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Conserved domains on  [gi|84370294|ref|NP_001028294|]
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early activation antigen CD69 [Mus musculus]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132518)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 85-196 1.81e-38

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.


:

Pssm-ID: 153063  Cd Length: 116  Bit Score: 128.60  E-value: 1.81e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEHWIGL-KNEANQTWKWANGKEFNS 163
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLsREKSEKPWKWIDGSPLNN 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 84370294 164 WFNLTG---SGRCVSVNHKNVTAVDCEANFHWVCSK 196
Cdd:cd03593  81 LFNIRGstkSGNCAYLSSTGIYSEDCSTKKRWICEK 116
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 85-196 1.81e-38

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.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 128.60  E-value: 1.81e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEHWIGL-KNEANQTWKWANGKEFNS 163
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLsREKSEKPWKWIDGSPLNN 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 84370294 164 WFNLTG---SGRCVSVNHKNVTAVDCEANFHWVCSK 196
Cdd:cd03593  81 LFNIRGstkSGNCAYLSSTGIYSEDCSTKKRWICEK 116
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 84-196 6.04e-26

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 99.42  E-value: 6.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294   84 TCKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEHWIGLKNE-ANQTWKWANGKEFN 162
Cdd:PHA02642  87 TCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNREsSNHPWKWADNSNYN 166

                         90       100       110
                 ....*....|....*....|....*....|....
gi 84370294  163 SWFNLTGSGRCVSVNHKNVTAVDCEANFHWVCSK 196
Cdd:PHA02642 167 ASFVITGTGECAYLNDIRISSSRVYANRKWICSK 200
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 85-194 1.08e-22

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: 88.43  E-value: 1.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294     85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFL----KRYSGELEHWIGL-KNEANQTWKWANGK 159
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllKNSGSSDYYWIGLsDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 84370294    160 EFNSWFNL------TGSGRCVSVNHKNVT--AVDCEANFHWVC 194
Cdd:smart00034  81 GPVSYSNWapgepnNSSGDCVVLSTSGGKwnDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 103-196 1.81e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 39.38  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294   103 TKSWALAQRSCSEDAATLAVIDSEKD----MTFLKRYSgeLEHWIGLKNE-ANQTWKWANGKEFNSWF------NLTGSG 171
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEEldflSSTLKKSN--KYFWIGLTDRkNEGTWKWVDGSPVNYTNwapepnNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 84370294   172 RCVSVNHKN--VTAVDCEANFHWVCSK 196
Cdd:pfam00059  79 DCVELSSSSgkWNDENCNSKNPFVCEK 105
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 85-196 1.81e-38

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.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 128.60  E-value: 1.81e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEHWIGL-KNEANQTWKWANGKEFNS 163
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLsREKSEKPWKWIDGSPLNN 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 84370294 164 WFNLTG---SGRCVSVNHKNVTAVDCEANFHWVCSK 196
Cdd:cd03593  81 LFNIRGstkSGNCAYLSSTGIYSEDCSTKKRWICEK 116
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 84-196 6.04e-26

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 99.42  E-value: 6.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294   84 TCKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEHWIGLKNE-ANQTWKWANGKEFN 162
Cdd:PHA02642  87 TCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNREsSNHPWKWADNSNYN 166

                         90       100       110
                 ....*....|....*....|....*....|....
gi 84370294  163 SWFNLTGSGRCVSVNHKNVTAVDCEANFHWVCSK 196
Cdd:PHA02642 167 ASFVITGTGECAYLNDIRISSSRVYANRKWICSK 200
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 85-194 1.08e-22

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: 88.43  E-value: 1.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294     85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFL----KRYSGELEHWIGL-KNEANQTWKWANGK 159
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllKNSGSSDYYWIGLsDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 84370294    160 EFNSWFNL------TGSGRCVSVNHKNVT--AVDCEANFHWVC 194
Cdd:smart00034  81 GPVSYSNWapgepnNSSGDCVVLSTSGGKwnDVSCTSKLPFVC 123
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 85-196 3.05e-19

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: 79.27  E-value: 3.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRY-SGELEHWIGLKNEANQ-TWKWANGKEFN 162
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIlSGNRSYWIGLSDEETEgEWKWVDGTPLN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 84370294 163 S--WF-------NLTGSG-RCVSVNHKNVTAVD--CEANFHWVCSK 196
Cdd:cd03590  81 SskTFwhpgepnNWGGGGeDCAELVYDSGGWNDvpCNLEYRWICEK 126
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 96-196 2.38e-17

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: 74.19  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  96 CYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRY---SGELEHWIGL-KNEANQTWKWANGKEFNSWFN----- 166
Cdd:cd00037   2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLlkkSSSSDVWIGLnDLSSEGTWKWSDGSPLVDYTNwapge 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 84370294 167 --LTGSGRCVSVNHKN---VTAVDCEANFHWVCSK 196
Cdd:cd00037  82 pnPGGSEDCVVLSSSSdgkWNDVSCSSKLPFICEK 116
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 43-197 3.68e-17

