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 1022943309  88 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVaKSGFFRVFIGVNDLEREGQYMFTDNTPLqNYSNWNE 167
Cdd:cd03591     1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV-KKGNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1022943309 168 GEPSDPYGHEDCVEMLSSGRWNDTECHLTMYFVCEF 203
Cdd:cd03591    79 GEPNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 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 1022943309  88 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVaKSGFFRVFIGVNDLEREGQYMFTDNTPLqNYSNWNE 167
Cdd:cd03591     1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV-KKGNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1022943309 168 GEPSDPYGHEDCVEMLSSGRWNDTECHLTMYFVCEF 203
Cdd:cd03591    79 GEPNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 114

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943309  98 KNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFFrVFIGVNDLEREGQYMFTDNTPLqNYSNWNeGEPSDPYGHE 177
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY-FWIGLTDRKNEGTWKWVDGSPV-NYTNWA-PEPNNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 1022943309 178 DCVEM-LSSGRWNDTECHLTMYFVCEF 203
Cdd:pfam00059  79 DCVELsSSSGKWNDENCNSKNPFVCEK 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 1022943309  88 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVaKSGFFRVFIGVNDLEREGQYMFTDNTPLqNYSNWNE 167
Cdd:cd03591     1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV-KKGNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1022943309 168 GEPSDPYGHEDCVEMLSSGRWNDTECHLTMYFVCEF 203
Cdd:cd03591    79 GEPNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 114

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 1022943309   88 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYV-AKSGFFRVFIGVNDLEREGQYMFTDNTPLQNYSNWN 166
Cdd:smart00034  10 GKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLkNSGSSDYYWIGLSDPDSNGSWQWSDGSGPVSYSNWA 89

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1022943309  167 EGEPSDpyGHEDCVEM-LSSGRWNDTECHLTMYFVCE 202
Cdd:smart00034  90 PGEPNN--SSGDCVVLsTSGGKWNDVSCTSKLPFVCE 124

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943309  89 KFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKS--GFFRVFIGVNDLEREGQYMFTDNTPLQnYSNWN 166
Cdd:cd03596    10 KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASvpGNWEVWLGINDMVAEGKWVDVNGSPIS-YFNWE 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1022943309 167 EGEPSDPYG--HEDCVEMLSS--GRWNDTECHLTMYFVCEF 203
Cdd:cd03596    89 REITAQPDGgkRENCVALSSSaqGKWFDEDCRREKPYVCEF 129

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943309 119 DEAANTLIADYV----AKSGFFRVFIGVNDLEREGQYMFTDNTPLqNYSNWNEGEPSDPYGHEDCVEM----LSSGRWND 190
Cdd:cd03589    46 SQEENDFVYDLFessrGPDTPYGLWIGLHDRTSEGPFEWTDGSPV-DFTKWAGGQPDNYGGNEDCVQMwrrgDAGQSWND 124

                          90
                  ....*....|.
gi 1022943309 191 TECHLTMYFVC 201
Cdd:cd03589   125 MPCDAVFPYIC 135

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 1022943309  92 YIVQEEKNYRESLTHCRIRGGMLA--------MPKDEAANTLIADYvaksGFFrvfIGVNDLER-EGQYMFTDNTPL-QN 161
Cdd:cd03601     4 LCSDETMNYAKAGAFCRSRGMRLAslamrdseMRDAILAFTLVKGH----GYW---VGADNLQDgEYDFLWNDGVSLpTD 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1022943309 162 YSNWNEGEPSDPYGHEDCVEMLSS-GRWNDTECHLTMYFVCE 202
Cdd:cd03601    77 SDLWAPNEPSNPQSRQLCVQLWSKyNLLDDEYCGRAKRVICE 118

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 1022943309  91 YYIVQEEKNYRESLTHCRIRGGMLA---MPKDEA-ANTLIADYVaksgffrvFIGVNDLEREGQYMFTDNTPLQnYSNWN 166
Cdd:cd03588    13 YRHFPDRETWEDAERRCREQQGHLSsivTPEEQEfVNNNAQDYQ--------WIGLNDRTIEGDFRWSDGHPLQ-FENWR 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1022943309 167 EGEPSDPYGH-EDCVEML--SSGRWNDTECHLTMYFVCE 202
Cdd:cd03588    84 PNQPDNFFATgEDCVVMIwhEEGEWNDVPCNYHLPFTCK 122

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 1022943309  90 FYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFFrvFIGVNDLEREGQYMFTDNTPLQnYSNWNEGE 169
Cdd:cd03603     2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS--WIGASDAATEGTWKWSDGEEST-YTNWGSGE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1022943309 170 PSDPY-GHEDCVEM----LSSGRWNDT-ECHLTMYFVCEF 203
Cdd:cd03603    79 PHNNGgGNEDYAAInhfpGISGKWNDLaNSYNTLGYVIEW 118

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943309  87 EEKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFfrvFIGVNDLEREGQYMFTDNTPlqnYSNWN 166
Cdd:cd03593     9 GNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY---WIGLSREKSEKPWKWIDGSP---LNNLF 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1022943309 167 EGEPSDPYGHedCVeMLSSGRWNDTECHLTMYFVCE 202
Cdd:cd03593    83 NIRGSTKSGN--CA-YLSSTGIYSEDCSTKKRWICE 115

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 1022943309  99 NYRESLTHCRIRGGMLAMPKDEAANTLIADYV----AKSGFFRVFI------GVNDLEREGQYMFTDNTPLQnYSNWNEG 168
Cdd:cd03595    26 NFEEARQACREDGGELLSIESENEQKLIERFIqtlrASDGDFWIGLrrssqyNVTSSACSSLYYWLDGSIST-FRNWYVD 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1022943309 169 EPSdpYGHEDCVEML-----SSG-------RWNDTECHLTMYFVCEF 203
Cdd:cd03595   105 EPS--CGSEVCVVMYhqpsaPAGqggpylfQWNDDNCNMKNNFICKY 149