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Conserved domains on  [gi|568942508|ref|XP_006506493|]
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Protein Classification

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

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein similar to Homo sapiens early activation antigen CD69 involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets

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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); ...
130-242 4.34e-39

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: 131.69  E-value: 4.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 130 CPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSL--SLVSWTGILRKGRGQPWVWKKDSTFKP 207
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQigSSSYWIGLSREKSEKPWKWIDGSPLNN 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568942508 208 KIAEI-LHDECNCAMMSASGLTADSCTTLHPYLCKC 242
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); ...
130-242 4.34e-39

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: 131.69  E-value: 4.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 130 CPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSL--SLVSWTGILRKGRGQPWVWKKDSTFKP 207
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQigSSSYWIGLSREKSEKPWKWIDGSPLNN 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568942508 208 KIAEI-LHDECNCAMMSASGLTADSCTTLHPYLCKC 242
Cdd:cd03593   81 LFNIRgSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
130-241 1.62e-20

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


Pssm-ID: 214480  Cd Length: 124  Bit Score: 83.80  E-value: 1.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508   130 CPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS------WTGILRKGRGQPWVW---- 199
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgssdyyWIGLSDPDSNGSWQWsdgs 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 568942508   200 -KKDSTFKPKIAEILHDEcNCAMMSASGLT--ADSCTTLHPYLCK 241
Cdd:smart00034  81 gPVSYSNWAPGEPNNSSG-DCVVLSTSGGKwnDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
148-241 4.96e-12

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


Pssm-ID: 395013  Cd Length: 104  Bit Score: 60.56  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508  148 RKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS----WTGILRKGRGQPWVWKKDSTFKPKIAEILHDECN---CA 220
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKQSneyfWIGLTDRKNEGTWKWEDGSPVNYTNWAEPNNNGEnedCV 80
                          90       100
                  ....*....|....*....|...
gi 568942508  221 MMSAS--GLTADSCTTLHPYLCK 241
Cdd:pfam00059  81 ELSSSsgKWNDENCNSKNPFVCE 103
PHA02642 PHA02642
C-type lectin-like protein; Provisional
127-217 9.89e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024  Cd Length: 216  Bit Score: 62.44  E-value: 9.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 127 YALCPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS--WTGILRKGRGQPWVWKKDST 204
Cdd:PHA02642  85 YVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSdhWIGLNRESSNHPWKWADNSN 164
                         90
                 ....*....|...
gi 568942508 205 FKPKIAEILHDEC 217
Cdd:PHA02642 165 YNASFVITGTGEC 177
 
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); ...
130-242 4.34e-39

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: 131.69  E-value: 4.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 130 CPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSL--SLVSWTGILRKGRGQPWVWKKDSTFKP 207
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQigSSSYWIGLSREKSEKPWKWIDGSPLNN 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568942508 208 KIAEI-LHDECNCAMMSASGLTADSCTTLHPYLCKC 242
Cdd:cd03593   81 LFNIRgSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
130-241 1.62e-20

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


Pssm-ID: 214480  Cd Length: 124  Bit Score: 83.80  E-value: 1.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508   130 CPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS------WTGILRKGRGQPWVW---- 199
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgssdyyWIGLSDPDSNGSWQWsdgs 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 568942508   200 -KKDSTFKPKIAEILHDEcNCAMMSASGLT--ADSCTTLHPYLCK 241
Cdd:smart00034  81 gPVSYSNWAPGEPNNSSG-DCVVLSTSGGKwnDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
140-241 5.71e-16

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  Cd Length: 116  Bit Score: 71.50  E-value: 5.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 140 NCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS-----WTGILRKGRGQPWVW------KKDSTFKPK 208
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSsssdvWIGLNDLSSEGTWKWsdgsplVDYTNWAPG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568942508 209 IAEILHDEcNCAMMSAS---GLTADSCTTLHPYLCK 241
Cdd:cd00037   81 EPNPGGSE-DCVVLSSSsdgKWNDVSCSSKLPFICE 115
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
130-199 1.05e-13

