SCRB1_RAT
ID SCRB1_RAT Reviewed; 509 AA.
AC P97943;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Scavenger receptor class B member 1;
DE Short=SRB1;
DE AltName: Full=SR-BI;
GN Name=Scarb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Johnson S.C.M., Svensson P.A., Carlsson B.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Ovary;
RX PubMed=9177301; DOI=10.1006/bbrc.1997.6646;
RA Mizutani T., Sonoda Y., Minegishi T., Wakabayashi K., Miyamoto K.;
RT "Cloning, characterization, and cellular distribution of rat scavenger
RT receptor class B type I (SRBI) in the ovary.";
RL Biochem. Biophys. Res. Commun. 234:499-505(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GLYCOSYLATION.
RC STRAIN=Donryu; TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP FUNCTION.
RX PubMed=9291126; DOI=10.1042/bj3260515;
RA Fluiter K., van Berkel T.J.C.;
RT "Scavenger receptor B1 (SR-B1) substrates inhibit the selective uptake of
RT high-density-lipoprotein cholesteryl esters by rat parenchymal liver
RT cells.";
RL Biochem. J. 326:515-519(1997).
RN [6]
RP INTERACTION WITH PDZK1.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=10829064; DOI=10.1073/pnas.100114397;
RA Ikemoto M., Arai H., Feng D., Tanaka K., Aoki J., Dohmae N., Takio K.,
RA Adachi H., Tsujimoto M., Inoue K.;
RT "Identification of a PDZ-domain-containing protein that interacts with the
RT scavenger receptor class B type I.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6538-6543(2000).
CC -!- FUNCTION: Receptor for different ligands such as phospholipids,
CC cholesterol ester, lipoproteins, phosphatidylserine and apoptotic
CC cells. Receptor for HDL, mediating selective uptake of cholesteryl
CC ether and HDL-dependent cholesterol efflux. Also facilitates the flux
CC of free and esterified cholesterol between the cell surface and apoB-
CC containing lipoproteins and modified lipoproteins, although less
CC efficiently than HDL. May be involved in the phagocytosis of apoptotic
CC cells, via its phosphatidylserine binding activity.
CC {ECO:0000250|UniProtKB:Q8WTV0}.
CC -!- SUBUNIT: The C-terminal region binds to PDZK1.
CC {ECO:0000269|PubMed:10829064}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WTV0};
CC Multi-pass membrane protein {ECO:0000250}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q61009}; Multi-pass membrane protein
CC {ECO:0000250}. Note=Predominantly localized to cholesterol and
CC sphingomyelin-enriched domains within the plasma membrane, called
CC caveolae. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12016218}.
CC -!- PTM: The six cysteines of the extracellular domain are all involved in
CC intramolecular disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR EMBL; U76205; AAB19203.1; -; mRNA.
DR EMBL; D89655; BAA14004.1; -; mRNA.
DR EMBL; AB002151; BAA74541.1; -; mRNA.
DR EMBL; BC076504; AAH76504.1; -; mRNA.
DR PIR; JC5533; JC5533.
DR RefSeq; NP_113729.1; NM_031541.1.
DR AlphaFoldDB; P97943; -.
DR SMR; P97943; -.
DR STRING; 10116.ENSRNOP00000060874; -.
DR GlyGen; P97943; 10 sites.
DR iPTMnet; P97943; -.
DR PhosphoSitePlus; P97943; -.
DR PaxDb; P97943; -.
DR GeneID; 25073; -.
DR KEGG; rno:25073; -.
DR UCSC; RGD:2302; rat.
DR CTD; 949; -.
DR RGD; 2302; Scarb1.
DR VEuPathDB; HostDB:ENSRNOG00000000981; -.
DR eggNOG; KOG3776; Eukaryota.
DR HOGENOM; CLU_019853_4_0_1; -.
DR InParanoid; P97943; -.
DR OMA; DENYWIN; -.
DR OrthoDB; 1106566at2759; -.
DR PhylomeDB; P97943; -.
DR TreeFam; TF317925; -.
DR Reactome; R-RNO-3000471; Scavenging by Class B Receptors.
DR Reactome; R-RNO-8964011; HDL clearance.
DR PRO; PR:P97943; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000981; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; P97943; baseline and differential.
DR Genevisible; P97943; RN.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0031528; C:microvillus membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0034186; F:apolipoprotein A-I binding; ISO:RGD.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:RGD.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; ISO:RGD.
DR GO; GO:0070506; F:high-density lipoprotein particle receptor activity; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; TAS:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; ISO:RGD.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:BHF-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:BHF-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR GO; GO:0044406; P:adhesion of symbiont to host; ISO:RGD.
DR GO; GO:0006702; P:androgen biosynthetic process; IDA:RGD.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0006707; P:cholesterol catabolic process; ISO:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0070508; P:cholesterol import; ISO:RGD.
DR GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR GO; GO:0032497; P:detection of lipopolysaccharide; ISO:RGD.
DR GO; GO:0001935; P:endothelial cell proliferation; ISO:RGD.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; ISS:BHF-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0050892; P:intestinal absorption; ISO:RGD.
DR GO; GO:0006869; P:lipid transport; IMP:RGD.
DR GO; GO:0015920; P:lipopolysaccharide transport; ISO:RGD.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0006910; P:phagocytosis, recognition; IMP:RGD.
DR GO; GO:0015914; P:phospholipid transport; ISO:RGD.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; IBA:GO_Central.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISS:BHF-UCL.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISO:RGD.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:BHF-UCL.
DR GO; GO:0050764; P:regulation of phagocytosis; IDA:RGD.
DR GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; ISO:RGD.
DR GO; GO:0043691; P:reverse cholesterol transport; ISS:BHF-UCL.
DR GO; GO:0006694; P:steroid biosynthetic process; TAS:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:RGD.
DR GO; GO:0035461; P:vitamin transmembrane transport; ISO:RGD.
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 Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Scavenger receptor class B member 1"
FT /id="PRO_0000144163"
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..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
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:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 251..384
FT /evidence="ECO:0000250"
SQ SEQUENCE 509 AA; 56957 MW; 792A0BBE8D11A105 CRC64;
MGVSSRARWV ALGLGVLGLL CAALGVIMIL MVPSLIKQQV LKNVRIDPSS LSFGMWKEIP
VPFYLSVYFF EVVNPSEVLN GQKPVVRERG PYVYREFRQK VNITFNDNDT VSYIENRSLR
FQPDRSQGSE SDYIVLPNIL VLGGAVMMED KPTSLKLLMT LGLVTMGQRA FMNRTVGEIL
WGYEDPFVNF LSKYFPDMFP IKGKFGLFVG MNDSSSGVFT VFTGVQNFSK IHLVDKWNGL
SEVNYWHSEQ CNMINGTAGQ MWAPFMTPES SLEFFSPEAC RSMKLTYQES RVFEGIPTYR
FTAPDTLFAN GSVYPPNEGF CPCRESGIQN VSTCRFGAPL FLSQPHFYNA DPVLSEAVLG
LNPDPKEHSL FLDIHPVTGI PMNCSVKMQL SLYIKSVKGV GQTGKIEPVV LPLLWFEQSG
MMGGKTLNTF YTQLVLMPQV LHYAQYVLLG LGGLLLLVPI IYQLRSQEKC FLFWSGSKKG
SQDKEAMQAY SESLMSPAAK GTVLQEAKL
