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 364502941 127 SKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQaGLARVFIGINDLEKEGAFVYSDHSPMrTFNKWRS 206
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKK-GNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 364502941 207 GEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMCEF 242
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 364502941 127 SKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQaGLARVFIGINDLEKEGAFVYSDHSPMrTFNKWRS 206
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKK-GNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 364502941 207 GEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMCEF 242
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 364502941  139 YADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGlARVFIGINDLEKEGAFVYSDHSPMRTFNkwRSGEPNNAYDEEDC 218
Cdd:pfam00059   4 WDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTWKWVDGSPVNYTN--WAPEPNNNGENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 364502941  219 VEM-VASGGWNDVACHTTMYFMCEF 242
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 364502941 127 SKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQaGLARVFIGINDLEKEGAFVYSDHSPMrTFNKWRS 206
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKK-GNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 364502941 207 GEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMCEF 242
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 364502941   130 YLLVKEEKRYADAQLSCQGRGGTLSMPKDEA-ANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRTFNKWRSGE 208
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAeNDFVASLLKNSGSSDYYWIGLSDPDSNGSWQWSDGSGPVSYSNWAPGE 92

                           90       100       110
                   ....*....|....*....|....*....|....
gi 364502941   209 PNNAydEEDCVEMVASGG-WNDVACHTTMYFMCE 241
Cdd:smart00034  93 PNNS--SGDCVVLSTSGGkWNDVSCTSKLPFVCE 124

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 364502941 126 ESKIYLLVKEEKRYADAQLSCQGRGGTLSMPK-DEAANGLMaaYLAQAGlARVFIGINDLEKEGAFVYSDHSPMRTFNK- 203
Cdd:cd03590    9 QSSCYFFSTEKKSWEESRQFCEDMGAHLVIINsQEEQEFIS--KILSGN-RSYWIGLSDEETEGEWKWVDGTPLNSSKTf 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 364502941 204 WRSGEPNNAY-DEEDCVEMV-ASGGWNDVACHTTMYFMCE 241
Cdd:cd03590   86 WHPGEPNNWGgGGEDCAELVyDSGGWNDVPCNLEYRWICE 125

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364502941  139 YADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGlARVFIGINDLEKEGAFVYSDHSPMRTFNkwRSGEPNNAYDEEDC 218
Cdd:pfam00059   4 WDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTWKWVDGSPVNYTN--WAPEPNNNGENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 364502941  219 VEM-VASGGWNDVACHTTMYFMCEF 242
Cdd:pfam00059  81 VELsSSSGKWNDENCNSKNPFVCEK 105

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 364502941 135 EEKRYADAQLSCQGRGGTLS--MPKDEAAnglmaaYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRtFNKWRSGEPNNA 212
Cdd:cd03588   18 DRETWEDAERRCREQQGHLSsiVTPEEQE------FVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQ-FENWRPNQPDNF 90

                         90       100       110
                 ....*....|....*....|....*....|..
gi 364502941 213 YDE-EDCVEMV--ASGGWNDVACHTTMYFMCE 241
Cdd:cd03588   91 FATgEDCVVMIwhEEGEWNDVPCNYHLPFTCK 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 364502941 130 YLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGlaRVFIGINDLEKEGAFVYSDHSPMrTFNKWRSGEP 209
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG--ASWIGASDAATEGTWKWSDGEES-TYTNWGSGEP 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 364502941 210 NNAYDE-EDCVEM----VASGGWNDVA-CHTTMYFMCEF 242
Cdd:cd03603   80 HNNGGGnEDYAAInhfpGISGKWNDLAnSYNTLGYVIEW 118

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 364502941 130 YLLVKEEKRYADAQLSCQG--RGGTLSMPkDEAANGLMAAYLAQAGLARVFIG--INDLEKEGAFVYSDHSPMRtFNKWR 205
Cdd:cd03598    4 YRFVKSPRTFRDAQVICRRcyRGNLASIH-SFAFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWN-YAYWA 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 364502941 206 SGEPNNayDEEDCVEMVASGG-WNDVACHTTMYFMCEF 242
Cdd:cd03598   82 PGQPGN--RRGHCVELCTRGGhWRRAHCKLRRPFICSY 117

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364502941 130 YLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGL------ARVFIGindLEKEGAFVYSDHSPMRTFNk 203
Cdd:cd03600    7 YTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGrhgrgsLRLWIG---LQREPRQCSDPSLPLRGFS- 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 364502941 204 WRSGEPNNAYDE-----------EDCVEMVASG------GWNDVACHTTMY-FMCEF 242
Cdd:cd03600   83 WVTGDQDTDFSNwlqepagtctsPRCVALSAAGstpdnlKWKDGPCSARADgYLCKF 139