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Conserved domains on  [gi|1907136733|ref|XP_036015513|]
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bone marrow proteoglycan isoform X1 [Mus musculus]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132538)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein similar to Homo sapiens bone marrow proteoglycan involved in antiparasitic defense mechanisms and immune hypersensitivity reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 107-223 1.03e-60

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.


:

Pssm-ID: 153068  Cd Length: 117  Bit Score: 186.12  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 107 TCRYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIKGWGRCKRFRWVDGSSWNFAYW 186
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907136733 187 AAGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFICSY 223
Cdd:cd03598    81 APGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFICSY 117
 
Name Accession Description Interval E-value
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 107-223 1.03e-60

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.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 186.12  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 107 TCRYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIKGWGRCKRFRWVDGSSWNFAYW 186
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907136733 187 AAGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFICSY 223
Cdd:cd03598    81 APGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFICSY 117
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 110-221 8.21e-23

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 89.20  E-value: 8.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733  110 YLLVRRAECFDKAQSVCRRCYrGTLASIHSFSVNFGIQSAVR-GINQGQVWIGGRIKGwgRCKRFRWVDGSSW-NFAYWA 187
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLG-GHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPD--SNGSWQWSDGSGPvSYSNWA 89

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907136733  188 AGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFIC 221
Cdd:smart00034  90 PGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 119-223 1.59e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 50.94  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 119 FDKAQSVCRRcYRGTLASIHSF-SVNFgIQSAVRGINQgQVWIGgrIKGWGRCKRFRWVDGSSWNFAYWAA-GQPCPGGG 196
Cdd:pfam00059   4 WDEAREACRK-LGGHLVSINSAeELDF-LSSTLKKSNK-YFWIG--LTDRKNEGTWKWVDGSPVNYTNWAPePNNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 1907136733 197 RCVTLCTQGGHWRLSHCVKRRPFICSY 223
Cdd:pfam00059  79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 90-223 1.41e-04

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.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 42.38  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733   90 CPKeeDTTSLMGDSGCktcrYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSV-NFGIQSAVRGINQGqVWIG-GRIKGW 167
Cdd:TIGR00864  318 CPK--DGEIFEENGHC----FQIVPEEAAWLDAQEQCLARAGAALAIVDNDALqNFLARKVTHSLDRG-VWIGfSDVNGA 390

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136733  168 GRcKRFRWVDGSSWNFAY-WAAGQPCPGGGR-CVTLCTQGghWRLSH-CVKRRPFICSY 223
Cdd:TIGR00864  391 EK-GPAHQGEAFEAEECEeGLAGEPHPARAEhCVRLDPRG--QCNSDlCNAPHAYVCEL 446
 
Name Accession Description Interval E-value
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 107-223 1.03e-60

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.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 186.12  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 107 TCRYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIKGWGRCKRFRWVDGSSWNFAYW 186
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907136733 187 AAGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFICSY 223
Cdd:cd03598    81 APGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFICSY 117
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 110-221 8.21e-23

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 89.20  E-value: 8.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733  110 YLLVRRAECFDKAQSVCRRCYrGTLASIHSFSVNFGIQSAVR-GINQGQVWIGGRIKGwgRCKRFRWVDGSSW-NFAYWA 187
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLG-GHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPD--SNGSWQWSDGSGPvSYSNWA 89

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907136733  188 AGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFIC 221
Cdd:smart00034  90 PGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 110-223 1.82e-20

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.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 83.05  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 110 YLLVRRAECFDKAQSVCRRcYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIkgWGRCKRFRWVDGSS-WNFAYWAA 188
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRS-LGGHLASIHSEEENDFLASLLKKSSSSDVWIGLND--LSSEGTWKWSDGSPlVDYTNWAP 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907136733 189 GQPCPGG-GRCVTL-CTQGGHWRLSHCVKRRPFICSY 223
Cdd:cd00037    80 GEPNPGGsEDCVVLsSSSDGKWNDVSCSSKLPFICEK 116
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 90-223 1.46e-11

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 59.69  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733  90 CPKEedttSLMGDSGCktcrYLLVRRAECFDKAQSVCRRCYRGT-LASIHSFSVNFGIQSAVRGI--NQGQVWIGgrIKG 166
Cdd:cd03594     1 CPKG----WLPYKGNC----YGYFRQPLSWSDAELFCQKYGPGAhLASIHSPAEAAAIASLISSYqkAYQPVWIG--LHD 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136733 167 WGRCKRFRWVDGSSWNFAYWAAGQPCPGGGRCVTLCTQGGH--WRLSHCVKRRPFICSY 223
Cdd:cd03594    71 PQQSRGWEWSDGSKLDYRSWDRNPPYARGGYCAELSRSTGFlkWNDANCEERNPFICKY 129
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 109-222 1.88e-11

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.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 58.92  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 109 RYLLVRRAECFDKAQSVCRRCYrGTLASIHSFSVNFGIQSAVRGINqGQVWIG--GRIKGWgrckrfRWVDGSSWNFAYW 186
Cdd:cd03602     2 TFYLVNESKTWSEAQQYCRENY-TDLATVQNQEDNALLSNLSRVSN-SAAWIGlyRDVDSW------RWSDGSESSFRNW 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907136733 187 AAGQPcPGGGRCVTLcTQGGHWRLSHCVKRRPFICS 222
Cdd:cd03602    74 NTFQP-FGQGDCATM-YSSGRWYAALCSALKPFICY 107
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 110-223 2.79e-09

