SCRB1_HUMAN
ID SCRB1_HUMAN Reviewed; 552 AA.
AC Q8WTV0; F8W8N0; Q14016; Q52LZ5; Q6KFX4;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Scavenger receptor class B member 1;
DE Short=SRB1;
DE AltName: Full=CD36 and LIMPII analogous 1;
DE Short=CLA-1;
DE AltName: Full=CD36 antigen-like 1;
DE AltName: Full=Collagen type I receptor, thrombospondin receptor-like 1;
DE AltName: Full=SR-BI;
DE AltName: CD_antigen=CD36;
GN Name=SCARB1; Synonyms=CD36L1, CLA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Promyelocyte;
RX PubMed=7689561; DOI=10.1016/s0021-9258(17)46716-0;
RA Calvo D., Vega M.;
RT "Identification, primary structure and distribution of CLA-1, a novel
RT member of the CD36/LIMPII gene family.";
RL J. Biol. Chem. 268:18929-18935(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Hirano K., Yamashita S., Matsuzawa Y.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Liver, Prostate, and Rhabdomyosarcoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION (ISOFORM 5).
RX PubMed=9254074;
RA Webb N.R., de Villiers W.J., Connell P.M., de Beer F.C.,
RA van der Westhuyzen D.R.;
RT "Alternative forms of the scavenger receptor BI (SR-BI).";
RL J. Lipid Res. 38:1490-1495(1997).
RN [7]
RP IDENTIFICATION (ISOFORM 5).
RX PubMed=9614139; DOI=10.1074/jbc.273.24.15241;
RA Webb N.R., Connell P.M., Graf G.A., Smart E.J., de Villiers W.J.,
RA de Beer F.C., van der Westhuyzen D.R.;
RT "SR-BII, an isoform of the scavenger receptor BI containing an alternate
RT cytoplasmic tail, mediates lipid transfer between high density lipoprotein
RT and cells.";
RL J. Biol. Chem. 273:15241-15248(1998).
RN [8]
RP FUNCTION.
RX PubMed=12356718; DOI=10.1093/emboj/cdf529;
RA Scarselli E., Ansuini H., Cerino R., Roccasecca R.M., Acali S.,
RA Filocamo G., Traboni C., Nicosia A., Cortese R., Vitelli A.;
RT "The human scavenger receptor class B type I is a novel candidate receptor
RT for the hepatitis C virus.";
RL EMBO J. 21:5017-5025(2002).
RN [9]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=12016218; DOI=10.1074/jbc.m202879200;
RA Kawasaki Y., Nakagawa A., Nagaosa K., Shiratsuchi A., Nakanishi Y.;
RT "Phosphatidylserine binding of class B scavenger receptor type I, a
RT phagocytosis receptor of testicular Sertoli cells.";
RL J. Biol. Chem. 277:27559-27566(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER.
RX PubMed=12913001; DOI=10.1074/jbc.m305289200;
RA Bartosch B., Vitelli A., Granier C., Goujon C., Dubuisson J., Pascale S.,
RA Scarselli E., Cortese R., Nicosia A., Cosset F.-L.;
RT "Cell entry of hepatitis C virus requires a set of co-receptors that
RT include the CD81 tetraspanin and the SR-B1 scavenger receptor.";
RL J. Biol. Chem. 278:41624-41630(2003).
RN [11]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=16020694; DOI=10.1126/science.1116006;
RA Philips J.A., Rubin E.J., Perrimon N.;
RT "Drosophila RNAi screen reveals CD36 family member required for
RT mycobacterial infection.";
RL Science 309:1251-1253(2005).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS C VIRUS E1
RP AND E2 GLYCOPROTEINS.
RX PubMed=18000990; DOI=10.1002/hep.21994;
RA Zeisel M.B., Koutsoudakis G., Schnober E.K., Haberstroh A., Blum H.E.,
RA Cosset F.L., Wakita T., Jaeck D., Doffoel M., Royer C., Soulier E.,
RA Schvoerer E., Schuster C., Stoll-Keller F., Bartenschlager R.,
RA Pietschmann T., Barth H., Baumert T.F.;
RT "Scavenger receptor class B type I is a key host factor for hepatitis C
RT virus infection required for an entry step closely linked to CD81.";
RL Hepatology 46:1722-1731(2007).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102 AND ASN-330.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP INVOLVEMENT IN HDLCQ16.
