDKQLPFVCSF 225
Cdd:pfam00059  71 PNNNGEnEDCVELSSSSGKWNDENCNSKNPFVCEK 105

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 110 CRYLLVRTPKTFAEAQNVCSRCYGGNLVSIHDFNFNYRIQCCTSTVNQAQVWIGGNLRGWFLWKRFCWTDGSHWNFAYWS 189
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWVDGSVWNYAYWA 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 223633965 190 PGQPGNGQGSCVALCTKGGYWRRAQCDKQLPFVCSF 225
Cdd:cd03598   82 PGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFICSY 117

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 112 YLLVRTPKTFAEAQNVCSRcYGGNLVSIHDFNFNYRIQCCTSTVNQAQVWIGGNLRGwfLWKRFCWTDGS-HWNFAYWSP 190
Cdd:cd00037    3 YKFSTEKLTWEEAQEYCRS-LGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLS--SEGTWKWSDGSpLVDYTNWAP 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 223633965 191 GQP-GNGQGSCVAL-CTKGGYWRRAQCDKQLPFVCSF 225
Cdd:cd00037   80 GEPnPGGSEDCVVLsSSSDGKWNDVSCSSKLPFICEK 116

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 112 YLLVRTPKTFAEAQNVCSRCY-GGNLVSIHDFNfnyRIQCCTSTVNQAQ-----VWIGGN-LRGWFLWKrfcWTDGSHWN 184
Cdd:cd03594   13 YGYFRQPLSWSDAELFCQKYGpGAHLASIHSPA---EAAAIASLISSYQkayqpVWIGLHdPQQSRGWE---WSDGSKLD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 223633965 185 FAYWSPGQPGNGQGSCVALCTKGGY--WRRAQCDKQLPFVCSF 225
Cdd:cd03594   87 YRSWDRNPPYARGGYCAELSRSTGFlkWNDANCEERNPFICKY 129

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 119 KTFAEAQNVC----SRCYGGNLVSIH-----DFNFNYrIQCCTSTVNQAQVWIGGNLR---GWFLWkrfcwTDGSHWNFA 186
Cdd:cd03589   20 LTWEEAELRCrsfsIPGLIAHLVSIHsqeenDFVYDL-FESSRGPDTPYGLWIGLHDRtseGPFEW-----TDGSPVDFT 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 223633965 187 YWSPGQPGNGQGS--CVALC---TKGGYWRRAQCDKQLPFVC 223
Cdd:cd03589   94 KWAGGQPDNYGGNedCVQMWrrgDAGQSWNDMPCDAVFPYIC 135

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 112 YLLVRTPKTFAEAQNVCSRcYGGNLVSIHDFNFNYRIQcctSTVNQA--QVWIGGNLRGwfLWKRFCWTDGSHWNFAYWS 189
Cdd:cd03591    4 FVTNGEEKNFDDAQKLCSE-AGGTLAMPRNAAENAAIA---SYVKKGntYAFIGITDLE--TEGQFVYLDGGPLTYTNWK 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 223633965 190 PGQPgNGQGS---CVALCTKGGyWRRAQCDKQLPFVCSF 225
Cdd:cd03591   78 PGEP-NNAGGgedCVEMYTSGK-WNDVACNLTRLFVCEF 114

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 119 KTFAEAQNVCsRCYGGNLVSIhdfnFNYRIQCCTSTVNQAQVWIGGNLRGwfLWKRFCWTDGSHWNFAYWSPGQPGN--- 195
Cdd:cd03588   20 ETWEDAERRC-REQQGHLSSI----VTPEEQEFVNNNAQDYQWIGLNDRT--IEGDFRWSDGHPLQFENWRPNQPDNffa 92

                         90       100
                 ....*....|....*....|....*....
gi 223633965 196 -GQGSCVALCTKGGYWRRAQCDKQLPFVC 223
Cdd:cd03588   93 tGEDCVVMIWHEEGEWNDVPCNYHLPFTC 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223633965 112 YLLVRTPKTFAEAQNVCSRcYGGNLVSIHDFNFNYRIQ--CCTSTVNQAQVWIGGNLR---GWFLWkrfcwTDGSHWNFA 186
Cdd:cd03596   12 YLVSEETKHYHEASEDCIA-RGGTLATPRDSDENDALRdyVKASVPGNWEVWLGINDMvaeGKWVD-----VNGSPISYF 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 223633965 187 YW---SPGQPGNG-QGSCVALCTKG-GYWRRAQCDKQLPFVCSF 225
Cdd:cd03596   86 NWereITAQPDGGkRENCVALSSSAqGKWFDEDCRREKPYVCEF 129