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Conserved domains on  [gi|2168985279|ref|NP_032553|]
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killer cell lectin-like receptor subfamily B member 1C isoform 2 [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); ...
 91-209 2.55e-43

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: 141.70  E-value: 2.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  91 CPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEkyNSFWIGLRFTLPDMNWKWINGTTF 170
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2168985279 171 NSDvLKITGVTENGSCASILGDKVTPESCASDNRWICQK 209
Cdd:cd03593    79 NNL-FNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 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); ...
 91-209 2.55e-43

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: 141.70  E-value: 2.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  91 CPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEkyNSFWIGLRFTLPDMNWKWINGTTF 170
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2168985279 171 NSDvLKITGVTENGSCASILGDKVTPESCASDNRWICQK 209
Cdd:cd03593    79 NNL-FNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 91-208 2.04e-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: 101.14  E-value: 2.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279   91 CPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKE--KYNSFWIGLRFTLPDMNWKWINGT 168
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2168985279  169 TFNSDVLKITG--VTENGSCASILGDKVT--PESCASDNRWICQ 208
Cdd:smart00034  81 GPVSYSNWAPGepNNSSGDCVVLSTSGGKwnDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 109-209 2.25e-22

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 87.53  E-value: 2.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279 109 SNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLK--ITGVTENGSC 186
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWApePNNNGENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 2168985279 187 ASILGD--KVTPESCASDNRWICQK 209
Cdd:pfam00059  81 VELSSSsgKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 42-220 2.21e-16

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 74.77  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  42 KLSCAGLILLVLTLIGMSVLVRVLVqkpsrekccvFIQENLNKTTVNLECPQDWLLHRDKCFHVSQVSNTWEEGQADCGR 121
Cdd:PHA02642   49 KLYCCIITICILITINLVPIIILMA----------FKSDTQEPTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279 122 KGATLLLIQDQEELRFLldSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLkitgVTENGSCASILGDKVTPESCAS 201
Cdd:PHA02642  119 LGATLVKVETEEELNFL--KRYKDSSDHWIGLNRESSNHPWKWADNSNYNASFV----ITGTGECAYLNDIRISSSRVYA 192

                         170       180
                  ....*....|....*....|
gi 2168985279 202 DNRWICQKEL-NHETPSNDS 220
Cdd:PHA02642  193 NRKWICSKTYtNIYIPSNNS 212
 
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); ...
 91-209 2.55e-43

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: 141.70  E-value: 2.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  91 CPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEkyNSFWIGLRFTLPDMNWKWINGTTF 170
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2168985279 171 NSDvLKITGVTENGSCASILGDKVTPESCASDNRWICQK 209
Cdd:cd03593    79 NNL-FNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 91-208 2.04e-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: 101.14  E-value: 2.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279   91 CPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKE--KYNSFWIGLRFTLPDMNWKWINGT 168
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2168985279  169 TFNSDVLKITG--VTENGSCASILGDKVT--PESCASDNRWICQ 208
Cdd:smart00034  81 GPVSYSNWAPGepNNSSGDCVVLSTSGGKwnDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 109-209 2.25e-22

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 87.53  E-value: 2.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279 109 SNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLK--ITGVTENGSC 186
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWApePNNNGENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 2168985279 187 ASILGD--KVTPESCASDNRWICQK 209
Cdd:pfam00059  81 VELSSSsgKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 101-209 6.98e-20

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 81.51  E-value: 6.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279 101 KCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNS-FWIGLRFTLPDMNWKWINGTTFNSDVL---K 176
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGSPLVDYTNwapG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2168985279 177 ITGVTENGSCASILGD---KVTPESCASDNRWICQK 209
Cdd:cd00037    81 EPNPGGSEDCVVLSSSsdgKWNDVSCSSKLPFICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 91-209 1.88e-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: 80.43  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  91 CPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKyNSFWIGLRFTLPDMNWKWINGTTF 170
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGN-RSYWIGLSDEETEGEWKWVDGTPL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2168985279 171 NSDVL--------KITGVTENgsCASILGDKVT--PESCASDNRWICQK 209
Cdd:cd03590    80 NSSKTfwhpgepnNWGGGGED--CAELVYDSGGwnDVPCNLEYRWICEK 126
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 42-220 2.21e-16

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 74.77  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  42 KLSCAGLILLVLTLIGMSVLVRVLVqkpsrekccvFIQENLNKTTVNLECPQDWLLHRDKCFHVSQVSNTWEEGQADCGR 121
Cdd:PHA02642   49 KLYCCIITICILITINLVPIIILMA----------FKSDTQEPTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279 122 KGATLLLIQDQEELRFLldSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLkitgVTENGSCASILGDKVTPESCAS 201
Cdd:PHA02642  119 LGATLVKVETEEELNFL--KRYKDSSDHWIGLNRESSNHPWKWADNSNYNASFV----ITGTGECAYLNDIRISSSRVYA 192

