SCRB1_CRIGR
ID SCRB1_CRIGR Reviewed; 509 AA.
AC Q60417;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Scavenger receptor class B member 1;
DE Short=SRB1;
DE AltName: Full=HaSR-BI;
DE AltName: Full=SR-BI;
GN Name=SCARB1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian carcinoma;
RX PubMed=7520436; DOI=10.1016/s0021-9258(17)31921-x;
RA Acton S.L., Scherer P.E., Lodish H.F., Krieger M.;
RT "Expression cloning of SR-BI, a CD36-related class B scavenger receptor.";
RL J. Biol. Chem. 269:21003-21009(1994).
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 -!- 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:0000250}.
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; U11453; AAA61572.1; -; mRNA.
DR PIR; A53920; A53920.
DR RefSeq; NP_001231777.1; NM_001244848.2.
DR RefSeq; XP_016833814.1; XM_016978325.1.
DR AlphaFoldDB; Q60417; -.
DR SMR; Q60417; -.
DR STRING; 10029.NP_001231777.1; -.
DR Ensembl; ENSCGRT00001020889; ENSCGRP00001016645; ENSCGRG00001016917.
DR GeneID; 100736552; -.
DR KEGG; cge:100736552; -.
DR CTD; 949; -.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR OrthoDB; 1106566at2759; -.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0034186; F:apolipoprotein A-I binding; IEA:Ensembl.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0070506; F:high-density lipoprotein particle receptor activity; IEA:Ensembl.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IEA:Ensembl.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0044406; P:adhesion of symbiont to host; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
DR GO; GO:0032497; P:detection of lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0098856; P:intestinal lipid absorption; IEA:Ensembl.
DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:Ensembl.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0015914; P:phospholipid transport; IEA:Ensembl.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:0043654; P:recognition of apoptotic cell; IEA:Ensembl.
DR GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR GO; GO:0035461; P:vitamin transmembrane transport; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Scavenger receptor class B member 1"
FT /id="PRO_0000144159"
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 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; 56735 MW; 1A7C0F5F6CB61A17 CRC64;
MGGSARARWV AVGLGVVGLL CAVLGVVMIL VMPSLIKQQV LKNVRIDPSS LSFAMWKEIP
VPFYLSVYFF EVVNPSEILK GEKPVVRERG PYVYREFRHK ANITFNDNDT VSFVEHRSLH
FQPDRSHGSE SDYIILPNIL VLGGAVMMES KSAGLKLMMT LGLATLGQRA FMNRTVGEIL
WGYEDPFVNF INKYLPDMFP IKGKFGLFVE MNNSDSGLFT VFTGVQNFSK IHLVDRWNGL
SKVNYWHSEQ CNMINGTSGQ MWAPFMTPQS SLEFFSPEAC RSMKLTYHDS GVFEGIPTYR
FTAPKTLFAN GSVYPPNEGF CPCLESGIQN VSTCRFGAPL FLSHPHFYNA DPVLSEAVLG
LNPDPREHSL FLDIHPVTGI PMNCSVKLQI SLYIKAVKGI GQTGKIEPVV LPLLWFEQSG
AMGGEPLNTF YTQLVLMPQV LQYVQYVLLG LGGLLLLVPV IYQLRSQEKC FLFWSGSKKG
SQDKEAIQAY SESLMSPAAK GTVLQEAKL
