Q9BXN2 · CLC7A_HUMAN
- ProteinC-type lectin domain family 7 member A
- GeneCLEC7A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids247 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lectin that functions as a pattern recognizing receptor (PRR) specific for beta-1,3-linked and beta-1,6-linked glucans, which constitute cell wall constituents from pathogenic bacteria and fungi (PubMed:11567029, PubMed:12423684).
Necessary for the TLR2-mediated inflammatory response and activation of NF-kappa-B: upon beta-glucan binding, recruits SYK via its ITAM motif and promotes a signaling cascade that activates some CARD domain-BCL10-MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (By similarity).
Enhances cytokine production in macrophages and dendritic cells (By similarity).
Mediates production of reactive oxygen species in the cell (By similarity).
Mediates phagocytosis of C.albicans conidia (PubMed:17230442).
Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity).
Necessary for the TLR2-mediated inflammatory response and activation of NF-kappa-B: upon beta-glucan binding, recruits SYK via its ITAM motif and promotes a signaling cascade that activates some CARD domain-BCL10-MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (By similarity).
Enhances cytokine production in macrophages and dendritic cells (By similarity).
Mediates production of reactive oxygen species in the cell (By similarity).
Mediates phagocytosis of C.albicans conidia (PubMed:17230442).
Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 146-153 | (1,3-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: RQCWQLGS | ||||||
Binding site | 157 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 159 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 163 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 195 | (1,3-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 242 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameC-type lectin domain family 7 member A
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BXN2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-44 | Cytoplasmic | ||||
Sequence: MEYHPDLENLDEDGYTQLHFDSQSNTRIAVVSEKGSCAASPPWR | ||||||
Transmembrane | 45-65 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LIAVILGILCLVILVIAVVLG | ||||||
Topological domain | 66-247 | Extracellular | ||||
Sequence: TMAIWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGVLSSPCPPNWIIYEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKIDSSNELGFIVKQVSSQPDNSFWIGLSRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQLCSVPSYSICEKKFSM |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Candidiasis, familial, 4 (CANDF4)
- Note
- DescriptionA primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
- See alsoMIM:613108
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050111 | 223 | in dbSNP:rs16910527 | |||
Sequence: I → S | ||||||
Natural variant | VAR_084643 | 238-247 | probable risk factor for invasive aspergillosis | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 320 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000269491 | 1-247 | C-type lectin domain family 7 member A | |||
Sequence: MEYHPDLENLDEDGYTQLHFDSQSNTRIAVVSEKGSCAASPPWRLIAVILGILCLVILVIAVVLGTMAIWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGVLSSPCPPNWIIYEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKIDSSNELGFIVKQVSSQPDNSFWIGLSRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQLCSVPSYSICEKKFSM | ||||||
Glycosylation | 91 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 120↔131 | |||||
Sequence: CPPNWIIYEKSC | ||||||
Disulfide bond | 148↔241 | |||||
Sequence: CWQLGSNLLKIDSSNELGFIVKQVSSQPDNSFWIGLSRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQLCSVPSYSIC | ||||||
Disulfide bond | 220↔233 | |||||
Sequence: CVWIHVSVIYDQLC |
Post-translational modification
Phosphorylated on tyrosine residues in response to beta-glucan binding.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in peripheral blood leukocytes and dendritic cells. Detected in spleen, bone marrow, lung, muscle, stomach and placenta.
Induction
Up-regulated during differentiation from monocytes into dendritic cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer. Interacts with SYK; participates in leukocyte activation in presence of fungal pathogens. Interacts with CD37; this interaction controls CLEC7A-mediated IL-6 production (PubMed:17182550).
Isoform 5
Interacts with RANBP9.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 15-18 | ITAM-like | ||||
Sequence: YTQL | ||||||
Domain | 127-242 | C-type lectin | ||||
Sequence: YEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKIDSSNELGFIVKQVSSQPDNSFWIGLSRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQLCSVPSYSICE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 10 isoforms produced by Alternative splicing.
Q9BXN2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsA
- Length247
- Mass (Da)27,627
- Last updated2001-06-01 v1
- Checksum98393E36976111B9
Q9BXN2-2
- Name2
- SynonymsBeta, B
- NotePredominant isoform.