RX PubMed=20686565; DOI=10.1038/nature09270;
RA Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C., Stylianou I.M.,
RA Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I., Willer C.J.,
RA Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M., Barbalic M.,
RA Ricketts S.L., Bis J.C., Aulchenko Y.S., Thorleifsson G., Feitosa M.F.,
RA Chambers J., Orho-Melander M., Melander O., Johnson T., Li X., Guo X.,
RA Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y., Park T., Kim K.,
RA Sim X., Twee-Hee Ong R., Croteau-Chonka D.C., Lange L.A., Smith J.D.,
RA Song K., Hua Zhao J., Yuan X., Luan J., Lamina C., Ziegler A., Zhang W.,
RA Zee R.Y., Wright A.F., Witteman J.C., Wilson J.F., Willemsen G.,
RA Wichmann H.E., Whitfield J.B., Waterworth D.M., Wareham N.J., Waeber G.,
RA Vollenweider P., Voight B.F., Vitart V., Uitterlinden A.G., Uda M.,
RA Tuomilehto J., Thompson J.R., Tanaka T., Surakka I., Stringham H.M.,
RA Spector T.D., Soranzo N., Smit J.H., Sinisalo J., Silander K.,
RA Sijbrands E.J., Scuteri A., Scott J., Schlessinger D., Sanna S.,
RA Salomaa V., Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M.,
RA Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I., Perola M.,
RA Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N., Pare G., Oostra B.A.,
RA O'Donnell C.J., Nieminen M.S., Nickerson D.A., Montgomery G.W.,
RA Meitinger T., McPherson R., McCarthy M.I., McArdle W., Masson D.,
RA Martin N.G., Marroni F., Mangino M., Magnusson P.K., Lucas G., Luben R.,
RA Loos R.J., Lokki M.L., Lettre G., Langenberg C., Launer L.J., Lakatta E.G.,
RA Laaksonen R., Kyvik K.O., Kronenberg F., Konig I.R., Khaw K.T., Kaprio J.,
RA Kaplan L.M., Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E.,
RA Igl W., Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A.,
RA Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D.,
RA Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C.,
RA Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L., Erdmann J.,
RA Elliott P., Ejebe K.G., Doring A., Dominiczak A.F., Demissie S.,
RA Deloukas P., de Geus E.J., de Faire U., Crawford G., Collins F.S.,
RA Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P., Bonnycastle L.L.,
RA Boomsma D.I., Boekholdt S.M., Bergman R.N., Barroso I., Bandinelli S.,
RA Ballantyne C.M., Assimes T.L., Quertermous T., Altshuler D., Seielstad M.,
RA Wong T.Y., Tai E.S., Feranil A.B., Kuzawa C.W., Adair L.S.,
RA Taylor H.A. Jr., Borecki I.B., Gabriel S.B., Wilson J.G., Holm H.,
RA Thorsteinsdottir U., Gudnason V., Krauss R.M., Mohlke K.L., Ordovas J.M.,
RA Munroe P.B., Kooner J.S., Tall A.R., Hegele R.A., Kastelein J.J.,
RA Schadt E.E., Rotter J.I., Boerwinkle E., Strachan D.P., Mooser V.,
RA Stefansson K., Reilly M.P., Samani N.J., Schunkert H., Cupples L.A.,
RA Sandhu M.S., Ridker P.M., Rader D.J., van Duijn C.M., Peltonen L.,
RA Abecasis G.R., Boehnke M., Kathiresan S.;
RT "Biological, clinical and population relevance of 95 loci for blood
RT lipids.";
RL Nature 466:707-713(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493 (ISOFORM 1),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=33244168; DOI=10.1038/s42255-020-00324-0;
RA Wei C., Wan L., Yan Q., Wang X., Zhang J., Yang X., Zhang Y., Fan C.,
RA Li D., Deng Y., Sun J., Gong J., Yang X., Wang Y., Wang X., Li J., Yang H.,
RA Li H., Zhang Z., Wang R., Du P., Zong Y., Yin F., Zhang W., Wang N.,
RA Peng Y., Lin H., Feng J., Qin C., Chen W., Gao Q., Zhang R., Cao Y.,
RA Zhong H.;
RT "HDL-scavenger receptor B type 1 facilitates SARS-CoV-2 entry.";
RL Nat. Metab. 2:1391-1400(2020).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN HDLCQ16, VARIANT LEU-376,
RP AND CHARACTERIZATION OF VARIANT LEU-376.
