SCRB1_BOVIN
ID SCRB1_BOVIN Reviewed; 509 AA.
AC O18824;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Scavenger receptor class B member 1;
DE Short=SRB1;
DE AltName: Full=SR-BI;
GN Name=SCARB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus luteum;
RX PubMed=9406850; DOI=10.1016/s0303-7207(97)00173-1;
RA Rajapaksha W.R.A.K.J.S., McBride M., Robertson L., O'Shaughnessy P.J.;
RT "Sequence of the bovine HDL-receptor (SR-BI) cDNA and changes in receptor
RT mRNA expression during granulosa cell luteinization in vivo and in vitro.";
RL Mol. Cell. Endocrinol. 134:59-67(1997).
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}.
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; AF019384; AAB70920.1; -; mRNA.
DR RefSeq; NP_777022.1; NM_174597.2.
DR AlphaFoldDB; O18824; -.
DR SMR; O18824; -.
DR STRING; 9913.ENSBTAP00000018959; -.
DR PaxDb; O18824; -.
DR PRIDE; O18824; -.
DR Ensembl; ENSBTAT00000018959; ENSBTAP00000018959; ENSBTAG00000014269.
DR GeneID; 282346; -.
DR KEGG; bta:282346; -.
DR CTD; 949; -.
DR VEuPathDB; HostDB:ENSBTAG00000014269; -.
DR VGNC; VGNC:34324; SCARB1.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR HOGENOM; CLU_019853_4_0_1; -.
DR InParanoid; O18824; -.
DR OMA; DENYWIN; -.
DR OrthoDB; 1106566at2759; -.
DR TreeFam; TF317925; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000014269; Expressed in diaphragm and 106 other tissues.
DR ExpressionAtlas; O18824; baseline and differential.
DR GO; GO:0005901; C:caveola; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0008289; F:lipid binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0070508; P:cholesterol import; IBA:GO_Central.
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:0034381; P:plasma lipoprotein particle clearance; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR002159; CD36_fam.
DR PANTHER; PTHR11923; PTHR11923; 1.
DR Pfam; PF01130; CD36; 1.
DR PRINTS; PR01609; CD36FAMILY.
PE 2: Evidence at transcript 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_0000144158"
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; 57610 MW; B3B7FD368C22C12F CRC64;
MGNLSRARRV TAALGFIGLL FAVLGIIMIV MVPSIIKQQV LKNVRIDPNS LSFNMWKEIP
VPFYLSVYFF NIVNPEGIIQ GQKPQVQEHG PYVYREFRHK SNITFNNNDT VSFLEYRSYQ
FQPDKSRGQE SDYIVMPNIL VLSASMMMEN RPGLLKLMMT LAFSTLGQRA FMNRTVGEIM
WGYDDPLIHL INQYFPNSLP FKGKFGLFAE LNNSDSGLFT VFTGVKNFSR IHLVDKWNGV
SKVNYWHSDQ CNMINGTSGQ MWAPFMTPES SLEFYSPEAC RSMKLVYKEQ GVFGGIPTFR
FVAPSTLFAN GSVYPPNEGF CPCRESGIQN VSTCRFNAPL FLSHPHFYNA DPVLAEAVSG
LHPNPKEHSL FLDIHPVTGI PMNCSVKLQL SLFVKSVKGI GQTGNIQPVV LPLMWFEESG
AMEGETLETF YIQLVLMPKV LHYAQYVLLA LGCVLLLIPI IYQIRSQEKC YLFWISFKKG
SKDKEAVQAY SEFLMTSAPK GTVLQEARL
