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Conserved domains on  [gi|568942883|ref|XP_006506675|]
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C-type lectin domain family 12 member B isoform X2 [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

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); ...
 142-264 1.34e-41

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: 139.00  E-value: 1.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQlsLTFSFFWLGLSWNSSGRNWLWEDGSF 221
Cdd:cd03593    1 CPKDWICYGNKCYYFS-MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQ--IGSSSYWIGLSREKSEKPWKWIDGSP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568942883 222 PPPTLlsdkELASFNGSRECAYFERGNIYTSRCRAEIPWICEK 264
Cdd:cd03593   78 LNNLF----NIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 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); ...
 142-264 1.34e-41

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: 139.00  E-value: 1.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQlsLTFSFFWLGLSWNSSGRNWLWEDGSF 221
Cdd:cd03593    1 CPKDWICYGNKCYYFS-MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQ--IGSSSYWIGLSREKSEKPWKWIDGSP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568942883 222 PPPTLlsdkELASFNGSRECAYFERGNIYTSRCRAEIPWICEK 264
Cdd:cd03593   78 LNNLF----NIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 142-263 3.34e-27

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: 102.29  E-value: 3.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883   142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLS--LTFSFFWLGLSWNSSGRNWLWEDG 219
Cdd:smart00034   1 CPSGWISYGGKCYKFS-TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsGSSDYYWIGLSDPDSNGSWQWSDG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568942883   220 SfPPPTLLSDKELASFNGSRECAYF--ERGNIYTSRCRAEIPWICE 263
Cdd:smart00034  80 S-GPVSYSNWAPGEPNNSSGDCVVLstSGGKWNDVSCTSKLPFVCE 124
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 142-264 6.19e-15

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 71.69  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSltFSFFWLGLSWNSSGRNWLWEDGSF 221
Cdd:PHA02642  88 CPKGWIGFGYKCFYFS-EDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKD--SSDHWIGLNRESSNHPWKWADNSN 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568942883 222 PPPTLLsdkelasFNGSRECAYFERGNIYTSRCRAEIPWICEK 264
Cdd:PHA02642 165 YNASFV-------ITGTGECAYLNDIRISSSRVYANRKWICSK 200
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 162-264 1.33e-13

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 65.58  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883  162 KSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSLTFSFFWLGLSWNSSGRNWLWEDGSfpPPTLLSDKELASFNGSRE- 240
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGS--PVNYTNWAPEPNNNGENEd 79

                          90       100
                  ....*....|....*....|....*.
gi 568942883  241 CAYFERGN--IYTSRCRAEIPWICEK 264
Cdd:pfam00059  80 CVELSSSSgkWNDENCNSKNPFVCEK 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); ...
 142-264 1.34e-41

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: 139.00  E-value: 1.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQlsLTFSFFWLGLSWNSSGRNWLWEDGSF 221
Cdd:cd03593    1 CPKDWICYGNKCYYFS-MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQ--IGSSSYWIGLSREKSEKPWKWIDGSP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568942883 222 PPPTLlsdkELASFNGSRECAYFERGNIYTSRCRAEIPWICEK 264
Cdd:cd03593   78 LNNLF----NIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 142-263 3.34e-27

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: 102.29  E-value: 3.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883   142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLS--LTFSFFWLGLSWNSSGRNWLWEDG 219
Cdd:smart00034   1 CPSGWISYGGKCYKFS-TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsGSSDYYWIGLSDPDSNGSWQWSDG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568942883   220 SfPPPTLLSDKELASFNGSRECAYF--ERGNIYTSRCRAEIPWICE 263
Cdd:smart00034  80 S-GPVSYSNWAPGEPNNSSGDCVVLstSGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 152-264 1.34e-22

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: 89.60  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 152 SCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSLT-FSFFWLGLSWNSSGRNWLWEDGSFPPPTLLSDK 230
Cdd:cd00037    1 SCYKFS-TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSsSSDVWIGLNDLSSEGTWKWSDGSPLVDYTNWAP 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568942883 231 ELASFNGSRECAYF---ERGNIYTSRCRAEIPWICEK 264
Cdd:cd00037   80 GEPNPGGSEDCVVLsssSDGKWNDVSCSSKLPFICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 142-264 4.55e-20

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: 83.51  E-value: 4.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSLTFsFFWLGLSWNSSGRNWLWEDGSf 221
Cdd:cd03590    1 CPTNWKSFQSSCYFFS-TEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNR-SYWIGLSDEETEGEWKWVDGT- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568942883 222 PPPTLLS---DKELASFNGSRE-CAYF--ERGNIYTSRCRAEIPWICEK 264
Cdd:cd03590   78 PLNSSKTfwhPGEPNNWGGGGEdCAELvyDSGGWNDVPCNLEYRWICEK 126
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 142-264 6.19e-15

