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Scavenger receptor class B member 1 (SRB1) (CD36 and LIMPII analogous 1) (CLA-1) (CD36 antigen-like 1) (Collagen type I receptor, thrombospondin receptor-like 1) (SR-BI) (CD antigen CD36)

 SCRB1_HUMAN             Reviewed;         552 AA.
Q8WTV0; F8W8N0; Q14016; Q52LZ5; Q6KFX4;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
27-SEP-2017, entry version 160.
RecName: Full=Scavenger receptor class B member 1;
Short=SRB1;
AltName: Full=CD36 and LIMPII analogous 1;
Short=CLA-1;
AltName: Full=CD36 antigen-like 1;
AltName: Full=Collagen type I receptor, thrombospondin receptor-like 1;
AltName: Full=SR-BI;
AltName: CD_antigen=CD36;
Name=SCARB1; Synonyms=CD36L1, CLA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Promyelocyte;
PubMed=7689561;
Calvo D., Vega M.;
"Identification, primary structure and distribution of CLA-1, a novel
member of the CD36/LIMPII gene family.";
J. Biol. Chem. 268:18929-18935(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Hirano K., Yamashita S., Matsuzawa Y.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Liver, Prostate, and Rhabdomyosarcoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION (ISOFORM 5).
PubMed=9254074;
Webb N.R., de Villiers W.J., Connell P.M., de Beer F.C.,
van der Westhuyzen D.R.;
"Alternative forms of the scavenger receptor BI (SR-BI).";
J. Lipid Res. 38:1490-1495(1997).
[7]
IDENTIFICATION (ISOFORM 5).
PubMed=9614139;
Webb N.R., Connell P.M., Graf G.A., Smart E.J., de Villiers W.J.,
de Beer F.C., van der Westhuyzen D.R.;
"SR-BII, an isoform of the scavenger receptor BI containing an
alternate cytoplasmic tail, mediates lipid transfer between high
density lipoprotein and cells.";
J. Biol. Chem. 273:15241-15248(1998).
[8]
FUNCTION.
PubMed=12356718; DOI=10.1093/emboj/cdf529;
Scarselli E., Ansuini H., Cerino R., Roccasecca R.M., Acali S.,
Filocamo G., Traboni C., Nicosia A., Cortese R., Vitelli A.;
"The human scavenger receptor class B type I is a novel candidate
receptor for the hepatitis C virus.";
EMBO J. 21:5017-5025(2002).
[9]
FUNCTION, AND GLYCOSYLATION.
PubMed=12016218; DOI=10.1074/jbc.M202879200;
Kawasaki Y., Nakagawa A., Nagaosa K., Shiratsuchi A., Nakanishi Y.;
"Phosphatidylserine binding of class B scavenger receptor type I, a
phagocytosis receptor of testicular Sertoli cells.";
J. Biol. Chem. 277:27559-27566(2002).
[10]
FUNCTION, AND INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER.
PubMed=12913001; DOI=10.1074/jbc.M305289200;
Bartosch B., Vitelli A., Granier C., Goujon C., Dubuisson J.,
Pascale S., Scarselli E., Cortese R., Nicosia A., Cosset F.-L.;
"Cell entry of hepatitis C virus requires a set of co-receptors that
include the CD81 tetraspanin and the SR-B1 scavenger receptor.";
J. Biol. Chem. 278:41624-41630(2003).
[11]
FUNCTION (MICROBIAL INFECTION).
PubMed=16020694; DOI=10.1126/science.1116006;
Philips J.A., Rubin E.J., Perrimon N.;
"Drosophila RNAi screen reveals CD36 family member required for
mycobacterial infection.";
Science 309:1251-1253(2005).
[12]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS C VIRUS
E1 AND E2 GLYCOPROTEINS.
