SCARB1

The protein encoded by this gene is a plasma membrane receptor for high density lipoprotein cholesterol (HDL). The encoded protein mediates cholesterol transfer to and from HDL. In addition, this protein is a receptor for hepatitis C virus glycoprotein E2. Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Mar 2011]

Scavenger Receptor Class B Member 1

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.

Biological Process adhesion of symbiont to hostManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process blood vessel endothelial cell migrationIEA:Ensembl
Biological Process carotenoid transportIEA:Ensembl
Biological Process cholesterol catabolic processIEA:Ensembl
Biological Process cholesterol effluxManual Assertion Based On ExperimentIMP:AgBase
Biological Process cholesterol homeostasisISS:BHF-UCL
Biological Process cholesterol importManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process detection of lipopolysaccharideManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process endothelial cell proliferationIEA:Ensembl
Biological Process high-density lipoprotein particle clearanceManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process high-density lipoprotein particle remodelingISS:BHF-UCL
Biological Process intestinal lipid absorptionIEA:Ensembl
Biological Process lipopolysaccharide transportManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process low-density lipoprotein particle clearanceISS:BHF-UCL
Biological Process phospholipid transportISS:BHF-UCL
Biological Process plasma lipoprotein particle clearanceManual Assertion Based On ExperimentIBA:GO_Central
Biological Process positive regulation of cholesterol storageManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process positive regulation of endothelial cell migrationManual Assertion Based On ExperimentTAS:BHF-UCL
Biological Process positive regulation of nitric-oxide synthase activityManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process positive regulation of triglyceride biosynthetic processISS:BHF-UCL
Biological Process recognition of apoptotic cellManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process regulation of phagocytosis1 PublicationIC:BHF-UCL
Biological Process regulation of phosphatidylcholine catabolic processISS:BHF-UCL
Biological Process reverse cholesterol transportManual Assertion Based On ExperimentIEP:BHF-UCL
Biological Process triglyceride homeostasisISS:BHF-UCL
Biological Process vitamin transmembrane transportManual Assertion Based On ExperimentIMP:AgBase
Biological Process wound healingManual Assertion Based On ExperimentTAS:BHF-UCL

Cell membrane
Membrane, caveola
Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae.

Cytoplasmic: 1-11
Helical: 12-32
Extracellular: 33-443
Helical: 444-464
Cytoplasmic: 465-552

N-glycosylated.
The six cysteines of the extracellular domain are all involved in intramolecular disulfide bonds.