RX PubMed=26965621; DOI=10.1126/science.aad3517;
RG CHD Exome+ Consortium;
RG CARDIoGRAM Exome Consortium;
RG Global Lipids Genetics Consortium;
RA Zanoni P., Khetarpal S.A., Larach D.B., Hancock-Cerutti W.F., Millar J.S.,
RA Cuchel M., DerOhannessian S., Kontush A., Surendran P., Saleheen D.,
RA Trompet S., Jukema J.W., De Craen A., Deloukas P., Sattar N., Ford I.,
RA Packard C., Majumder A., Alam D.S., Di Angelantonio E., Abecasis G.,
RA Chowdhury R., Erdmann J., Nordestgaard B.G., Nielsen S.F.,
RA Tybjaerg-Hansen A., Schmidt R.F., Kuulasmaa K., Liu D.J., Perola M.,
RA Blankenberg S., Salomaa V., Maennistoe S., Amouyel P., Arveiler D.,
RA Ferrieres J., Mueller-Nurasyid M., Ferrario M., Kee F., Willer C.J.,
RA Samani N., Schunkert H., Butterworth A.S., Howson J.M., Peloso G.M.,
RA Stitziel N.O., Danesh J., Kathiresan S., Rader D.J.;
RT "Rare variant in scavenger receptor BI raises HDL cholesterol and increases
RT risk of coronary heart disease.";
RL Science 351:1166-1171(2016).
RN [19]
RP FUNCTION, AND VARIANT SER-2.
RX PubMed=12519372; DOI=10.1034/j.1399-0004.2003.630108.x;
RA Tai E.S., Adiconis X., Ordovas J.M., Carmena-Ramon R., Real J., Corella D.,
RA Ascaso J., Carmena R.;
RT "Polymorphisms at the SRBI locus are associated with lipoprotein levels in
RT subjects with heterozygous familial hypercholesterolemia.";
RL Clin. Genet. 63:53-58(2003).
RN [20]
RP VARIANTS SER-2; ILE-135 AND SER-167.
RX PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA Alvin G.B., Das K., Gilliam T.C.;
RT "Association of extreme blood lipid profile phenotypic variation with 11
RT reverse cholesterol transport genes and 10 non-genetic cardiovascular
RT disease risk factors.";
RL Hum. Mol. Genet. 12:2733-2743(2003).
RN [21]
RP FUNCTION, VARIANT SER-297, AND INVOLVEMENT IN HDLCQ16.
RX PubMed=21226579; DOI=10.1056/nejmoa0907687;
RA Vergeer M., Korporaal S.J., Franssen R., Meurs I., Out R., Hovingh G.K.,
RA Hoekstra M., Sierts J.A., Dallinga-Thie G.M., Motazacker M.M.,
RA Holleboom A.G., Van Berkel T.J., Kastelein J.J., Van Eck M.,
RA Kuivenhoven J.A.;
RT "Genetic variant of the scavenger receptor BI in humans.";
RL N. Engl. J. Med. 364:136-145(2011).
CC -!- FUNCTION: Receptor for different ligands such as phospholipids,
CC cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells
CC (PubMed:12016218, PubMed:12519372, PubMed:21226579). Receptor for HDL,
CC mediating selective uptake of cholesteryl ether and HDL-dependent
CC cholesterol efflux (PubMed:26965621). Also facilitates the flux of free
CC and esterified cholesterol between the cell surface and apoB-containing
CC lipoproteins and modified lipoproteins, although less efficiently than
CC HDL. May be involved in the phagocytosis of apoptotic cells, via its
CC phosphatidylserine binding activity (PubMed:12016218).
CC {ECO:0000269|PubMed:12016218, ECO:0000269|PubMed:12519372,
CC ECO:0000269|PubMed:16020694, ECO:0000269|PubMed:21226579,
CC ECO:0000269|PubMed:26965621}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
CC virus in hepatocytes and appears to facilitate its cell entry
CC (PubMed:12356718, PubMed:12913001, PubMed:18000990). Binding between
CC SCARB1 and the hepatitis C virus glycoprotein E2 is independent of the
CC genotype of the viral isolate (PubMed:12356718).
CC {ECO:0000269|PubMed:12356718, ECO:0000269|PubMed:18000990}.