PubMed=18000990; DOI=10.1002/hep.21994;
Zeisel M.B., Koutsoudakis G., Schnober E.K., Haberstroh A., Blum H.E.,
Cosset F.L., Wakita T., Jaeck D., Doffoel M., Royer C., Soulier E.,
Schvoerer E., Schuster C., Stoll-Keller F., Bartenschlager R.,
Pietschmann T., Barth H., Baumert T.F.;
"Scavenger receptor class B type I is a key host factor for hepatitis
C virus infection required for an entry step closely linked to CD81.";
Hepatology 46:1722-1731(2007).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102 AND ASN-330.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[14]
INVOLVEMENT IN HDLCQ16.
PubMed=20686565; DOI=10.1038/nature09270;
Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C.,
Stylianou I.M., Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I.,
Willer C.J., Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M.,
Barbalic M., Ricketts S.L., Bis J.C., Aulchenko Y.S., Thorleifsson G.,
Feitosa M.F., Chambers J., Orho-Melander M., Melander O., Johnson T.,
Li X., Guo X., Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y.,
Park T., Kim K., Sim X., Twee-Hee Ong R., Croteau-Chonka D.C.,
Lange L.A., Smith J.D., Song K., Hua Zhao J., Yuan X., Luan J.,
Lamina C., Ziegler A., Zhang W., Zee R.Y., Wright A.F., Witteman J.C.,
Wilson J.F., Willemsen G., Wichmann H.E., Whitfield J.B.,
Waterworth D.M., Wareham N.J., Waeber G., Vollenweider P.,
Voight B.F., Vitart V., Uitterlinden A.G., Uda M., Tuomilehto J.,
Thompson J.R., Tanaka T., Surakka I., Stringham H.M., Spector T.D.,
Soranzo N., Smit J.H., Sinisalo J., Silander K., Sijbrands E.J.,
Scuteri A., Scott J., Schlessinger D., Sanna S., Salomaa V.,
Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M.,
Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I.,
Perola M., Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N.,
Pare G., Oostra B.A., O'Donnell C.J., Nieminen M.S., Nickerson D.A.,
Montgomery G.W., Meitinger T., McPherson R., McCarthy M.I.,
McArdle W., Masson D., Martin N.G., Marroni F., Mangino M.,
Magnusson P.K., Lucas G., Luben R., Loos R.J., Lokki M.L., Lettre G.,
Langenberg C., Launer L.J., Lakatta E.G., Laaksonen R., Kyvik K.O.,
Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., Kaplan L.M.,
Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., Igl W.,
Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A.,
Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D.,
Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C.,
Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L.,
Erdmann J., Elliott P., Ejebe K.G., Doring A., Dominiczak A.F.,
Demissie S., Deloukas P., de Geus E.J., de Faire U., Crawford G.,
Collins F.S., Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P.,
Bonnycastle L.L., Boomsma D.I., Boekholdt S.M., Bergman R.N.,
Barroso I., Bandinelli S., Ballantyne C.M., Assimes T.L.,
Quertermous T., Altshuler D., Seielstad M., Wong T.Y., Tai E.S.,
Feranil A.B., Kuzawa C.W., Adair L.S., Taylor H.A. Jr., Borecki I.B.,
Gabriel S.B., Wilson J.G., Holm H., Thorsteinsdottir U., Gudnason V.,
Krauss R.M., Mohlke K.L., Ordovas J.M., Munroe P.B., Kooner J.S.,
Tall A.R., Hegele R.A., Kastelein J.J., Schadt E.E., Rotter J.I.,
Boerwinkle E., Strachan D.P., Mooser V., Stefansson K., Reilly M.P.,
Samani N.J., Schunkert H., Cupples L.A., Sandhu M.S., Ridker P.M.,
Rader D.J., van Duijn C.M., Peltonen L., Abecasis G.R., Boehnke M.,
Kathiresan S.;
"Biological, clinical and population relevance of 95 loci for blood
lipids.";
Nature 466:707-713(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493 (ISOFORM 1),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 (ISOFORM 4), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN HDLCQ16, VARIANT
LEU-376, AND CHARACTERIZATION OF VARIANT LEU-376.
