NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039774400|ref|XP_017176906|]
View 

killer cell lectin-like receptor 6 isoform X2 [Mus musculus]

Protein Classification

Ly49 and CLECT_NK_receptors_like domain-containing protein( domain architecture ID 10551997)

Ly49 and CLECT_NK_receptors_like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 40-154 3.99e-63

Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or are similar to, Ly49 receptors. These are type II transmembrane receptors expressed by mouse natural killer (NK) cells. They are classified as being activating (e.g.Ly49D and H) or inhibitory (e.g. Ly49A and G), depending on their effect on NK cell function. They are members of the C-type lectin receptor superfamily, and in fact in many family members this region is found immediately N-terminal to a lectin C-type domain (pfam00059).


:

Pssm-ID: 462461 [Multi-domain]  Cd Length: 119  Bit Score: 193.73  E-value: 3.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400  40 WQLIVKALGILCFLLLITVAVLAVKIFQYGQHNQEIHETLNYHHNCSNMQSDFNLKEEMLTNRSIDSRPGNELLESLNRE 119
Cdd:pfam08391   4 WHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLNLHQNCSIMQNDIYLKEEMLRNKSIECSILNNLLDSLNRE 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774400 120 QNRGYSETKTDLDSSQDTGTGVK-YWFCYRTKCYYF 154
Cdd:pfam08391  84 QNRWYRKTKTVLKSLQHTGKGVEiHWFCYGIKCYYF 119
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 142-256 4.30e-45

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: 147.48  E-value: 4.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 142 KYWFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDSYWIGLSYDKEKKEWAWIDNGQSKLDM 221
Cdd:cd03593     3 KDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNNLF 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039774400 222 KIRKMNfKPGGCVFLSKRRLEDTNCKNSHYCICGK 256
Cdd:cd03593    83 NIRGST-KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
 
Name Accession Description Interval E-value
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 40-154 3.99e-63

Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or are similar to, Ly49 receptors. These are type II transmembrane receptors expressed by mouse natural killer (NK) cells. They are classified as being activating (e.g.Ly49D and H) or inhibitory (e.g. Ly49A and G), depending on their effect on NK cell function. They are members of the C-type lectin receptor superfamily, and in fact in many family members this region is found immediately N-terminal to a lectin C-type domain (pfam00059).


Pssm-ID: 462461 [Multi-domain]  Cd Length: 119  Bit Score: 193.73  E-value: 3.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400  40 WQLIVKALGILCFLLLITVAVLAVKIFQYGQHNQEIHETLNYHHNCSNMQSDFNLKEEMLTNRSIDSRPGNELLESLNRE 119
Cdd:pfam08391   4 WHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLNLHQNCSIMQNDIYLKEEMLRNKSIECSILNNLLDSLNRE 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774400 120 QNRGYSETKTDLDSSQDTGTGVK-YWFCYRTKCYYF 154
Cdd:pfam08391  84 QNRWYRKTKTVLKSLQHTGKGVEiHWFCYGIKCYYF 119
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 142-256 4.30e-45

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: 147.48  E-value: 4.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 142 KYWFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDSYWIGLSYDKEKKEWAWIDNGQSKLDM 221
Cdd:cd03593     3 KDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNNLF 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039774400 222 KIRKMNfKPGGCVFLSKRRLEDTNCKNSHYCICGK 256
Cdd:cd03593    83 NIRGST-KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 144-254 3.33e-22

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 88.81  E-value: 3.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400  144 WFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQV----IPDSYWIGLSYDKEKKEWAWIDNGQSKL 219
Cdd:smart00034   5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDPDSNGSWQWSDGSGPVS 84

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1039774400  220 DMKIRKM--NFKPGGCVFLSKR--RLEDTNCKNSHYCIC 254
Cdd:smart00034  85 YSNWAPGepNNSSGDCVVLSTSggKWNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 158-256 1.11e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 60.18  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 158 KNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQV--IPDSYWIGLSYDKEKKEWAWIDNgqSKLDMKIRKMNFKPGG--- 232
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRKNEGTWKWVDG--SPVNYTNWAPEPNNNGene 78