CC -!- FUNCTION: (Microbial infection) Mediates uptake of M.fortuitum, E.coli
CC and S.aureus. {ECO:0000269|PubMed:16020694}.
CC -!- FUNCTION: (Microbial infection) Facilitates the entry of human
CC coronavirus SARS-CoV-2 by acting as an entry cofactor through HDL
CC binding. {ECO:0000269|PubMed:33244168}.
CC -!- SUBUNIT: The C-terminal region binds to PDZK1.
CC {ECO:0000250|UniProtKB:P97943}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus E1:E2
CC glycoproteins. {ECO:0000269|PubMed:18000990}.
CC -!- INTERACTION:
CC Q8WTV0; P05067: APP; NbExp=3; IntAct=EBI-78657, EBI-77613;
CC Q8WTV0; P60033: CD81; NbExp=4; IntAct=EBI-78657, EBI-712921;
CC Q8WTV0; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-78657, EBI-9087876;
CC Q8WTV0; P05412: JUN; NbExp=3; IntAct=EBI-78657, EBI-852823;
CC Q8WTV0; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-78657, EBI-10172052;
CC Q8WTV0; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-78657, EBI-3958099;
CC Q8WTV0; PRO_0000037570 [P27958]; Xeno; NbExp=2; IntAct=EBI-78657, EBI-6904269;
CC Q8WTV0-2; P02649: APOE; NbExp=3; IntAct=EBI-21529758, EBI-1222467;
CC Q8WTV0-3; P19174: PLCG1; NbExp=2; IntAct=EBI-20819026, EBI-79387;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26965621};
CC Multi-pass membrane protein. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q61009}; Multi-pass membrane protein.
CC Note=Predominantly localized to cholesterol and sphingomyelin-enriched
CC domains within the plasma membrane, called caveolae.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=3;
CC IsoId=Q8WTV0-1; Sequence=Displayed;
CC Name=1; Synonyms=SR-BI;
CC IsoId=Q8WTV0-2; Sequence=VSP_008554;
CC Name=2; Synonyms=SR-BII;
CC IsoId=Q8WTV0-3; Sequence=VSP_008553, VSP_008554;
CC Name=4; Synonyms=SR-BIII;
CC IsoId=Q8WTV0-4; Sequence=VSP_011037, VSP_008554;
CC Name=5; Synonyms=SR-BI.2 {ECO:0000303|PubMed:9254074}, SR-BII
CC {ECO:0000303|PubMed:9614139};
CC IsoId=Q8WTV0-5; Sequence=VSP_054083;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12016218,
CC ECO:0000269|PubMed:19159218}.
CC -!- PTM: The six cysteines of the extracellular domain are all involved in
CC intramolecular disulfide bonds. {ECO:0000250|UniProtKB:Q61009}.
CC -!- POLYMORPHISM: Genetic variations in SCARB1 define the high density
CC lipoprotein cholesterol level quantitative trait locus 6 (HDLCQ16)
CC [MIM:610762]. {ECO:0000269|PubMed:20686565,
CC ECO:0000269|PubMed:21226579, ECO:0000269|PubMed:26965621}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice
CC site.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z22555; CAA80277.1; -; mRNA.
DR EMBL; AF515445; AAQ08185.1; -; mRNA.
DR EMBL; AC073593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98459.1; -; Genomic_DNA.
DR EMBL; BC022087; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC080647; AAH80647.1; -; mRNA.
DR EMBL; BC093732; AAH93732.1; -; mRNA.
DR EMBL; BC112037; AAI12038.1; -; mRNA.
DR CCDS; CCDS45008.1; -. [Q8WTV0-5]
DR CCDS; CCDS9259.1; -. [Q8WTV0-2]
DR PIR; S36656; A48528.
DR RefSeq; NP_001076428.1; NM_001082959.1. [Q8WTV0-5]
DR RefSeq; NP_005496.4; NM_005505.4. [Q8WTV0-2]
DR AlphaFoldDB; Q8WTV0; -.
DR SMR; Q8WTV0; -.
DR BioGRID; 107387; 137.
DR IntAct; Q8WTV0; 47.
DR MINT; Q8WTV0; -.
DR STRING; 9606.ENSP00000261693; -.
DR BindingDB; Q8WTV0; -.
DR ChEMBL; CHEMBL1914272; -.