PubMed=26965621; DOI=10.1126/science.aad3517;
CHD Exome+ Consortium;
CARDIoGRAM Exome Consortium;
Global Lipids Genetics Consortium;
Zanoni P., Khetarpal S.A., Larach D.B., Hancock-Cerutti W.F.,
Millar J.S., Cuchel M., DerOhannessian S., Kontush A., Surendran P.,
Saleheen D., Trompet S., Jukema J.W., De Craen A., Deloukas P.,
Sattar N., Ford I., Packard C., Majumder A., Alam D.S.,
Di Angelantonio E., Abecasis G., Chowdhury R., Erdmann J.,
Nordestgaard B.G., Nielsen S.F., Tybjaerg-Hansen A., Schmidt R.F.,
Kuulasmaa K., Liu D.J., Perola M., Blankenberg S., Salomaa V.,
Maennistoe S., Amouyel P., Arveiler D., Ferrieres J.,
Mueller-Nurasyid M., Ferrario M., Kee F., Willer C.J., Samani N.,
Schunkert H., Butterworth A.S., Howson J.M., Peloso G.M.,
Stitziel N.O., Danesh J., Kathiresan S., Rader D.J.;
"Rare variant in scavenger receptor BI raises HDL cholesterol and
increases risk of coronary heart disease.";
Science 351:1166-1171(2016).
[18]
FUNCTION, AND VARIANT SER-2.
PubMed=12519372; DOI=10.1034/j.1399-0004.2003.630108.x;
Tai E.S., Adiconis X., Ordovas J.M., Carmena-Ramon R., Real J.,
Corella D., Ascaso J., Carmena R.;
"Polymorphisms at the SRBI locus are associated with lipoprotein
levels in subjects with heterozygous familial hypercholesterolemia.";
Clin. Genet. 63:53-58(2003).
[19]
VARIANTS SER-2; ILE-135 AND SER-167.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
[20]
FUNCTION, VARIANT SER-297, AND INVOLVEMENT IN HDLCQ16.
PubMed=21226579; DOI=10.1056/NEJMoa0907687;
Vergeer M., Korporaal S.J., Franssen R., Meurs I., Out R.,
Hovingh G.K., Hoekstra M., Sierts J.A., Dallinga-Thie G.M.,
Motazacker M.M., Holleboom A.G., Van Berkel T.J., Kastelein J.J.,
Van Eck M., Kuivenhoven J.A.;
"Genetic variant of the scavenger receptor BI in humans.";
N. Engl. J. Med. 364:136-145(2011).
-!- 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). {ECO:0000269|PubMed:12016218,
ECO:0000269|PubMed:12519372, ECO:0000269|PubMed:16020694,
ECO:0000269|PubMed:21226579, ECO:0000269|PubMed:26965621}.
-!- FUNCTION: (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). Mediates uptake of M.fortuitum, E.coli and
S.aureus (PubMed:16020694). {ECO:0000269|PubMed:12356718,
ECO:0000269|PubMed:16020694, ECO:0000269|PubMed:18000990}.
-!- SUBUNIT: The C-terminal region binds to PDZK1.
{ECO:0000250|UniProtKB:P97943}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus
E1:E2 glycoproteins. {ECO:0000269|PubMed:18000990}.
-!- INTERACTION:
P27958:- (xeno); NbExp=2; IntAct=EBI-78657, EBI-6904269;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-78657, EBI-10172052;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-78657, EBI-3958099;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26965621};
Multi-pass membrane protein. Membrane, caveola
{ECO:0000250|UniProtKB:Q61009}; Multi-pass membrane protein.
Note=Predominantly localized to cholesterol and sphingomyelin-
enriched domains within the plasma membrane, called caveolae.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=3;
IsoId=Q8WTV0-1; Sequence=Displayed;
Note=May be due to a competing donor splice site. No
experimental confirmation available.;
Name=1; Synonyms=SR-BI;
IsoId=Q8WTV0-2; Sequence=VSP_008554;
Note=Contains a phosphoserine at position 493.
