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 767991504 184 CPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQKYL-----GSAYTWMGLSDP--EGAWKWVDGTDYA 256
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIskilsGNRSYWIGLSDEetEGEWKWVDGTPLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767991504 257 TGFQNWKPGQPDDWQghglGGGEDCAHF-HPDGRWNDDVCQRPYHWVCE 304
Cdd:cd03590   81 SSKTFWHPGEPNNWG----GGGEDCAELvYDSGGWNDVPCNLEYRWICE 125

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 767991504 184 CPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQKYL-----GSAYTWMGLSDP--EGAWKWVDGTDYA 256
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIskilsGNRSYWIGLSDEetEGEWKWVDGTPLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767991504 257 TGFQNWKPGQPDDWQghglGGGEDCAHF-HPDGRWNDDVCQRPYHWVCE 304
Cdd:cd03590   81 SSKTFWHPGEPNNWG----GGGEDCAELvYDSGGWNDVPCNLEYRWICE 125

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504   184 CPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQKYL--------GSAYTWMGLSDP--EGAWKWVDGT 253
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllknsgSSDYYWIGLSDPdsNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767991504   254 dYATGFQNWKPGQPDdwqghglGGGEDCAHFHPD-GRWNDDVCQRPYHWVCE 304
Cdd:smart00034  81 -GPVSYSNWAPGEPN-------NSSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124

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 767991504   137 HCPSVCVPVHSemllrVQQLVQDLKKLTCQVA-TLNNNGEE-ASTEGTCCPVNWVEHQDS--CYWFSHSGMSWAEAEKYC 212
Cdd:TIGR00864  274 HCPSLVQADES-----LDLSIQNRGGSDLDAAwKITAHGEEpAKASHPHCPKDGEIFEENghCFQIVPEEAAWLDAQEQC 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504   213 QLK-NAHLVVINSREEQKYLGSAYT-------WMGLSDPEGAWK----WVDGTDYATGfQNWKPGQPDdwqghgLGGGED 280
Cdd:TIGR00864  349 LARaGAALAIVDNDALQNFLARKVThsldrgvWIGFSDVNGAEKgpahQGEAFEAEEC-EEGLAGEPH------PARAEH 421

                          170       180       190
                   ....*....|....*....|....*....|....
gi 767991504   281 CAHFHPDGRWNDDVCQRPYHWVCEAGLGQTSQES 314
Cdd:TIGR00864  422 CVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDA 455

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 767991504 184 CPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQKYL-----GSAYTWMGLSDP--EGAWKWVDGTDYA 256
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIskilsGNRSYWIGLSDEetEGEWKWVDGTPLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767991504 257 TGFQNWKPGQPDDWQghglGGGEDCAHF-HPDGRWNDDVCQRPYHWVCE 304
Cdd:cd03590   81 SSKTFWHPGEPNNWG----GGGEDCAELvYDSGGWNDVPCNLEYRWICE 125

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504   184 CPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQKYL--------GSAYTWMGLSDP--EGAWKWVDGT 253
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllknsgSSDYYWIGLSDPdsNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767991504   254 dYATGFQNWKPGQPDdwqghglGGGEDCAHFHPD-GRWNDDVCQRPYHWVCE 304
Cdd:smart00034  81 -GPVSYSNWAPGEPN-------NSSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504 184 CPVNWVEHQDSCYWFSHSGMSWAEAEKYCQL-----KNAHLVVINSREEQKYLGSAY-----------TWMGLSDP--EG 245
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFessrgpdtpygLWIGLHDRtsEG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767991504 246 AWKWVDGTDYatGFQNWKPGQPDDWqghglGGGEDCAHF----HPDGRWNDDVCQRPYHWVC 303
Cdd:cd03589   81 PFEWTDGSPV--DFTKWAGGQPDNY-----GGNEDCVQMwrrgDAGQSWNDMPCDAVFPYIC 135

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504  203 MSWAEAEKYCQLKNAHLVVINSREEQKYL------GSAYTWMGLSD--PEGAWKWVDGTDYatGFQNWKPGQPDDwqghg 274
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLsstlkkSNKYFWIGLTDrkNEGTWKWVDGSPV--NYTNWAPEPNNN----- 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767991504  275 lGGGEDCAHFH-PDGRWNDDVCQRPYHWVCE 304
Cdd:pfam00059  75 -GENEDCVELSsSSGKWNDENCNSKNPFVCE 104

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 767991504 196 YWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQKYL-------GSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPD 268
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLngfalkyNLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767991504 269 DwqghglGGGEDC--AHFHPDGRWNDDVCQRPYHWVCE 304
Cdd:cd03592   83 N------GRNENCleIYIKDNGKWNDEPCSKKKSAICY 114

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 767991504 203 MSWAEAEKYCQLKNAHLVVINSREEQKYL------GSAYTWMGLSD--PEGAWKWVDGTdyATGFQNWKPGQPDDWqghg 274
Cdd:cd03591   11 KNFDDAQKLCSEAGGTLAMPRNAAENAAIasyvkkGNTYAFIGITDleTEGQFVYLDGG--PLTYTNWKPGEPNNA---- 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 767991504 275 lGGGEDCAHFHPDGRWNDDVCQRPYHWVCE 304
Cdd:cd03591   85 -GGGEDCVEMYTSGKWNDVACNLTRLFVCE 113

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504 196 YWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQKYL------GSAYTWMGLSDPEGAWKWVDGTDyaTGFQNWKPGQPDd 269
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLsnlsrvSNSAAWIGLYRDVDSWRWSDGSE--SSFRNWNTFQPF- 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767991504 270 wqghglgGGEDCAHFHPDGRWNDDVCQRPYHWVC 303
Cdd:cd03602   80 -------GQGDCATMYSSGRWYAALCSALKPFIC 106

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504 197 WFSHSGMSWAEAEKYCQLKNAHLVVINSRE-EQKYLGSAYT-------WMGLSD---PEGAWKWVDGTDYATGFQNWKPG 265
Cdd:cd03601    4 LCSDETMNYAKAGAFCRSRGMRLASLAMRDsEMRDAILAFTlvkghgyWVGADNlqdGEYDFLWNDGVSLPTDSDLWAPN 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767991504 266 QPDDWQGHglgggEDCAH-FHPDGRWNDDVCQRPYHWVCE 304
Cdd:cd03601   84 EPSNPQSR-----QLCVQlWSKYNLLDDEYCGRAKRVICE 118

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767991504 170 LNNNGEEASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREE----QKYLGSAYTWMGLSDPEG 245
Cdd:PHA02642  74 FKSDTQEPTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEElnflKRYKDSSDHWIGLNRESS 153

                         90
                 ....*....|....*.
gi 767991504 246 --AWKWVDGTDYATGF 259
Cdd:PHA02642 154 nhPWKWADNSNYNASF 169

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 767991504 194 SCYWFSHSGMSWAEAEKYCQ-LKNAHLVVINS---REEQKYLGSAYT----WMG--LSDPEGAWK--WVDGTDYatGFQN 261
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRrCYRGNLASIHSfafNYRVQRLVSTLNqaqvWIGgiITGKGRCRRfsWVDGSVW--NYAY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767991504 262 WKPGQPddwqghGLGGGEDCAHFHPDGRWNDDVCQRPYHWVC 303
Cdd:cd03598   80 WAPGQP------GNRRGHCVELCTRGGHWRRAHCKLRRPFIC 115