DR DrugBank; DB14003; alpha-Tocopherol acetate.
DR DrugBank; DB00144; Phosphatidyl serine.
DR DrugBank; DB11635; Tocofersolan.
DR DrugBank; DB11251; Tocopherol.
DR DrugBank; DB00163; Vitamin E.
DR SwissLipids; SLP:000001519; -.
DR TCDB; 9.B.39.1.3; the long chain fatty acid translocase (lcfat) family.
DR GlyConnect; 1722; 1 N-Linked glycan (1 site).
DR GlyGen; Q8WTV0; 12 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8WTV0; -.
DR PhosphoSitePlus; Q8WTV0; -.
DR SwissPalm; Q8WTV0; -.
DR BioMuta; SCARB1; -.
DR DMDM; 37999904; -.
DR EPD; Q8WTV0; -.
DR jPOST; Q8WTV0; -.
DR MassIVE; Q8WTV0; -.
DR MaxQB; Q8WTV0; -.
DR PaxDb; Q8WTV0; -.
DR PeptideAtlas; Q8WTV0; -.
DR PRIDE; Q8WTV0; -.
DR ProteomicsDB; 30176; -.
DR ProteomicsDB; 74602; -. [Q8WTV0-1]
DR ProteomicsDB; 74603; -. [Q8WTV0-2]
DR ProteomicsDB; 74604; -. [Q8WTV0-3]
DR ProteomicsDB; 74605; -. [Q8WTV0-4]
DR Antibodypedia; 31879; 646 antibodies from 40 providers.
DR DNASU; 949; -.
DR Ensembl; ENST00000261693.11; ENSP00000261693.6; ENSG00000073060.17. [Q8WTV0-2]
DR Ensembl; ENST00000339570.9; ENSP00000343795.4; ENSG00000073060.17. [Q8WTV0-5]
DR Ensembl; ENST00000415380.6; ENSP00000414979.2; ENSG00000073060.17. [Q8WTV0-1]
DR GeneID; 949; -.
DR KEGG; hsa:949; -.
DR MANE-Select; ENST00000261693.11; ENSP00000261693.6; NM_005505.5; NP_005496.4. [Q8WTV0-2]
DR UCSC; uc001ugm.5; human. [Q8WTV0-1]
DR CTD; 949; -.
DR DisGeNET; 949; -.
DR GeneCards; SCARB1; -.
DR HGNC; HGNC:1664; SCARB1.
DR HPA; ENSG00000073060; Tissue enriched (adrenal).
DR MalaCards; SCARB1; -.
DR MIM; 601040; gene.
DR MIM; 610762; phenotype.
DR neXtProt; NX_Q8WTV0; -.
DR OpenTargets; ENSG00000073060; -.
DR PharmGKB; PA97; -.
DR VEuPathDB; HostDB:ENSG00000073060; -.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR InParanoid; Q8WTV0; -.
DR OMA; DENYWIN; -.
DR PhylomeDB; Q8WTV0; -.
DR TreeFam; TF317925; -.
DR PathwayCommons; Q8WTV0; -.
DR Reactome; R-HSA-3000471; Scavenging by Class B Receptors. [Q8WTV0-2]
DR Reactome; R-HSA-8964011; HDL clearance. [Q8WTV0-2]
DR SignaLink; Q8WTV0; -.
DR SIGNOR; Q8WTV0; -.
DR BioGRID-ORCS; 949; 11 hits in 1087 CRISPR screens.
DR ChiTaRS; SCARB1; human.
DR GeneWiki; SCARB1; -.
DR GenomeRNAi; 949; -.
DR Pharos; Q8WTV0; Tchem.
DR PRO; PR:Q8WTV0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8WTV0; protein.
DR Bgee; ENSG00000073060; Expressed in right adrenal gland cortex and 161 other tissues.
DR ExpressionAtlas; Q8WTV0; baseline and differential.
DR Genevisible; Q8WTV0; HS.
DR GO; GO:0005901; C:caveola; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; TAS:BHF-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL.
DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0070506; F:high-density lipoprotein particle receptor activity; IDA:BHF-UCL.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IDA:BHF-UCL.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:BHF-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0044406; P:adhesion of symbiont to host; IMP:BHF-UCL.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0046867; P:carotenoid transport; IEA:Ensembl.
DR GO; GO:0006707; P:cholesterol catabolic process; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IMP:AgBase.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0070508; P:cholesterol import; IMP:UniProtKB.