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  Cd Length: 126  Bit Score: 65.79  E-value: 1.05e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568942508 130 CPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS---WTGILRKGRGQPWVW 199
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNrsyWIGLSDEETEGEWKW 73
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
148-241 4.96e-12

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


Pssm-ID: 395013  Cd Length: 104  Bit Score: 60.56  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508  148 RKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS----WTGILRKGRGQPWVWKKDSTFKPKIAEILHDECN---CA 220
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKQSneyfWIGLTDRKNEGTWKWEDGSPVNYTNWAEPNNNGEnedCV 80
                          90       100
                  ....*....|....*....|...
gi 568942508  221 MMSAS--GLTADSCTTLHPYLCK 241
Cdd:pfam00059  81 ELSSSsgKWNDENCNSKNPFVCE 103
PHA02642 PHA02642
C-type lectin-like protein; Provisional
127-217 9.89e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024  Cd Length: 216  Bit Score: 62.44  E-value: 9.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 127 YALCPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS--WTGILRKGRGQPWVWKKDST 204
Cdd:PHA02642  85 YVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSdhWIGLNRESSNHPWKWADNSN 164
                         90
                 ....*....|...
gi 568942508 205 FKPKIAEILHDEC 217
Cdd:PHA02642 165 YNASFVITGTGEC 177
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
130-242 2.41e-08

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  Cd Length: 129  Bit Score: 51.22  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 130 CPKEWILYSHNCYYIGMERKSWNDSLVSC--ISKNCSLLYIDSEEEQDFLQslSLVS---------WTGILRKGRGQPWV 198
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIA--SLISsyqkayqpvWIGLHDPQQSRGWE 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568942508 199 WKKDSTF-------KPKIAEILHdecnCAMMSA-SGLT---ADSCTTLHPYLCKC 242
Cdd:cd03594   79 WSDGSKLdyrswdrNPPYARGGY----CAELSRsTGFLkwnDANCEERNPFICKY 129
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
130-241 8.94e-08

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: 49.66  E-value: 8.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 130 CPKEWILYSHNCY-YIGmERKSWNDSLVSCISKNCS-----LLYIDSEEEQDFLQSL--SLVS-------WTGILRKGRG 194
Cdd:cd03589    1 CPTFWTAFGGYCYrFFG-DRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVYDLfeSSRGpdtpyglWIGLHDRTSE 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 195 QPWVWKKDSTF--------KPKIAEILHDecnCAMMSASGLTADS-----CTTLHPYLCK 241
Cdd:cd03589   80 GPFEWTDGSPVdftkwaggQPDNYGGNED---CVQMWRRGDAGQSwndmpCDAVFPYICK 136
PHA03097 PHA03097
C-type lectin-like protein; Provisional
130-245 5.51e-06

C-type lectin-like protein; Provisional


Pssm-ID: 222982  Cd Length: 157  Bit Score: 45.24  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 130 CPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVS--WTGILRKGRGQPWVWKKDSTFKP 207
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQdlWIGIEKKKGDDDDREVLDKVVKP 125
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568942508 208 KIAEilhdecNCAMMSASGLTADSCTTLHPYLCKCKFP 245
Cdd:PHA03097 126 PKSG------KCAYLKDKTIISSNCNATKGWICFDRLP 157
PHA02867 PHA02867
C-type lectin protein; Provisional
129-240 5.68e-06

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 45.06  E-value: 5.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942508 129 LCPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQslslvswtgilRKGRGQPWVWKKDSTFKPK 208
Cdd:PHA02867  48 VCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVS-----------RYGKGSYWIDINQNRKIPG 116
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568942508 209 IAEILHDECN----CAMMSASGLTADSCTTLHPYLC 240
Cdd:PHA02867 117 INFSLYYEQGvndiCLLFDTSNIIEMSCIFHERTIC 152
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
142-204 7.38e-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  Cd Length: 118  Bit Score: 35.48  E-value: 7.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568942508 142 YYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLV---SWTGILRKGRGQPWVWKKDST 204
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGygaSWIGASDAATEGTWKWSDGEE 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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