{ECO:0000244|PubMed:24275569};
Name=2; Synonyms=SR-BII;
IsoId=Q8WTV0-3; Sequence=VSP_008553, VSP_008554;
Note=Contains a phosphoserine at position 393.
{ECO:0000244|PubMed:24275569};
Name=4; Synonyms=SR-BIII;
IsoId=Q8WTV0-4; Sequence=VSP_011037, VSP_008554;
Note=Contains a phosphoserine at position 458.
{ECO:0000244|PubMed:24275569};
Name=5; Synonyms=SR-BI.2 {ECO:0000303|PubMed:9254074}, SR-BII
{ECO:0000303|PubMed:9614139};
IsoId=Q8WTV0-5; Sequence=VSP_054083;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12016218,
ECO:0000269|PubMed:19159218}.
-!- PTM: The six cysteines of the extracellular domain are all
involved in intramolecular disulfide bonds.
{ECO:0000250|UniProtKB:Q61009}.
-!- POLYMORPHISM: Genetic variations in SCARB1 define the high density
lipoprotein cholesterol level quantitative trait locus 6 (HDLCQ16)
[MIM:610762]. {ECO:0000269|PubMed:20686565,
ECO:0000269|PubMed:21226579, ECO:0000269|PubMed:26965621}.
-!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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EMBL; Z22555; CAA80277.1; -; mRNA.
EMBL; AF515445; AAQ08185.1; -; mRNA.
EMBL; AC073593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW98459.1; -; Genomic_DNA.
EMBL; BC022087; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC080647; AAH80647.1; -; mRNA.
EMBL; BC093732; AAH93732.1; -; mRNA.
EMBL; BC112037; AAI12038.1; -; mRNA.
CCDS; CCDS45008.1; -. [Q8WTV0-5]
CCDS; CCDS9259.1; -. [Q8WTV0-2]
PIR; S36656; A48528.
RefSeq; NP_001076428.1; NM_001082959.1. [Q8WTV0-5]
RefSeq; NP_005496.4; NM_005505.4. [Q8WTV0-2]
UniGene; Hs.731377; -.
ProteinModelPortal; Q8WTV0; -.
SMR; Q8WTV0; -.
BioGrid; 107387; 30.
IntAct; Q8WTV0; 10.
MINT; MINT-5001419; -.
STRING; 9606.ENSP00000261693; -.
BindingDB; Q8WTV0; -.
ChEMBL; CHEMBL1914272; -.
DrugBank; DB00144; Phosphatidyl serine.
SwissLipids; SLP:000001519; -.
TCDB; 9.B.39.1.3; the long chain fatty acid translocase (lcfat) family.
iPTMnet; Q8WTV0; -.
PhosphoSitePlus; Q8WTV0; -.
SwissPalm; Q8WTV0; -.
BioMuta; SCARB1; -.
DMDM; 37999904; -.
EPD; Q8WTV0; -.
MaxQB; Q8WTV0; -.
PaxDb; Q8WTV0; -.
PeptideAtlas; Q8WTV0; -.
PRIDE; Q8WTV0; -.
DNASU; 949; -.
Ensembl; ENST00000261693; ENSP00000261693; ENSG00000073060. [Q8WTV0-2]
Ensembl; ENST00000339570; ENSP00000343795; ENSG00000073060. [Q8WTV0-5]
Ensembl; ENST00000415380; ENSP00000414979; ENSG00000073060. [Q8WTV0-1]
GeneID; 949; -.
KEGG; hsa:949; -.
UCSC; uc001ugm.5; human. [Q8WTV0-1]
CTD; 949; -.
DisGeNET; 949; -.
EuPathDB; HostDB:ENSG00000073060.15; -.
GeneCards; SCARB1; -.