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.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 53.07  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 110 YLLVRRAECFDKAQSVCRRcYRGTLASIHSFSVNFGIQSAVRGINqGQVWIGgrIKGWGRCKRFRWVDGSSWNFAYWAAG 189
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSE-AGGTLAMPRNAAENAAIASYVKKGN-TYAFIG--ITDLETEGQFVYLDGGPLTYTNWKPG 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907136733 190 QPCPGGGR--CVTLCTqGGHWRLSHCVKRRPFICSY 223
Cdd:cd03591    80 EPNNAGGGedCVEMYT-SGKWNDVACNLTRLFVCEF 114
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 119-223 1.59e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 50.94  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 119 FDKAQSVCRRcYRGTLASIHSF-SVNFgIQSAVRGINQgQVWIGgrIKGWGRCKRFRWVDGSSWNFAYWAA-GQPCPGGG 196
Cdd:pfam00059   4 WDEAREACRK-LGGHLVSINSAeELDF-LSSTLKKSNK-YFWIG--LTDRKNEGTWKWVDGSPVNYTNWAPePNNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 1907136733 197 RCVTLCTQGGHWRLSHCVKRRPFICSY 223
Cdd:pfam00059  79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 122-221 1.69e-07

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.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 48.89  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 122 AQSVCRR----CYRGTLASIHSFSVNFGI----QSAVRGINQGQVWIGGRIKGWGRCkrFRWVDGSSWNFAYWAAGQPCP 193
Cdd:cd03589    25 AELRCRSfsipGLIAHLVSIHSQEENDFVydlfESSRGPDTPYGLWIGLHDRTSEGP--FEWTDGSPVDFTKWAGGQPDN 102

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907136733 194 GGGrcVTLCTQ-------GGHWRLSHCVKRRPFIC 221
Cdd:cd03589   103 YGG--NEDCVQmwrrgdaGQSWNDMPCDAVFPYIC 135
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 113-223 3.54e-05

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.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 42.57  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 113 VRRAECFDKAQSVCRRcYRGTLASIHSFSVNFGIQSAVRG--INQGQVWIG-----GRIKGWGRCK-RFRWVDGSSWNFA 184
Cdd:cd03595    21 SRRRLNFEEARQACRE-DGGELLSIESENEQKLIERFIQTlrASDGDFWIGlrrssQYNVTSSACSsLYYWLDGSISTFR 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907136733 185 YWAAGQPCPGGGRCVTL-------CTQGGH----WRLSHCVKRRPFICSY 223
Cdd:cd03595   100 NWYVDEPSCGSEVCVVMyhqpsapAGQGGPylfqWNDDNCNMKNNFICKY 149
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 90-223 1.41e-04

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.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 42.38  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733   90 CPKeeDTTSLMGDSGCktcrYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSV-NFGIQSAVRGINQGqVWIG-GRIKGW 167
Cdd:TIGR00864  318 CPK--DGEIFEENGHC----FQIVPEEAAWLDAQEQCLARAGAALAIVDNDALqNFLARKVTHSLDRG-VWIGfSDVNGA 390

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136733  168 GRcKRFRWVDGSSWNFAY-WAAGQPCPGGGR-CVTLCTQGghWRLSH-CVKRRPFICSY 223
Cdd:TIGR00864  391 EK-GPAHQGEAFEAEECEeGLAGEPHPARAEhCVRLDPRG--QCNSDlCNAPHAYVCEL 446
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 172-221 2.17e-04

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.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 39.60  E-value: 2.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907136733 172 RFRWVDGS--SWNFAYWAAGQP---CPGGGRCVTLCTQGGHWRLSHCVKRRPFIC 221
Cdd:cd03590    70 EWKWVDGTplNSSKTFWHPGEPnnwGGGGEDCAELVYDSGGWNDVPCNLEYRWIC 124
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 119-221 4.47e-04

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.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 38.51  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 119 FDKAQSVCRRcyRGT-LASIHSFSVNFGIQSAVRGINQGQVWIGGR--IKGWgrckrfRWVDGSSWNFAY--WAAGQPCP 193
Cdd:cd03592    12 FNEAVKYCKS--RGTdLVAIQNAEENALLNGFALKYNLGYYWIDGNdiNNEG------TWVDTDKKELEYknWAPGEPNN 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907136733 194 GGGR-CVT-LCTQGGHWRLSHCVKRRPFIC 221
Cdd:cd03592    84 GRNEnCLEiYIKDNGKWNDEPCSKKKSAIC 113
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 109-196 6.14e-04

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.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 38.17  E-value: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136733 109 RYLLVRRAECFDKAQSVCRRcYRGTLASIHSFSVNFGIQSAVRGInqGQVWIGGR---IKGwgrckRFRWVDGSSWNFAY 185
Cdd:cd03603     2 FYKFVDGGMTWEAAQTLAES-LGGHLVTINSAEENDWLLSNFGGY--GASWIGASdaaTEG-----TWKWSDGEESTYTN 73

                          90
                  ....*....|.
gi 1907136733 186 WAAGQPCPGGG 196
Cdd:cd03603    74 WGSGEPHNNGG 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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