TSPO_RAT
ID TSPO_RAT Reviewed; 169 AA.
AC P16257;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Translocator protein;
DE AltName: Full=Mitochondrial benzodiazepine receptor;
DE AltName: Full=PKBS;
DE AltName: Full=Peripheral-type benzodiazepine receptor;
DE Short=PBR;
GN Name=Tspo; Synonyms=Bzrp, Mbr;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Adrenal gland;
RX PubMed=2555358; DOI=10.1016/s0021-9258(19)47078-6;
RA Sprengel R., Werner P., Seeburg P.H., Mukhin A.G., Santi M.R.,
RA Grayson D.R., Guidotti A., Krueger K.E.;
RT "Molecular cloning and expression of cDNA encoding a peripheral-type
RT benzodiazepine receptor.";
RL J. Biol. Chem. 264:20415-20421(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=1332914; DOI=10.1016/0378-1119(92)90147-h;
RA Casalotti S.O., Pelaia G., Yakovlev A.G., Csikos T., Grayson D.R.,
RA Krueger K.E.;
RT "Structure of the rat gene encoding the mitochondrial benzodiazepine
RT receptor.";
RL Gene 121:377-382(1992).
RN [3]
RP FUNCTION IN PROTOPORPHYRIN BINDING.
RX PubMed=20336621; DOI=10.1002/syn.20779;
RA Ozaki H., Zoghbi S.S., Hong J., Verma A., Pike V.W., Innis R.B., Fujita M.;
RT "In vivo binding of protoporphyrin IX to rat translocator protein imaged
RT with positron emission tomography.";
RL Synapse 64:649-653(2010).
CC -!- FUNCTION: Promotes the transport of cholesterol across mitochondrial
CC membranes and may play a role in lipid metabolism, but its precise
CC physiological role is controversial. It is apparently not required for
CC steroid hormone biosynthesis (By similarity). Can bind protoporphyrin
CC IX and may play a role in the transport of porphyrins and heme. Was
CC initially identified as peripheral-type benzodiazepine receptor; can
CC also bind isoquinoline carboxamides (PubMed:2555358). {ECO:0000250,
CC ECO:0000269|PubMed:20336621, ECO:0000269|PubMed:2555358}.
CC -!- SUBUNIT: Interacts with TSPOAP1. Interacts with MOST-1. May interact
CC with STAR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:2555358};
CC Multi-pass membrane protein {ECO:0000269|PubMed:2555358}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adrenal gland.
CC {ECO:0000269|PubMed:2555358}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; J05122; AAA41862.1; -; mRNA.
DR EMBL; M84221; AAA41978.1; -; Genomic_DNA.
DR PIR; JC1393; JC1393.
DR RefSeq; NP_036647.1; NM_012515.2.
DR AlphaFoldDB; P16257; -.
DR SMR; P16257; -.
DR STRING; 10116.ENSRNOP00000014089; -.
DR BindingDB; P16257; -.
DR ChEMBL; CHEMBL4552; -.
DR DrugCentral; P16257; -.
DR GuidetoPHARMACOLOGY; 2879; -.
DR PaxDb; P16257; -.
DR Ensembl; ENSRNOT00000014089; ENSRNOP00000014089; ENSRNOG00000010549.
DR GeneID; 24230; -.
DR KEGG; rno:24230; -.
DR UCSC; RGD:2228; rat.
DR CTD; 706; -.
DR RGD; 2228; Tspo.
DR eggNOG; KOG3797; Eukaryota.
DR GeneTree; ENSGT00390000012980; -.
DR HOGENOM; CLU_091805_2_1_1; -.
DR InParanoid; P16257; -.
DR OMA; GLNLIWM; -.
DR OrthoDB; 1592225at2759; -.
DR PhylomeDB; P16257; -.
DR TreeFam; TF342852; -.
DR Reactome; R-RNO-196108; Pregnenolone biosynthesis.
DR PRO; PR:P16257; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000010549; Expressed in esophagus and 20 other tissues.
DR Genevisible; P16257; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005497; F:androgen binding; IDA:RGD.
DR GO; GO:0008503; F:benzodiazepine receptor activity; IDA:RGD.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0030325; P:adrenal gland development; IEP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0048266; P:behavioral response to pain; IMP:RGD.
DR GO; GO:0071476; P:cellular hypotonic response; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071294; P:cellular response to zinc ion; IEP:RGD.
DR GO; GO:0006821; P:chloride transport; IDA:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:RGD.
DR GO; GO:0060242; P:contact inhibition; IDA:RGD.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0008347; P:glial cell migration; IDA:RGD.
DR GO; GO:0006811; P:ion transport; IDA:RGD.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0072656; P:maintenance of protein location in mitochondrion; ISO:RGD.
DR GO; GO:1903579; P:negative regulation of ATP metabolic process; ISO:RGD.
DR GO; GO:1903147; P:negative regulation of autophagy of mitochondrion; ISO:RGD.
DR GO; GO:2000853; P:negative regulation of corticosterone secretion; IMP:RGD.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IDA:RGD.
DR GO; GO:0010823; P:negative regulation of mitochondrion organization; ISO:RGD.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:RGD.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IDA:RGD.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IDA:RGD.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IMP:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:RGD.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IMP:RGD.
DR GO; GO:1905144; P:response to acetylcholine; IMP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0010042; P:response to manganese ion; IEP:RGD.
DR GO; GO:0048265; P:response to pain; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0010266; P:response to vitamin B1; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; IMP:RGD.
DR CDD; cd15904; TSPO_MBR; 1.
DR Gene3D; 1.20.1260.100; -; 1.
DR InterPro; IPR030164; TSPO.
DR InterPro; IPR038330; TspO/MBR-related_sf.
DR InterPro; IPR004307; TspO_MBR.
DR PANTHER; PTHR10057; PTHR10057; 1.
DR PANTHER; PTHR10057:SF5; PTHR10057:SF5; 1.
DR Pfam; PF03073; TspO_MBR; 1.
DR PIRSF; PIRSF005859; PBR; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipid transport; Membrane; Mitochondrion;
KW Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..169
FT /note="Translocator protein"
FT /id="PRO_0000190999"
FT TOPO_DOM 1..5
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 6..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 27..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 47..67
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 68..79
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 80..100
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 101..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 106..126
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 127..134
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..155
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 156..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 169 AA; 18940 MW; 0D750157DB5585AF CRC64;
MSQSWVPAVG LTLVPSLGGF MGAYFVRGEG LRWYASLQKP SWHPPRWTLA PIWGTLYSAM
GYGSYIIWKE LGGFTEEAMV PLGLYTGQLA LNWAWPPIFF GARQMGWALV DLMLVSGVAT
ATTLAWHRVS PPAARLLYPY LAWLAFATML NYYVWRDNSG RRGGSRLTE