                          90       100
                  ....*....|....*....|....*..
gi 1039774400 233 -CVFLSKR--RLEDTNCKNSHYCICGK 256
Cdd:pfam00059  79 dCVELSSSsgKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 142-256 7.72e-10

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 57.43  E-value: 7.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 142 KYWFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDSYWIGLSYDKEKKEWAWIDNGQSKLDM 221
Cdd:PHA02642   90 KGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNSNYNASF 169

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039774400 222 KIRKMnfkpGGCVFLSKRRLEDTNCKNSHYCICGK 256
Cdd:PHA02642  170 VITGT----GECAYLNDIRISSSRVYANRKWICSK 200
 
Name Accession Description Interval E-value
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 40-154 3.99e-63

Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or are similar to, Ly49 receptors. These are type II transmembrane receptors expressed by mouse natural killer (NK) cells. They are classified as being activating (e.g.Ly49D and H) or inhibitory (e.g. Ly49A and G), depending on their effect on NK cell function. They are members of the C-type lectin receptor superfamily, and in fact in many family members this region is found immediately N-terminal to a lectin C-type domain (pfam00059).


Pssm-ID: 462461 [Multi-domain]  Cd Length: 119  Bit Score: 193.73  E-value: 3.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400  40 WQLIVKALGILCFLLLITVAVLAVKIFQYGQHNQEIHETLNYHHNCSNMQSDFNLKEEMLTNRSIDSRPGNELLESLNRE 119
Cdd:pfam08391   4 WHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLNLHQNCSIMQNDIYLKEEMLRNKSIECSILNNLLDSLNRE 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774400 120 QNRGYSETKTDLDSSQDTGTGVK-YWFCYRTKCYYF 154
Cdd:pfam08391  84 QNRWYRKTKTVLKSLQHTGKGVEiHWFCYGIKCYYF 119
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 142-256 4.30e-45

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: 147.48  E-value: 4.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 142 KYWFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDSYWIGLSYDKEKKEWAWIDNGQSKLDM 221
Cdd:cd03593     3 KDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNNLF 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039774400 222 KIRKMNfKPGGCVFLSKRRLEDTNCKNSHYCICGK 256
Cdd:cd03593    83 NIRGST-KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 144-254 3.33e-22

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 88.81  E-value: 3.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400  144 WFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQV----IPDSYWIGLSYDKEKKEWAWIDNGQSKL 219
Cdd:smart00034   5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDPDSNGSWQWSDGSGPVS 84

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1039774400  220 DMKIRKM--NFKPGGCVFLSKR--RLEDTNCKNSHYCIC 254
Cdd:smart00034  85 YSNWAPGepNNSSGDCVVLSTSggKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 150-256 2.09e-17

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 75.73  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 150 KCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQV---IPDSYWIGLSYDKEKKEWAWIDNGQSKLDMKIRK- 225
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkksSSSDVWIGLNDLSSEGTWKWSDGSPLVDYTNWAPg 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774400 226 --MNFKPGGCVFLSKR---RLEDTNCKNSHYCICGK 256
Cdd:cd00037    81 epNPGGSEDCVVLSSSsdgKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 158-256 1.11e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 60.18  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 158 KNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQV--IPDSYWIGLSYDKEKKEWAWIDNgqSKLDMKIRKMNFKPGG--- 232
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRKNEGTWKWVDG--SPVNYTNWAPEPNNNGene 78

                          90       100
                  ....*....|....*....|....*..
gi 1039774400 233 -CVFLSKR--RLEDTNCKNSHYCICGK 256
Cdd:pfam00059  79 dCVELSSSsgKWNDENCNSKNPFVCEK 105
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 144-224 2.60e-10

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: 56.93  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 144 WFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFL-QFQVIPDSYWIGLSyDKEKK-EWAWIDNgqSKLDM 221
Cdd:cd03590     5 WKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIsKILSGNRSYWIGLS-DEETEgEWKWVDG--TPLNS 81


