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MGP004718

UniProt Annotations

Entry Information
Gene NameC-type lectin domain family 5, member A
Protein EntryCLC5A_HUMAN
UniProt IDQ9NY25
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NY25-1; Sequence=Displayed; Name=2; IsoId=Q9NY25-2; Sequence=VSP_012839;
FunctionFunctions as a positive regulator of osteoclastogenesis. Cell surface receptor that signals via TYROBP. Regulates inflammatory responses. Acts as a key regulator of synovial injury and bone erosion during autoimmune joint inflammation (By similarity). Critical macrophage receptor for dengue virus serotypes 1-4. The binding of dengue virus to CLEC5A triggers signaling through the phosphylation of TYROBP, this interaction does not result in viral entry, but stimulates proinflammatory cytokine release. {ECO:0000250, ECO:0000269|PubMed:10449773, ECO:0000269|PubMed:18496526}.
PtmN-glycosylated. Contains sialic acid residues (By similarity). {ECO:0000250}.
SimilarityContains 1 C-type lectin domain. {ECO:0000255|PROSITE- ProRule:PRU00040}.
Subcellular LocationCell membrane {ECO:0000269|PubMed:21566123}; Single-pass type II membrane protein {ECO:0000269|PubMed:21566123}.
SubunitMonomer. Homodimer. The majority of CLEC5A is expressed as a monomeric form on macrophages. Interacts with TYROBP/DAP12. The interaction with TYROBP is required for CLEC5 cell surface expression. Interacts with HCST/DAP10. Forms an CLEC5A/TYROBP/HCST trimolecular complex depending almost solely on TYROBP. {ECO:0000269|PubMed:10449773, ECO:0000269|PubMed:21566123}.
Tissue SpecificityExpressed in peripheral blood monocytes and in the monocyte/macrophage cell lines U-937 and Mono-Mac-6, but not in cell lines of other origins. Expression is down-regulated when monocytes differentiate into dendritic cells. {ECO:0000269|PubMed:10449773}.
Web ResourceName=Functional Glycomics Gateway - Glycan Binding; Note=MDL-1; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_244";
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