HGNC; HGNC:1664; SCARB1.
HPA; CAB070124; -.
HPA; HPA066285; -.
MIM; 601040; gene.
MIM; 610762; phenotype.
neXtProt; NX_Q8WTV0; -.
OpenTargets; ENSG00000073060; -.
PharmGKB; PA97; -.
eggNOG; KOG3776; Eukaryota.
eggNOG; ENOG410XS17; LUCA.
GeneTree; ENSGT00530000062927; -.
HOVERGEN; HBG106577; -.
InParanoid; Q8WTV0; -.
KO; K13885; -.
OMA; PDACRSM; -.
OrthoDB; EOG091G0CH9; -.
PhylomeDB; Q8WTV0; -.
TreeFam; TF317925; -.
Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
Reactome; R-HSA-8964011; HDL clearance.
ChiTaRS; SCARB1; human.
GeneWiki; SCARB1; -.
GenomeRNAi; 949; -.
PRO; PR:Q8WTV0; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000073060; -.
CleanEx; HS_SCARB1; -.
ExpressionAtlas; Q8WTV0; baseline and differential.
Genevisible; Q8WTV0; HS.
GO; GO:0005901; C:caveola; TAS:BHF-UCL.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0005545; F:1-phosphatidylinositol binding; TAS:BHF-UCL.
GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
GO; GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL.
GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0070506; F:high-density lipoprotein particle receptor activity; IDA:BHF-UCL.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
GO; GO:0001875; F:lipopolysaccharide receptor activity; IDA:BHF-UCL.
GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
GO; GO:0001786; F:phosphatidylserine binding; ISS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:BHF-UCL.
GO; GO:0006702; P:androgen biosynthetic process; IEA:Ensembl.
GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
GO; GO:0006707; P:cholesterol catabolic process; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; IMP:AgBase.
GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
GO; GO:0070508; P:cholesterol import; IMP:UniProtKB.
GO; GO:0032497; P:detection of lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
GO; GO:0034384; P:high-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:BHF-UCL.
GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
GO; GO:0015920; P:lipopolysaccharide transport; IDA:BHF-UCL.
GO; GO:0034383; P:low-density lipoprotein particle clearance; ISS:BHF-UCL.
GO; GO:0015914; P:phospholipid transport; ISS:BHF-UCL.
GO; GO:0010886; P:positive regulation of cholesterol storage; IDA:BHF-UCL.
GO; GO:0010595; P:positive regulation of endothelial cell migration; TAS:BHF-UCL.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0043654; P:recognition of apoptotic cell; IDA:BHF-UCL.
GO; GO:0050764; P:regulation of phagocytosis; IC:BHF-UCL.
GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; ISS:BHF-UCL.
GO; GO:0043691; P:reverse cholesterol transport; IEP:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; ISS:BHF-UCL.
GO; GO:0035461; P:vitamin transmembrane transport; IMP:AgBase.
GO; GO:0042060; P:wound healing; TAS:BHF-UCL.
InterPro; IPR005428; CD36/SCARB1/SNMP1.
InterPro; IPR002159; CD36_fam.
PANTHER; PTHR11923; PTHR11923; 1.
Pfam; PF01130; CD36; 1.
PRINTS; PR01610; CD36ANTIGEN.
PRINTS; PR01609; CD36FAMILY.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 552 Scavenger receptor class B member 1.
/FTId=PRO_0000144160.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 32 Helical. {ECO:0000255}.
TOPO_DOM 33 443 Extracellular. {ECO:0000255}.
TRANSMEM 444 464 Helical. {ECO:0000255}.
TOPO_DOM 465 552 Cytoplasmic. {ECO:0000255}.
LIPID 462 462 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q61009}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 383 383 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 251 384 {ECO:0000250}.
VAR_SEQ 1 42 MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVL
K -> MALQPSW (in isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_011037.
VAR_SEQ 43 142 Missing (in isoform 2).
