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 1034607878 186 CPEGWLPFEGKCYYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAKAHGSPRVYWLGLNDRAQEGDWRWLDGSPV- 264
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034607878 265 -TLSFWEPEEPNNIH--DEDCATMNK-GGTWNDLSCYKTTYWICER 306
Cdd:cd03590    81 sSKTFWHPGEPNNWGggGEDCAELVYdSGGWNDVPCNLEYRWICEK 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 1034607878 186 CPEGWLPFEGKCYYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAKAHGSPRVYWLGLNDRAQEGDWRWLDGSPV- 264
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034607878 265 -TLSFWEPEEPNNIH--DEDCATMNK-GGTWNDLSCYKTTYWICER 306
Cdd:cd03590    81 sSKTFWHPGEPNNWGggGEDCAELVYdSGGWNDVPCNLEYRWICEK 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607878 204 TKSWDEARMFCQENYSHLVIINSFAEHNFVAK-AHGSPRVYWLGLNDRAQEGDWRWLDGSPVTLSFWEPEEPNNIHDEDC 282
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSStLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 1034607878 283 ATMNKG-GTWNDLSCYKTTYWICER 306
Cdd:pfam00059  81 VELSSSsGKWNDENCNSKNPFVCEK 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 1034607878  186 CPEGWLPFE--GKCYYFSPSTKSWDEARMFCQE-NYSHLVIINSFAEHNFVAK--AHGSPRVYWLGLND--RAQEGDWRW 258
Cdd:TIGR00864  318 CPKDGEIFEenGHCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARkvTHSLDRGVWIGFSDvnGAEKGPAHQ 397

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034607878  259 LDGSPV-TLSFWEPEEPNNIHDEDCATMNKGGTWNDLSCYKTTYWICE 305
Cdd:TIGR00864  398 GEAFEAeECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCE 445

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 1034607878 186 CPEGWLPFEGKCYYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAKAHGSPRVYWLGLNDRAQEGDWRWLDGSPV- 264
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034607878 265 -TLSFWEPEEPNNIH--DEDCATMNK-GGTWNDLSCYKTTYWICER 306
Cdd:cd03590    81 sSKTFWHPGEPNNWGggGEDCAELVYdSGGWNDVPCNLEYRWICEK 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 1034607878 196 KCYYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAK--AHGSPRVYWLGLNDRAQEGDWRWLDGSP-VTLSFWEPE 272
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASllKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034607878 273 EPNNIHDEDCATMNKG--GTWNDLSCYKTTYWICER 306
Cdd:cd00037    81 EPNPGGSEDCVVLSSSsdGKWNDVSCSSKLPFICEK 116

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607878 204 TKSWDEARMFCQENYSHLVIINSFAEHNFVAK-AHGSPRVYWLGLNDRAQEGDWRWLDGSPVTLSFWEPEEPNNIHDEDC 282
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSStLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 1034607878 283 ATMNKG-GTWNDLSCYKTTYWICER 306
Cdd:pfam00059  81 VELSSSsGKWNDENCNSKNPFVCEK 105

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 1034607878 195 GKCYYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAK--AHGSPRVYwLGLNDRAQEGDWRWLDGSPVTLSFWEPE 272
Cdd:cd03591     1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASyvKKGNTYAF-IGITDLETEGQFVYLDGGPLTYTNWKPG 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034607878 273 EPNNIHD-EDCATMNKGGTWNDLSCYKTTYWICE 305
Cdd:cd03591    80 EPNNAGGgEDCVEMYTSGKWNDVACNLTRLFVCE 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607878 198 YYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFV---AKAHgSPRVYWLGLNDRAQEGDWRWLDGSPVTLSFWEPEEP 274
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLngfALKY-NLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEP 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034607878 275 NNIHDEDCATM--NKGGTWNDLSCYKTTYWICER 306
Cdd:cd03592    82 NNGRNENCLEIyiKDNGKWNDEPCSKKKSAICYT 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607878 198 YYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAKAHGSPRVYWLGLNDRAQEGDWRWLDGSPVTLSFWEPEEP--N 275
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPhnN 82

                          90       100
                  ....*....|....*....|....
gi 1034607878 276 NIHDEDCATMNKG----GTWNDLS 295
Cdd:cd03603    83 GGGNEDYAAINHFpgisGKWNDLA 106

C-type lectin-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607878 182 RRITCPEGWLPFEGKCYYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAKAHGSPRvYWLGLNDRAQEGDWRWLDG 261
Cdd:PHA02642   84 KYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSD-HWIGLNRESSNHPWKWADN 162

                  ....*..
gi 1034607878 262 SPVTLSF 268
Cdd:PHA02642  163 SNYNASF 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 1034607878 195 GKCYYFSPSTKSWDEARMFCQENY-SHLVIINSFAEHNFVAK--AHGSPRVYWLGLNDRAQEGDWR--WLDGSPVTLSFW 269
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRCYrGNLASIHSFAFNYRVQRlvSTLNQAQVWIGGIITGKGRCRRfsWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034607878 270 EPEEPNNiHDEDCATM-NKGGTWNDLSCYKTTYWIC 304
Cdd:cd03598    81 APGQPGN-RRGHCVELcTRGGHWRRAHCKLRRPFIC 115

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 1034607878 199 YFSPSTKSWDEARMFCQENYSHLVIINS-FAE------HNFVAKAHGsprvYWLGLND-RAQEGDWRWLDGS--PVTLSF 268
Cdd:cd03601     4 LCSDETMNYAKAGAFCRSRGMRLASLAMrDSEmrdailAFTLVKGHG----YWVGADNlQDGEYDFLWNDGVslPTDSDL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034607878 269 WEPEEPNNIHD-EDCATM-NKGGTWNDLSCYKTTYWICE 305
Cdd:cd03601    80 WAPNEPSNPQSrQLCVQLwSKYNLLDDEYCGRAKRVICE 118

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607878 193 FEGKCY---YFSPSTK--SWDEARMFCQENYSHLVIINSFAEH----NFVAKAHGSPRVYWLGLNDRAQEG--------D 255
Cdd:cd03595     8 TEKPCYkiaYFQDSRRrlNFEEARQACREDGGELLSIESENEQklieRFIQTLRASDGDFWIGLRRSSQYNvtssacssL 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034607878 256 WRWLDGSPVTLSFWEPEEPnNIHDEDCATM--------NKGG----TWNDLSCYKTTYWICE 305
Cdd:cd03595    88 YYWLDGSISTFRNWYVDEP-SCGSEVCVVMyhqpsapaGQGGpylfQWNDDNCNMKNNFICK 148

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034607878   15 PPykDLPPKPGSSAPPRPPRAAKETEKPPLPCKPRNMTGLdlaavtcPPPQLAVNLEPSPLQPSLAATPVPWL 87
Cdd:PHA03247  2901 PP--DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR-------PQPPLAPTTDPAGAGEPSGAVPQPWL 2964

C-type lectin protein; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607878 186 CPEGWLPFEGKCYYFSPSTKSWDEARMFCQENYSHLVIINSFAEHNFVAKAHGSPrvYWL 245
Cdd:PHA02867   49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRYGKGS--YWI 106