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 1907141435 108 CNYVLVRTPETFDKAQRVCRRCYRGNLASVHSYSFNYQIQNLARKINQSIVWIGGILRGWF-WKKFCWMDGSCWDFGYWA 186
Cdd:cd03598     2 RCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGrCRRFSWVDGSVWNYAYWA 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907141435 187 PGQPGSGGGHCVTLCTKGGHWRRASCKSHLPFICSF 222
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 1907141435 108 CNYVLVRTPETFDKAQRVCRRCYRGNLASVHSYSFNYQIQNLARKINQSIVWIGGILRGWF-WKKFCWMDGSCWDFGYWA 186
Cdd:cd03598     2 RCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGrCRRFSWVDGSVWNYAYWA 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907141435 187 PGQPGSGGGHCVTLCTKGGHWRRASCKSHLPFICSF 222
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 1907141435 116 PETFDKAQRVCRRcYRGNLASVHSYSFNYQIQNLARKINQSIvWIGGILRGWFwKKFCWMDGSCWDFGYWAP-GQPGSGG 194
Cdd:pfam00059   1 SKTWDEAREACRK-LGGHLVSINSAEELDFLSSTLKKSNKYF-WIGLTDRKNE-GTWKWVDGSPVNYTNWAPePNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 1907141435 195 GHCVTLCTKGGHWRRASCKSHLPFICSF 222
Cdd:pfam00059  78 EDCVELSSSSGKWNDENCNSKNPFVCEK 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 1907141435 108 CNYVLVRTPETFDKAQRVCRRCYRGNLASVHSYSFNYQIQNLARKINQSIVWIGGILRGWF-WKKFCWMDGSCWDFGYWA 186
Cdd:cd03598     2 RCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGrCRRFSWVDGSVWNYAYWA 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907141435 187 PGQPGSGGGHCVTLCTKGGHWRRASCKSHLPFICSF 222
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 1907141435 107 SCnYVLVRTPETFDKAQRVCRRcYRGNLASVHSYSFNYQIQNLARKINQSIVWIGGIlRGWFWKKFCWMDGS-CWDFGYW 185
Cdd:cd00037     1 SC-YKFSTEKLTWEEAQEYCRS-LGGHLASIHSEEENDFLASLLKKSSSSDVWIGLN-DLSSEGTWKWSDGSpLVDYTNW 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907141435 186 APGQP-GSGGGHCVTL-CTKGGHWRRASCKSHLPFICSF 222
Cdd:cd00037    78 APGEPnPGGSEDCVVLsSSSDGKWNDVSCSSKLPFICEK 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 1907141435 107 SCnYVLVRTPETFDKAQRVCRRCYRG-NLASVHSYSfnyQIQNLARKINQSI-----VWIGgiLRGWF----WKkfcWMD 176
Cdd:cd03594    11 NC-YGYFRQPLSWSDAELFCQKYGPGaHLASIHSPA---EAAAIASLISSYQkayqpVWIG--LHDPQqsrgWE---WSD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907141435 177 GSCWDFGYWAPGQPGSGGGHCVTLCTKGGH--WRRASCKSHLPFICSF 222
Cdd:cd03594    82 GSKLDYRSWDRNPPYARGGYCAELSRSTGFlkWNDANCEERNPFICKY 129

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 1907141435 110 YVLVRTPETFDKAQRVCRRcYRGNLASVHSYSFNYQIQNLARKINqSIVWIgGILRGWFWKKFCWMDGSCWDFGYWAPGQ 189
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSE-AGGTLAMPRNAAENAAIASYVKKGN-TYAFI-GITDLETEGQFVYLDGGPLTYTNWKPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907141435 190 PGSGGGH--CVTLCTkGGHWRRASCKSHLPFICSF 222
Cdd:cd03591    81 PNNAGGGedCVEMYT-SGKWNDVACNLTRLFVCEF 114

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141435 109 NYVLVRTPETFDKAQRVCRRcyRG-NLASVHSYSFNYQIQNLARKINQSIVWIGG--ILRGWFWKKfcwMDGSCWDFGYW 185
Cdd:cd03592     2 TYHYSTEKMTFNEAVKYCKS--RGtDLVAIQNAEENALLNGFALKYNLGYYWIDGndINNEGTWVD---TDKKELEYKNW 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907141435 186 APGQP-GSGGGHCVT-LCTKGGHWRRASCKSHLPFIC 220
Cdd:cd03592    77 APGEPnNGRNENCLEiYIKDNGKWNDEPCSKKKSAIC 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141435 110 YVLVRTPETFDKAQRVCRRcYRGNLASVHSYSFNYQIQNLARKINQSivWIGGILRG--WFWKkfcWMDGSCWDFGYWAP 187
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAES-LGGHLVTINSAEENDWLLSNFGGYGAS--WIGASDAAteGTWK---WSDGEESTYTNWGS 76

                  ....*...
gi 1907141435 188 GQPGSGGG 195
Cdd:cd03603    77 GEPHNNGG 84