{ECO:0000303|PubMed:7689561}.
/FTId=VSP_008553.
VAR_SEQ 468 552 VGAGQRAARADSHSLACWGKGASDRTLWPTAAWSPPPAAVL
RLCRSGSGHCWGLRSTLASFACRVATTLPVLEGLGPSLGGG
TGS -> EKCYLFWSSSKKGSKDKEAIQAYSESLMTSAPKG
SVLQEAKL (in isoform 1, isoform 2 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7689561,
ECO:0000303|Ref.2}.
/FTId=VSP_008554.
VAR_SEQ 468 552 VGAGQRAARADSHSLACWGKGASDRTLWPTAAWSPPPAAVL
RLCRSGSGHCWGLRSTLASFACRVATTLPVLEGLGPSLGGG
TGS -> GPEDTVSQPGLAAGPDRPPSPYTPLLPDSPSGQP
PSPTA (in isoform 5). {ECO:0000305}.
/FTId=VSP_054083.
VARIANT 2 2 G -> S (associated with higher plasma
triglyceride concentration in subjects
with hypercholesterolemia;
dbSNP:rs4238001).
{ECO:0000269|PubMed:12519372,
ECO:0000269|PubMed:12966036}.
/FTId=VAR_017098.
VARIANT 135 135 V -> I (in dbSNP:rs5891).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_017099.
VARIANT 167 167 G -> S (in dbSNP:rs199588922).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_017100.
VARIANT 229 229 S -> G (in dbSNP:rs10396213).
/FTId=VAR_019507.
VARIANT 297 297 P -> S (mutation carriers have increased
HDL cholesterol levels and a reduction in
cholesterol efflux from macrophages;
dbSNP:rs387906791).
{ECO:0000269|PubMed:21226579}.
/FTId=VAR_064909.
VARIANT 376 376 P -> L (rare variant; associated with
high HDL-cholesterol levels and increased
risk for coronary heart disease; results
in highly reduced cholesterol uptake from
HDL; markedly reduced localization at the
cell surface; dbSNP:rs74830677).
{ECO:0000269|PubMed:26965621}.
/FTId=VAR_076314.
VARIANT 511 511 C -> R (in dbSNP:rs2293440).
/FTId=VAR_017101.
CONFLICT 70 70 F -> L (in Ref. 2; AAQ08185).
{ECO:0000305}.
CONFLICT 97 97 F -> S (in Ref. 1; CAA80277).
{ECO:0000305}.
SEQUENCE 552 AA; 60878 MW; 06B0BD771FEA284F CRC64;
MGCSAKARWA AGALGVAGLL CAVLGAVMIV MVPSLIKQQV LKNVRIDPSS LSFNMWKEIP
IPFYLSVYFF DVMNPSEILK GEKPQVRERG PYVYREFRHK SNITFNNNDT VSFLEYRTFQ
FQPSKSHGSE SDYIVMPNIL VLGAAVMMEN KPMTLKLIMT LAFTTLGERA FMNRTVGEIM
WGYKDPLVNL INKYFPGMFP FKDKFGLFAE LNNSDSGLFT VFTGVQNISR IHLVDKWNGL
SKVDFWHSDQ CNMINGTSGQ MWPPFMTPES SLEFYSPEAC RSMKLMYKES GVFEGIPTYR
FVAPKTLFAN GSIYPPNEGF CPCLESGIQN VSTCRFSAPL FLSHPHFLNA DPVLAEAVTG
LHPNQEAHSL FLDIHPVTGI PMNCSVKLQL SLYMKSVAGI GQTGKIEPVV LPLLWFAESG
AMEGETLHTF YTQLVLMPKV MHYAQYVLLA LGCVLLLVPV ICQIRSQVGA GQRAARADSH
SLACWGKGAS DRTLWPTAAW SPPPAAVLRL CRSGSGHCWG LRSTLASFAC RVATTLPVLE
GLGPSLGGGT GS


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