                         170       180
                  ....*....|....*....|
gi 2168985279 202 DNRWICQKEL-NHETPSNDS 220
Cdd:PHA02642  193 NRKWICSKTYtNIYIPSNNS 212
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 91-171 1.63e-09

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: 53.91  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  91 CPQDWLLHRDKCFHVSQVSNTWEEGQADCGR--KGATLLLIQDQEELRFL---LDSIKEKYNSFWIGLRFTLPDMNWKWI 165
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIaslISSYQKAYQPVWIGLHDPQQSRGWEWS 80


                  ....*.
gi 2168985279 166 NGTTFN 171
Cdd:cd03594    81 DGSKLD 86
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 91-171 3.91e-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: 50.43  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  91 CPQDWLLHRDKCFHVSQVSNTWEEGQADC-----GRKGATLLLIQDQEELRFLLD---SIKEK--YNSFWIGLRFTLPDM 160
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCrsfsiPGLIAHLVSIHSQEENDFVYDlfeSSRGPdtPYGLWIGLHDRTSEG 80

                          90
                  ....*....|.
gi 2168985279 161 NWKWINGTTFN 171
Cdd:cd03589    81 PFEWTDGSPVD 91
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 41-207 8.14e-06

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 44.47  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  41 LKLSCAGLILLVLT-----LIGMSVLVRVLVQKPSrekccvfiQENLNKttvnLECPQDWLLHRDKCFHVSQVSNTWEEG 115
Cdd:PHA03097    3 EKKCCKVTVHWILVpcgsiIIALIALVIILSCKLS--------PGDRSG----LNCRSGWVGYNNKCYTFSENITNKHLA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279 116 QADCGRKGATLLLIQDQEELRFLLDSIKEKynSFWIGLRFTLPDMNWKWINGttfnsdvlKITGVTENGSCASILGDKVT 195
Cdd:PHA03097   71 IERCADMDGILTLIDDQKEVLFVSRYKGGQ--DLWIGIEKKKGDDDDREVLD--------KVVKPPKSGKCAYLKDKTII 140

                         170
                  ....*....|..
gi 2168985279 196 PESCASDNRWIC 207
Cdd:PHA03097  141 SSNCNATKGWIC 152
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 111-207 1.06e-05

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: 43.13  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279 111 TWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLRFTLpdMNWKWINGTTFNSDVLKITGVTENGSCASIL 190
Cdd:cd03602    11 TWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDV--DSWRWSDGSESSFRNWNTFQPFGQGDCATMY 88

                          90
                  ....*....|....*...
gi 2168985279 191 GD-KVTPESCASDNRWIC 207
Cdd:cd03602    89 SSgRWYAALCSALKPFIC 106
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 97-208 2.58e-05

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: 42.38  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  97 LHRdKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNS---FWIGLRFTLPDMNWKWING---TTF 170
Cdd:cd03596     7 IHK-KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGnweVWLGINDMVAEGKWVDVNGspiSYF 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2168985279 171 NSDVLKIT----GVTENgsCASILGD---KVTPESCASDNRWICQ 208
Cdd:cd03596    86 NWEREITAqpdgGKREN--CVALSSSaqgKWFDEDCRREKPYVCE 128
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 103-169 3.13e-05

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: 42.03  E-value: 3.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168985279 103 FHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLdSIKEKYNSFWIGLRFTLPDMNWKWINGTT 169
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLL-SNFGGYGASWIGASDAATEGTWKWSDGEE 68
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 103-166 5.27e-04

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 38.51  E-value: 5.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168985279 103 FHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKeKYNS--FWIGLRftlpDMN--WKWIN 166
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFAL-KYNLgyYWIDGN----DINneGTWVD 65
PHA02867 PHA02867
C-type lectin protein; Provisional
 75-213 4.01e-03

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 36.58  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985279  75 CVFIQENLNKTtvnleCPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYnsfWIGLR 154
Cdd:PHA02867   38 WYYAFPYFSKV-----CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRYGKGSY---WIDIN 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168985279 155 FTlpdMNWKWINGTTFNSdvlkitgVTENGSCASILGDKVTPESCASDNRWICQKELNH 213
Cdd:PHA02867  110 QN---RKIPGINFSLYYE-------QGVNDICLLFDTSNIIEMSCIFHERTICVKEDRY 158
 
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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