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 74.90  E-value: 3.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294   43 WAVL-IVVLITSLIIALIALNVGkyncpgLYEKLESSDHHVATCKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLA 121
Cdd:PHA03097   9 VTVHwILVPCGSIIIALIALVII------LSCKLSPGDRSGLNCRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILT 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84370294  122 VIDSEKDMTFLKRYSGELEHWIGLKNEAnqtwKWANGKE-FNSWFNLTGSGRCVSVNHKNVTAVDCEANFHWVCSKP 197
Cdd:PHA03097  83 LIDDQKEVLFVSRYKGGQDLWIGIEKKK----GDDDDREvLDKVVKPPKSGKCAYLKDKTIISSNCNATKGWICFDR 155
PHA02867 PHA02867
C-type lectin protein; Provisional
 85-198 2.90e-09

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 53.92  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294   85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYsGELEHWIGLKNEANqtwkwANGKEFNSW 164
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRY-GKGSYWIDINQNRK-----IPGINFSLY 122

                         90       100       110
                 ....*....|....*....|....*....|....
gi 84370294  165 FNLTGSGRCVSVNHKNVTAVDCEANFHWVCSKPS 198
Cdd:PHA02867 123 YEQGVNDICLLFDTSNIIEMSCIFHERTICVKED 156
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 97-196 7.48e-09

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: 51.22  E-value: 7.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  97 YFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEH--WIGLKNeANQTWKWANGKEFNS----WFNLTGS 170
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSaaWIGLYR-DVDSWRWSDGSESSFrnwnTFQPFGQ 81

                        90       100
                ....*....|....*....|....*..
gi 84370294 171 GRCVSVN-HKNVTAVDCEANFHWVCSK 196
Cdd:cd03602  82 GDCATMYsSGRWYAALCSALKPFICYD 108
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 85-196 8.36e-06

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.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 43.34  E-value: 8.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEhWIGLKNEA-NQTWKWANGK--EF 161
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-WIGLNDRTiEGDFRWSDGHplQF 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 84370294 162 NSW-------FNLTGSGRCVSVNHKNVTAVDCEANFH--WVCSK 196
Cdd:cd03588  80 ENWrpnqpdnFFATGEDCVVMIWHEEGEWNDVPCNYHlpFTCKK 123
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 85-194 2.34e-05

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: 42.36  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  85 CKNEWISYKRTCYFFSTTTKSWALAQRSC--SEDAATLAVIDSEKDMTFLKRY-----SGELEHWIGLKN-EANQTWKWA 156
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLissyqKAYQPVWIGLHDpQQSRGWEWS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 84370294 157 NG--KEFNSWF---NLTGSGRCVSVNHKNVTAV----DCEANFHWVC 194
Cdd:cd03594  81 DGskLDYRSWDrnpPYARGGYCAELSRSTGFLKwndaNCEERNPFIC 127
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 85-164 1.81e-04

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: 40.03  E-value: 1.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  85 CKNEWISYKRTCYFFSTTTKSWALAQRSCSE-----DAATLAVIDSEKDMTFLKRY-------SGELEHWIGLKNEANQ- 151
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLfessrgpDTPYGLWIGLHDRTSEg 80

                        90
                ....*....|....*
gi 84370294 152 TWKWANGK--EFNSW 164
Cdd:cd03589  81 PFEWTDGSpvDFTKW 95
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 103-196 1.81e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 39.38  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294   103 TKSWALAQRSCSEDAATLAVIDSEKD----MTFLKRYSgeLEHWIGLKNE-ANQTWKWANGKEFNSWF------NLTGSG 171
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEEldflSSTLKKSN--KYFWIGLTDRkNEGTWKWVDGSPVNYTNwapepnNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 84370294   172 RCVSVNHKN--VTAVDCEANFHWVCSK 196
Cdd:pfam00059  79 DCVELSSSSgkWNDENCNSKNPFVCEK 105
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 97-164 6.60e-03

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: 35.09  E-value: 6.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370294  97 YFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFL----KRYSGElehWIGL-KNEANQTWKWANGKE--FNSW 164
Cdd:cd03603   3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLlsnfGGYGAS---WIGAsDAATEGTWKWSDGEEstYTNW 74
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 96-176 9.41e-03

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.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 35.10  E-value: 9.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370294  96 CYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKR---------YSGELEHWIGLKNEANQT---------WKWAN 157
Cdd:cd03600   6 CYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLllaagpgrhGRGSLRLWIGLQREPRQCsdpslplrgFSWVT 85

                        90       100
                ....*....|....*....|....*.
gi 84370294 158 GKE---FNSWF----NLTGSGRCVSV 176
Cdd:cd03600  86 GDQdtdFSNWLqepaGTCTSPRCVAL 111
 
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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