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 71.69  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSltFSFFWLGLSWNSSGRNWLWEDGSF 221
Cdd:PHA02642  88 CPKGWIGFGYKCFYFS-EDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKD--SSDHWIGLNRESSNHPWKWADNSN 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568942883 222 PPPTLLsdkelasFNGSRECAYFERGNIYTSRCRAEIPWICEK 264
Cdd:PHA02642 165 YNASFV-------ITGTGECAYLNDIRISSSRVYANRKWICSK 200
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 162-264 1.33e-13

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 65.58  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883  162 KSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSLTFSFFWLGLSWNSSGRNWLWEDGSfpPPTLLSDKELASFNGSRE- 240
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGS--PVNYTNWAPEPNNNGENEd 79

                          90       100
                  ....*....|....*....|....*.
gi 568942883  241 CAYFERGN--IYTSRCRAEIPWICEK 264
Cdd:pfam00059  80 CVELSSSSgkWNDENCNSKNPFVCEK 105
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 142-263 5.82e-10

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: 55.84  E-value: 5.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCY-YFSIneEKSWSDSRKDC--IDKNATLVKIDSTEERDLLQSQLS---LTFSFFWLGLSWNSSGRNWL 215
Cdd:cd03594    1 CPKGWLPYKGNCYgYFRQ--PLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISsyqKAYQPVWIGLHDPQQSRGWE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568942883 216 WEDGSFPPPTLLSDKElaSFNGSRECAYFERGNIYTS----RCRAEIPWICE 263
Cdd:cd03594   79 WSDGSKLDYRSWDRNP--PYARGGYCAELSRSTGFLKwndaNCEERNPFICK 128
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 154-262 5.15e-08

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: 50.06  E-value: 5.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 154 YYFsINEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSLTFSFFWLGLSWNSSgrNWLWEDGSfpPPTLLSDKELA 233
Cdd:cd03602    3 FYL-VNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVD--SWRWSDGS--ESSFRNWNTFQ 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 568942883 234 SFNGSrECAYFE-RGNIYTSRCRAEIPWIC 262
Cdd:cd03602   78 PFGQG-DCATMYsSGRWYAALCSALKPFIC 106
PHA02867 PHA02867
C-type lectin protein; Provisional
 142-264 4.14e-07

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 48.91  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSINeEKSWSDSRKDCIDKNATLVKIDSTEERDLLqsqlsltfsffwlglswNSSGRNWLW-EDGS 220
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTIN-ETNWNDSKKLCDVMDSSLIRFDNIETLNFV-----------------SRYGKGSYWiDINQ 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568942883 221 FPPPTLLSDKELASFNGSRECAYFERGNIYTSRCRAEIPWICEK 264
Cdd:PHA02867 111 NRKIPGINFSLYYEQGVNDICLLFDTSNIIEMSCIFHERTICVK 154
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 142-220 5.07e-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: 48.12  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCY-YFsiNEEKSWSDSRKDCID-----KNATLVKIDSTEERDLLqsqlsltFSFF------------WL 203
Cdd:cd03589    1 CPTFWTAFGGYCYrFF--GDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFV-------YDLFessrgpdtpyglWI 71

                         90
                 ....*....|....*..
gi 568942883 204 GLSWNSSGRNWLWEDGS 220
Cdd:cd03589   72 GLHDRTSEGPFEWTDGS 88
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 154-220 1.43e-06

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: 46.26  E-value: 1.43e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942883 154 YYFSINEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSlTFSFFWLGLSWNSSGRNWLWEDGS 220
Cdd:cd03603    2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFG-GYGASWIGASDAATEGTWKWSDGE 67
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 142-262 1.90e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 41.00  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 142 CPKTWQWYGNSCYYFSINEEKSWSDSRKdCIDKNATLVKIDSTEERDLLQSQLSLtfSFFWLGLSWNSSgrnwlWEDGSF 221
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIER-CADMDGILTLIDDQKEVLFVSRYKGG--QDLWIGIEKKKG-----DDDDRE 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568942883 222 PPPTLLSDKelasfnGSRECAYFERGNIYTSRCRAEIPWIC 262
Cdd:PHA03097 118 VLDKVVKPP------KSGKCAYLKDKTIISSNCNATKGWIC 152
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 150-263 4.96e-03

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 36.21  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942883 150 GNSCYYFSiNEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSLTF---SFFWLGLSWNSSGRNWLWEDGSfpPPTL 226
Cdd:cd03596    8 HKKCYLVS-EETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVpgnWEVWLGINDMVAEGKWVDVNGS--PISY 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568942883 227 LS-DKELASF--NGSRE-CAYF---ERGNIYTSRCRAEIPWICE 263
Cdd:cd03596   85 FNwEREITAQpdGGKREnCVALsssAQGKWFDEDCRREKPYVCE 128
 
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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