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UniProt functional annotation for Q9P126 | ||
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| UniProt code: Q9P126. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
C-type lectin-like receptor that functions as a platelet receptor for the lymphatic endothelial marker, PDPN (PubMed:18215137). After ligand activation, signals via sequential activation of SRC and SYK tyrosine kinases leading to activation of PLCG2 (PubMed:18955485). {ECO:0000269|PubMed:18215137, ECO:0000269|PubMed:18955485}. |
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| Function: | |
(Microbial infection) Acts as a receptor for the platelet- aggregating snake venom protein rhodocytin. Rhodocytin binding leads to tyrosine phosphorylation and this promotes the binding of spleen tyrosine kinase (SYK) and initiation of downstream tyrosine phosphorylation events and activation of PLCG2 (PubMed:16174766, PubMed:18955485). {ECO:0000269|PubMed:18955485, ECO:0000305|PubMed:16174766}. |
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| Function: | |
(Microbial infection) Acts as an attachment factor for Human immunodeficiency virus type 1 (HIV-1) and facilitates its capture by platelets (PubMed:16940507). {ECO:0000305|PubMed:16940507}. |
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| Subunit: | |
Homodimer. Interacts (via cytoplasmic domain) with RACK1; promotes CLEC1B ubiquitination and proteasome-mediated degradation. Interacts (dimer) with SYK (via SH2 domains). Interacts with PDPN; the interaction is independent of CLEC1B glycosylation and activates CLEC1B (PubMed:18215137). {ECO:0000269|PubMed:17132623, ECO:0000269|PubMed:18215137, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:19824697, ECO:0000269|PubMed:20154219}. |
| Subcellular location: | |
Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. |
| Tissue specificity: | |
Expressed preferentially in the liver. Also expressed in immune cells of myeloid origin and on the surface of platelets. {ECO:0000269|PubMed:10671229, ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:16940507}. |
| Ptm: | |
Glycosylated. {ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:18215137}. |
| Ptm: | |
Phosphorylated on tyrosine residue in response to rhodocytin binding. {ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:20154219}. |
Annotations taken from UniProtKB at the EBI.