- Differences from canonical
- 68-113: Missing
Q9BXN2-3
- Name3
- SynonymsC
Q9BXN2-4
- Name4
- SynonymsG
Q9BXN2-5
- Name5
- SynonymsE
- Differences from canonical
- 36-114: Missing
Q9BXN2-6
- Name6
Q9BXN2-7
- Name7
- SynonymsD
Q9BXN2-8
- Name8
- SynonymsF
Q9BXN2-9
- Name9
Q9BXN2-10
- Name10
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q68D78 | Q68D78_HUMAN | CLEC7A | 136 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 31 | in Ref. 4; AAL11714 | ||||
Sequence: V → I | ||||||
Alternative sequence | VSP_022049 | 36-45 | in isoform 8 | |||
Sequence: SCAASPPWRL → IYSKTSVFPT | ||||||
Alternative sequence | VSP_022048 | 36-114 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022050 | 46-247 | in isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022051 | 68-113 | in isoform 2, isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047589 | 68-116 | in isoform 10 | |||
Sequence: AIWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGVL → GTGQFLKDLSFLNNRRKLFGDPIQEATHWRMATFYQEIKRTTVNPHNHL | ||||||
Alternative sequence | VSP_043298 | 69-77 | in isoform 9 | |||
Sequence: IWRSNSGSN → GFKAVEFKG | ||||||
Alternative sequence | VSP_043299 | 78-247 | in isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047590 | 117-247 | in isoform 10 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022054 | 165-178 | in isoform 6 | |||
Sequence: GFIVKQVSSQPDNS → VSVDFCYDYLWCVS | ||||||
Alternative sequence | VSP_022053 | 165-189 | in isoform 3 and isoform 7 | |||
Sequence: GFIVKQVSSQPDNSFWIGLSRPQTE → ISDQNHSYPRKPISKLCMDSRVSHL | ||||||
Alternative sequence | VSP_022052 | 165-196 | in isoform 4 | |||
Sequence: GFIVKQVSSQPDNSFWIGLSRPQTEVPWLWED → SLTLLPKLECSEAATSQAQVILPPQLPE | ||||||
Alternative sequence | VSP_022055 | 179-247 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022056 | 190-247 | in isoform 3 and isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022057 | 197-247 | in isoform 4 | |||
Sequence: Missing |
Polymorphism
A stop polymorphism at position 238 may be associated with invasive aspergillosis following hematopoietic stem cell transplantation (PubMed:20807886).
The risk is highest when the polymorphism is present in both donors and recipients [MIM:614079] (PubMed:20807886).
The risk is highest when the polymorphism is present in both donors and recipients [MIM:614079] (PubMed:20807886).
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY026769 EMBL· GenBank· DDBJ | AAK20114.2 EMBL· GenBank· DDBJ | mRNA | ||
AY026770 EMBL· GenBank· DDBJ | AAK20115.1 EMBL· GenBank· DDBJ | mRNA | ||
AY026771 EMBL· GenBank· DDBJ | AAK20116.1 EMBL· GenBank· DDBJ | mRNA | ||
AF313468 EMBL· GenBank· DDBJ | AAK37473.1 EMBL· GenBank· DDBJ | mRNA | ||
AF313469 EMBL· GenBank· DDBJ | AAK37474.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400595 EMBL· GenBank· DDBJ | AAL11711.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400596 EMBL· GenBank· DDBJ | AAL11712.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400597 EMBL· GenBank· DDBJ | AAL11713.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400598 EMBL· GenBank· DDBJ | AAL11714.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400599 EMBL· GenBank· DDBJ | AAL11715.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400600 EMBL· GenBank· DDBJ | AAL11716.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400601 EMBL· GenBank· DDBJ | AAL11717.1 EMBL· GenBank· DDBJ | mRNA | ||
AF400602 EMBL· GenBank· DDBJ | AAL11718.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ312372 EMBL· GenBank· DDBJ | CAC43846.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ312373 EMBL· GenBank· DDBJ | CAC43847.1 EMBL· GenBank· DDBJ | mRNA | ||
AY009090 EMBL· GenBank· DDBJ | AAG33923.2 EMBL· GenBank· DDBJ | mRNA | ||
AY359002 EMBL· GenBank· DDBJ | AAQ89361.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297028 EMBL· GenBank· DDBJ | BAH12480.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298679 EMBL· GenBank· DDBJ | BAH12845.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298724 EMBL· GenBank· DDBJ | BAH12855.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313247 EMBL· GenBank· DDBJ | BAG36058.1 EMBL· GenBank· DDBJ | mRNA | ||
AC024224 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471094 EMBL· GenBank· DDBJ | EAW96144.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471094 EMBL· GenBank· DDBJ | EAW96145.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471094 EMBL· GenBank· DDBJ | EAW96146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471094 EMBL· GenBank· DDBJ | EAW96150.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471094 EMBL· GenBank· DDBJ | EAW96154.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC013385 EMBL· GenBank· DDBJ | AAH13385.1 EMBL· GenBank· DDBJ | mRNA | ||
BC071746 EMBL· GenBank· DDBJ | AAH71746.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093829 EMBL· GenBank· DDBJ | AAH93829.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093831 EMBL· GenBank· DDBJ | AAH93831.1 EMBL· GenBank· DDBJ | mRNA |