SCARB1
Function
Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells (PubMed:12016218, PubMed:12519372, PubMed:21226579). Receptor for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux (PubMed:26965621). Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity (PubMed:12016218).
(Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes and appears to facilitate its cell entry (PubMed:12356718, PubMed:12913001, PubMed:18000990). Binding between SCARB1 and the hepatitis C virus glycoprotein E2 is independent of the genotype of the viral isolate (PubMed:12356718).
(Microbial infection) Mediates uptake of M.fortuitum, E.coli and S.aureus.
(Microbial infection) Facilitates the entry of human coronavirus SARS-CoV-2 by acting as an entry cofactor through HDL binding.
Post-translational modifications
N-glycosylated.
The six cysteines of the extracellular domain are all involved in intramolecular disulfide bonds.
Sequence Similarities
Belongs to the CD36 family.
Tissue Specificity
Widely expressed.
Cellular localization
- Cell membrane
- Multi-pass membrane protein
- Membrane
- Caveola
- Multi-pass membrane protein
- Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae.
Alternative names
CD36, CD36L1, CLA1, SCARB1, Scavenger receptor class B member 1, SRB1, CD36 and LIMPII analogous 1, CD36 antigen-like 1, SR-BI, CLA-1