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SCRB1_PIG
ID   SCRB1_PIG               Reviewed;         509 AA.
AC   Q8SQC1;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Scavenger receptor class B member 1;
DE            Short=SRB1;
DE   AltName: Full=High density lipoprotein receptor SR-BI;
DE   AltName: Full=SR-BI;
GN   Name=SCARB1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kim J.G., Vallet J.L., Christenson R.K.;
RT   "Characterization of porcine high density lipoprotein (HDL) receptor SR-
RT   BI.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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; AF467889; AAL75567.1; -; mRNA.
DR   RefSeq; NP_999132.1; NM_213967.1.
DR   AlphaFoldDB; Q8SQC1; -.
DR   SMR; Q8SQC1; -.
DR   STRING; 9823.ENSSSCP00000010421; -.
DR   PaxDb; Q8SQC1; -.
DR   PeptideAtlas; Q8SQC1; -.
DR   PRIDE; Q8SQC1; -.
DR   Ensembl; ENSSSCT00000010699; ENSSSCP00000010421; ENSSSCG00000009759.
DR   Ensembl; ENSSSCT00015105967; ENSSSCP00015044464; ENSSSCG00015078283.
DR   Ensembl; ENSSSCT00025017217; ENSSSCP00025006884; ENSSSCG00025012867.
DR   Ensembl; ENSSSCT00030003725; ENSSSCP00030001466; ENSSSCG00030002857.
DR   Ensembl; ENSSSCT00050075288; ENSSSCP00050032476; ENSSSCG00050055165.
DR   Ensembl; ENSSSCT00055002768; ENSSSCP00055002087; ENSSSCG00055001468.
DR   Ensembl; ENSSSCT00070036281; ENSSSCP00070030335; ENSSSCG00070018349.
DR   GeneID; 397018; -.
DR   KEGG; ssc:397018; -.
DR   CTD; 949; -.
DR   VGNC; VGNC:92613; SCARB1.
DR   eggNOG; KOG3776; Eukaryota.
DR   GeneTree; ENSGT00940000153372; -.
DR   InParanoid; Q8SQC1; -.
DR   OMA; DENYWIN; -.
DR   OrthoDB; 1106566at2759; -.
DR   ChiTaRS; SCARB1; pig.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Proteomes; UP000314985; Chromosome 14.
DR   Bgee; ENSSSCG00000009759; Expressed in ovary and 45 other tissues.
DR   ExpressionAtlas; Q8SQC1; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:AgBase.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:AgBase.
DR   GO; GO:0005901; C:caveola; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR   GO; GO:0070506; F:high-density lipoprotein particle receptor activity; IMP:AgBase.
DR   GO; GO:0008289; F:lipid binding; IBA:GO_Central.
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:0033344; P:cholesterol efflux; IBA:GO_Central.
DR   GO; GO:0070508; P:cholesterol import; IBA:GO_Central.
DR   GO; GO:0034381; P:plasma lipoprotein particle clearance; IBA:GO_Central.
DR   GO; GO:0043654; P:recognition of apoptotic cell; IBA:GO_Central.
DR   GO; GO:0045056; P:transcytosis; IMP:AgBase.
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   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Scavenger receptor class B member 1"
FT                   /id="PRO_0000144162"
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..439
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        461..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        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;  57514 MW;  F7421796C391C4C1 CRC64;
     MGSRSRARQV AAALGFVGLL LAALGAVMIV MVPSIIKQQV LKNVRIDPSS LSFNMWKEIP
     VPFYLSVYFF DVINPNEILQ GQKPQVRERG PYVYREFRHK SNITFNDNDT VSFLEYRSYQ
     FQPHKSRGLE SDYIVIPNIL VLSASVMMED RPMSLKLIMT FAFSALGERA FVNRTVGEIM
     WGYEDPLIHL INKYFPNMFP FKGKFGLFAE LNNSDSGLFT VFTGVKDFSR IHLVDKWNGL
     SKVNFWHSDQ CNMINGTSGQ MWAPFMTPES SLEFYSPEAC RSMKLIYKEQ GVFEGIPTFR
     FVAPNTLFAN GSVYPPNEGF CPCMESGIQN VSTCRFNAPL FLSHPHFYNA DPVLAEAVSG
     LHPNTEEHSL FLDIHPVTGI PMNCSVKLQL SLYIKSVKGI GQTGKIEPVV LPLLWFAESG
     AMEGETLQTF YTQLVLMPKV LHYAQYVLLA LGCVLLFIPI VYQIRSQEKC YLFWSSSKKG
     SKDKEAIQAY SESLMTPAPK GTVLQEARL
 
 
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