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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B        3 KKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAK---TSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDE 79
Cdd:cd03591   1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKkgnTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                        90       100       110
                ....*....|....*....|....*....|....
1MSB_B       80 PNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEF 113
Cdd:cd03591  81 PNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B        3 KKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAK---TSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDE 79
Cdd:cd03591   1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKkgnTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                        90       100       110
                ....*....|....*....|....*....|....
1MSB_B       80 PNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEF 113
Cdd:cd03591  81 PNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B           2 GKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAK-----TSAFLGITDEVTEGQFMYVTG-GRLTYSNW 75
Cdd:smart00034   9 GGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsgssDYYWIGLSDPDSNGSWQWSDGsGPVSYSNW 88

                           90       100       110
                   ....*....|....*....|....*....|....*...
1MSB_B          76 KKDEPNdhGSGEDCVTI-VDNGLWNDISCQASHTAVCE 112
Cdd:smart00034  89 APGEPN--NSSGDCVVLsTSGGKWNDVSCTSKLPFVCE 124

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B        3 KKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAK---TSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDE 79
Cdd:cd03591   1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKkgnTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                        90       100       110
                ....*....|....*....|....*....|....
1MSB_B       80 PNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEF 113
Cdd:cd03591  81 PNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B           2 GKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAK-----TSAFLGITDEVTEGQFMYVTG-GRLTYSNW 75
Cdd:smart00034   9 GGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsgssDYYWIGLSDPDSNGSWQWSDGsGPVSYSNW 88

                           90       100       110
                   ....*....|....*....|....*....|....*...
1MSB_B          76 KKDEPNdhGSGEDCVTI-VDNGLWNDISCQASHTAVCE 112
Cdd:smart00034  89 APGEPN--NSSGDCVVLsTSGGKWNDVSCTSKLPFVCE 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B        2 GKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSA------FLGITDEVTEGQFMYVTGGRLTYSNW 75
Cdd:cd03596   8 HKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVpgnwevWLGINDMVAEGKWVDVNGSPISYFNW 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1MSB_B       76 KKDEPN--DHGSGEDCVTI--VDNGLWNDISCQASHTAVCEF 113
Cdd:cd03596  88 EREITAqpDGGKRENCVALssSAQGKWFDEDCRREKPYVCEF 129

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B        8 TNHERMPFSKVKALCSElRGT--VAIPrNAEENKAIQEVAKT----SAFLGITDEVTEGQFMYVTGGRLTYSNWKKDEPN 81
Cdd:cd03592   5 YSTEKMTFNEAVKYCKS-RGTdlVAIQ-NAEENALLNGFALKynlgYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                        90       100       110
                ....*....|....*....|....*....|...
1MSB_B       82 DhGSGEDCVT--IVDNGLWNDISCQASHTAVCE 112
Cdd:cd03592  83 N-GRNENCLEiyIKDNGKWNDEPCSKKKSAICY 114

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B       10 HERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSAF--LGITDEVTEGQFMYVTGGRLTYSNWKKDEP-NDHGSG 86
Cdd:cd03603   7 DGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAswIGASDAATEGTWKWSDGEESTYTNWGSGEPhNNGGGN 86

                        90
                ....*....|....*...
1MSB_B       87 EDCVTI----VDNGLWND 100
Cdd:cd03603  87 EDYAAInhfpGISGKWND 104

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B       11 ERMPFSKVKALCSELRGTVAIPRN--AEENKAI---QEVAKTSAFLGITD-EVTEGQFMYVTGGRL--TYSNWKKDEPND 82
Cdd:cd03601   8 ETMNYAKAGAFCRSRGMRLASLAMrdSEMRDAIlafTLVKGHGYWVGADNlQDGEYDFLWNDGVSLptDSDLWAPNEPSN 87

                        90       100       110
                ....*....|....*....|....*....|.
1MSB_B       83 HGSGEDCVTIVDN-GLWNDISCQASHTAVCE 112
Cdd:cd03601  88 PQSRQLCVQLWSKyNLLDDEYCGRAKRVICE 118

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MSB_B        6 FVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEV----------AKTSAFLGITDEVTEGQ--------FMYVTG 67
Cdd:cd03600   7 YTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLlaagpgrhgrGSLRLWIGLQREPRQCSdpslplrgFSWVTG 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
1MSB_B       68 GRLT-YSNWKKDEPNDHGSgEDCVTI------VDNGLWNDISCQASHTA-VCEF 113
Cdd:cd03600  87 DQDTdFSNWLQEPAGTCTS-PRCVALsaagstPDNLKWKDGPCSARADGyLCKF 139