                  ...
gi 1039774400 222 KIR 224
Cdd:cd03590    82 SKT 84
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 142-256 7.72e-10

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 57.43  E-value: 7.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 142 KYWFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDSYWIGLSYDKEKKEWAWIDNGQSKLDM 221
Cdd:PHA02642   90 KGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNSNYNASF 169

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039774400 222 KIRKMnfkpGGCVFLSKRRLEDTNCKNSHYCICGK 256
Cdd:PHA02642  170 VITGT----GECAYLNDIRISSSRVYANRKWICSK 200
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 144-254 3.19e-07

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 48.71  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 144 WFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDSYWIGLSYDKekkewAWIDNGQSKLDMKI 223
Cdd:PHA03097   50 WVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKK-----GDDDDREVLDKVVK 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039774400 224 RKmnfKPGGCVFLSKRRLEDTNCKNSHYCIC 254
Cdd:PHA03097  125 PP---KSGKCAYLKDKTIISSNCNATKGWIC 152
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 144-254 1.39e-06

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: 46.60  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 144 WFCYRTKCYYFIMNKNTWSGCKQNCQHY--SLPLVKIDDENELKFL-----QFQVIPDSYWIGLSYDKEKKEWAWIDNgq 216
Cdd:cd03594     5 WLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIaslisSYQKAYQPVWIGLHDPQQSRGWEWSDG-- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039774400 217 SKLDMKI--RKMNFKPGG-CVFLSK----RRLEDTNCKNSHYCIC 254
Cdd:cd03594    83 SKLDYRSwdRNPPYARGGyCAELSRstgfLKWNDANCEERNPFIC 127
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 152-217 1.15e-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: 43.57  E-value: 1.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039774400 152 YYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDS-YWIGLSYDKEKKEWAWIDNGQS 217
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGaSWIGASDAATEGTWKWSDGEES 69
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 152-231 5.40e-05

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: 41.59  E-value: 5.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 152 YYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIP---DSYWIGLsyDKEKKEWAWIDNGQSKLDMKirkmNF 228
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKynlGYYWIDG--NDINNEGTWVDTDKKELEYK----NW 76


                  ...
gi 1039774400 229 KPG 231
Cdd:cd03592    77 APG 79
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 152-254 6.35e-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: 41.21  E-value: 6.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 152 YYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQfQVIPDSY---WIGLSYDKEkkEWAWIDNGQSKLDMKIRKMNF 228
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLS-NLSRVSNsaaWIGLYRDVD--SWRWSDGSESSFRNWNTFQPF 79

                          90       100
                  ....*....|....*....|....*..
gi 1039774400 229 KPGGCVFLSKR-RLEDTNCKNSHYCIC 254
Cdd:cd03602    80 GQGDCATMYSSgRWYAALCSALKPFIC 106
PHA02867 PHA02867
C-type lectin protein; Provisional
 144-256 1.18e-03

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 38.51  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 144 WFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDsYWIglsydkEKKEWAWIDNGQSKLDMKI 223
Cdd:PHA02867   53 WIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRYGKGS-YWI------DINQNRKIPGINFSLYYEQ 125

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039774400 224 RKMNFkpggCVFLSKRRLEDTNCKNSHYCICGK 256
Cdd:PHA02867  126 GVNDI----CLLFDTSNIIEMSCIFHERTICVK 154
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 142-254 1.48e-03

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: 37.72  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774400 142 KYWFCYRTKCYYFIMNKNTWSGCKQNCQHYSLP-----LVKIDDENELKFL-------QFQVIPDSYWIGLSYDKEKKEW 209
Cdd:cd03589     3 TFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVydlfessRGPDTPYGLWIGLHDRTSEGPF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774400 210 AWIDNgqSKLDMKirkmNFKPG---------GCVFLSKR-----RLEDTNCKNSHYCIC 254
Cdd:cd03589    83 EWTDG--SPVDFT----KWAGGqpdnyggneDCVQMWRRgdagqSWNDMPCDAVFPYIC 135
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH