C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442  107 CPKDWRLFGSHCYLVPTvsSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIGLWDT-GHRQWQWVDQTP 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFST--EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6753442  186 YEESITFWHNGEPSS---GNEKCATIIYRWktgWGWNDISCSLKQKSVCQM 233
Cdd:cd03590  79 LNSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWICEK 126

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442  107 CPKDWRLFGSHCYLVPTvsSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIGLWDT-GHRQWQWVDQTP 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFST--EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6753442  186 YEESITFWHNGEPSS---GNEKCATIIYRWktgWGWNDISCSLKQKSVCQM 233
Cdd:cd03590  79 LNSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWICEK 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442    127 SASWNKSEENCSRMGAHLVVIQSQEEQDFITGIL-DTHAAYFIGLWDTGH-RQWQWVDQTPYeeSITFWhNGEPS--SGN 202
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLkKSNKYFWIGLTDRKNeGTWKWVDGSPV--NYTNW-APEPNnnGEN 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6753442    203 EKCATIIYRWktgWGWNDISCSLKQKSVCQM 233
Cdd:pfam00059  78 EDCVELSSSS---GKWNDENCNSKNPFVCEK 105

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442     107 CPKDWRLF--GSHCYLVptVSSSASWNKSEENC-SRMGAHLVVIQSQEEQDFITGILdTHA---AYFIGLWD---TGHRQ 177
Cdd:TIGR00864  318 CPKDGEIFeeNGHCFQI--VPEEAAWLDAQEQClARAGAALAIVDNDALQNFLARKV-THSldrGVWIGFSDvngAEKGP 394

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 6753442     178 WQWVDQTPYEESITfWHNGEPSSGN-EKCATIiyrWKTGWGWNDiSCSLKQKSVCQMK 234
Cdd:TIGR00864  395 AHQGEAFEAEECEE-GLAGEPHPARaEHCVRL---DPRGQCNSD-LCNAPHAYVCELN 447

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442  107 CPKDWRLFGSHCYLVPTvsSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIGLWDT-GHRQWQWVDQTP 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFST--EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6753442  186 YEESITFWHNGEPSS---GNEKCATIIYRWktgWGWNDISCSLKQKSVCQM 233
Cdd:cd03590  79 LNSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWICEK 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442  117 HCYLVptVSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGIL--DTHAAYFIGLWDTGH-RQWQWVDQTPYeESITFW 193
Cdd:cd00037   1 SCYKF--STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkkSSSSDVWIGLNDLSSeGTWKWSDGSPL-VDYTNW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6753442  194 HNGEP-SSGNEKCATIiyRWKTGWGWNDISCSLKQKSVCQM 233
Cdd:cd00037  78 APGEPnPGGSEDCVVL--SSSSDGKWNDVSCSSKLPFICEK 116

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 6753442  107 CPKDWRLFGSHCYLVptVSSSASWNKSEENC-----SRMGAHLVVIQSQEEQDFIT----GILDTHAAY--FIGLWDTGH 175
Cdd:cd03589   1 CPTFWTAFGGYCYRF--FGDRLTWEEAELRCrsfsiPGLIAHLVSIHSQEENDFVYdlfeSSRGPDTPYglWIGLHDRTS 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6753442  176 R-QWQWVDQTPYEesITFWHNGEPSS--GNEKCATIIYRWKTGWGWNDISCSLKQKSVCQM 233
Cdd:cd03589  79 EgPFEWTDGSPVD--FTKWAGGQPDNygGNEDCVQMWRRGDAGQSWNDMPCDAVFPYICKM 137

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 6753442  107 CPKDWRLFGSHCYLVptVSSSASWNKSEENCSRM--GAHLVVIQSQEEQDFITG-ILDTHAAY---FIGLWD-TGHRQWQ 179
Cdd:cd03594   1 CPKGWLPYKGNCYGY--FRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASlISSYQKAYqpvWIGLHDpQQSRGWE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6753442  180 WVDQTPYEESItfWHNGEPSSGNEKCATIiyRWKTGW-GWNDISCSLKQKSVCQ 232
Cdd:cd03594  79 WSDGSKLDYRS--WDRNPPYARGGYCAEL--SRSTGFlKWNDANCEERNPFICK 128

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 6753442  117 HCYLVptVSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIGLWDTGH-RQWQWVDQTpyEESITFWHN 195
Cdd:cd03603   1 HFYKF--VDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASDAATeGTWKWSDGE--ESTYTNWGS 76

                        90       100
                ....*....|....*....|....*...
gi 6753442  196 GEP---SSGNEKCATIIYRWKTGWGWND 220
Cdd:cd03603  77 GEPhnnGGGNEDYAAINHFPGISGKWND 104

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442  107 CPKDWRLFGSHCYlvPTVSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGilDTHAAYFIGLWD-TGHRQWQWVDQTP 185
Cdd:cd03588   1 CEEGWDKFQGHCY--RHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNN--NAQDYQWIGLNDrTIEGDFRWSDGHP 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6753442  186 YEesITFWHNGEPSS---GNEKCATIIyrWKTGWGWNDISCSLKQKSVCQM 233
Cdd:cd03588  77 LQ--FENWRPNQPDNffaTGEDCVVMI--WHEEGEWNDVPCNYHLPFTCKK 123

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753442   107 CPKDWRLFGSHCYLVPtvSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDThAAYFIGL-WDTGHRQWQWVDQTP 185
Cdd:PHA02642  88 CPKGWIGFGYKCFYFS--EDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDS-SDHWIGLnRESSNHPWKWADNSN 164

                         90
                 ....*....|....*...
gi 6753442   186 YEESITFWHNGEPSSGNE 203
Cdd:PHA02642 165 YNASFVITGTGECAYLND 182

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
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6753442  176 RQWQWVDQTPYEESitFWHNGEPSSGNEKCATIIyrwKTGWGWNDISCSLKQKSVCQ 232
Cdd:cd03598  65 RRFSWVDGSVWNYA--YWAPGQPGNRRGHCVELC---TRGGHWRRAHCKLRRPFICS 116