DR GO; GO:0032497; P:detection of lipopolysaccharide; IDA:BHF-UCL.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IDA:BHF-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:BHF-UCL.
DR GO; GO:0098856; P:intestinal lipid absorption; IEA:Ensembl.
DR GO; GO:0015920; P:lipopolysaccharide transport; IDA:BHF-UCL.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISS:BHF-UCL.
DR GO; GO:0015914; P:phospholipid transport; ISS:BHF-UCL.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; IBA:GO_Central.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IDA:BHF-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; TAS:BHF-UCL.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:BHF-UCL.
DR GO; GO:0050764; P:regulation of phagocytosis; IC:BHF-UCL.
DR GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; ISS:BHF-UCL.
DR GO; GO:0043691; P:reverse cholesterol transport; IEP:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; ISS:BHF-UCL.
DR GO; GO:0035461; P:vitamin transmembrane transport; IMP:AgBase.
DR GO; GO:0042060; P:wound healing; TAS:BHF-UCL.
DR InterPro; IPR005428; CD36/SCARB1/SNMP1.
DR InterPro; IPR002159; CD36_fam.
DR PANTHER; PTHR11923; PTHR11923; 1.
DR Pfam; PF01130; CD36; 1.
DR PRINTS; PR01610; CD36ANTIGEN.
DR PRINTS; PR01609; CD36FAMILY.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..552
FT /note="Scavenger receptor class B member 1"
FT /id="PRO_0000144160"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 462
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q61009"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 251..384
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..42
FT /note="MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVLK -> MALQPS
FT W (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011037"
FT VAR_SEQ 43..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7689561"
FT /id="VSP_008553"
FT VAR_SEQ 468..552
FT /note="VGAGQRAARADSHSLACWGKGASDRTLWPTAAWSPPPAAVLRLCRSGSGHCW
FT GLRSTLASFACRVATTLPVLEGLGPSLGGGTGS -> EKCYLFWSSSKKGSKDKEAIQA
FT YSESLMTSAPKGSVLQEAKL (in isoform 1, isoform 2 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7689561, ECO:0000303|Ref.2"
FT /id="VSP_008554"
FT VAR_SEQ 468..552
FT /note="VGAGQRAARADSHSLACWGKGASDRTLWPTAAWSPPPAAVLRLCRSGSGHCW
FT GLRSTLASFACRVATTLPVLEGLGPSLGGGTGS -> GPEDTVSQPGLAAGPDRPPSPY
FT TPLLPDSPSGQPPSPTA (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_054083"
FT VARIANT 2
FT /note="G -> S (associated with higher plasma triglyceride
FT concentration in subjects with hypercholesterolemia;
FT dbSNP:rs4238001)"
FT /evidence="ECO:0000269|PubMed:12519372,
FT ECO:0000269|PubMed:12966036"
FT /id="VAR_017098"
FT VARIANT 135
FT /note="V -> I (in dbSNP:rs5891)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_017099"
FT VARIANT 167
FT /note="G -> S (in dbSNP:rs199588922)"
FT /evidence="ECO:0000269|PubMed:12966036"
FT /id="VAR_017100"
FT VARIANT 229
FT /note="S -> G (in dbSNP:rs10396213)"
FT /id="VAR_019507"
FT VARIANT 297
FT /note="P -> S (mutation carriers have increased HDL
FT cholesterol levels and a reduction in cholesterol efflux
FT from macrophages; dbSNP:rs387906791)"
FT /evidence="ECO:0000269|PubMed:21226579"
FT /id="VAR_064909"
FT VARIANT 376
FT /note="P -> L (rare variant; associated with high HDL-
FT cholesterol levels and increased risk for coronary heart
FT disease; results in highly reduced cholesterol uptake from
FT HDL; markedly reduced localization at the cell surface;
FT dbSNP:rs74830677)"
FT /evidence="ECO:0000269|PubMed:26965621"
FT /id="VAR_076314"
FT VARIANT 511
FT /note="C -> R (in dbSNP:rs2293440)"
FT /id="VAR_017101"
FT CONFLICT 70
FT /note="F -> L (in Ref. 2; AAQ08185)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="F -> S (in Ref. 1; CAA80277)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8WTV0-2:493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q8WTV0-3:393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q8WTV0-4:458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ 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
