TSPO2_HUMAN
ID TSPO2_HUMAN Reviewed; 170 AA.
AC Q5TGU0; B2RPR2; B7ZMN8; Q3SX82;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translocator protein 2;
DE AltName: Full=Peripheral-type benzodiazepine receptor-like protein 1;
GN Name=TSPO2; Synonyms=BZRPL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19729679; DOI=10.1074/jbc.m109.029876;
RA Fan J., Rone M.B., Papadopoulos V.;
RT "Translocator protein 2 is involved in cholesterol redistribution during
RT erythropoiesis.";
RL J. Biol. Chem. 284:30484-30497(2009).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27641616; DOI=10.1038/srep33516;
RA Marginedas-Freixa I., Hattab C., Bouyer G., Halle F., Chene A.,
RA Lefevre S.D., Cambot M., Cueff A., Schmitt M., Gamain B., Lacapere J.J.,
RA Egee S., Bihel F., Le Van Kim C., Ostuni M.A.;
RT "TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to
RT the inhibition of P. falciparum growth in human blood.";
RL Sci. Rep. 6:33516-33516(2016).
RN [5]
RP FUNCTION.
RX PubMed=30061676; DOI=10.1038/s41598-018-29885-7;
RA Marginedas-Freixa I., Alvarez C.L., Moras M., Leal Denis M.F., Hattab C.,
RA Halle F., Bihel F., Mouro-Chanteloup I., Lefevre S.D., Le Van Kim C.,
RA Schwarzbaum P.J., Ostuni M.A.;
RT "Human erythrocytes release ATP by a novel pathway involving VDAC
RT oligomerization independent of pannexin-1.";
RL Sci. Rep. 8:11384-11384(2018).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31989647; DOI=10.1111/boc.201900098;
RA Manceau H., Lefevre S.D., Mirmiran A., Hattab C., Sugier H.R., Schmitt C.,
RA Peoc'h K., Puy H., Ostuni M.A., Gouya L., Lacapere J.J.;
RT "TSPO2 translocates 5-aminolevulinic acid into human erythroleukemia
RT cells.";
RL Biol. Cell 112:113-126(2020).
CC -!- FUNCTION: Cholesterol-binding protein involved in the redistribution of
CC cholesterol from lipid droplets to the endoplasmic reticulum
CC (PubMed:19729679). Required to meet cholesterol demands during
CC erythropoietic differentiation (PubMed:19729679). May play a role in
CC transport processes at the plasma membrane of erythrocytes, including
CC regulating VDAC-mediated ATP export, and import of the heme precursors
CC protoporphyrin IX and 5-aminolevulinic acid (PubMed:27641616,
CC PubMed:30061676, PubMed:31989647). {ECO:0000269|PubMed:19729679,
CC ECO:0000269|PubMed:27641616, ECO:0000269|PubMed:30061676,
CC ECO:0000269|PubMed:31989647}.
CC -!- SUBUNIT: Homotetramer (PubMed:27641616). May also form homodimer
CC (PubMed:27641616). {ECO:0000269|PubMed:27641616}.
CC -!- INTERACTION:
CC Q5TGU0; Q8IVF2-3: AHNAK2; NbExp=3; IntAct=EBI-12195249, EBI-12078468;
CC Q5TGU0; Q13520: AQP6; NbExp=3; IntAct=EBI-12195249, EBI-13059134;
CC Q5TGU0; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12195249, EBI-11343438;
CC Q5TGU0; P07307-3: ASGR2; NbExp=3; IntAct=EBI-12195249, EBI-12808270;
CC Q5TGU0; Q8WWH4: ASZ1; NbExp=3; IntAct=EBI-12195249, EBI-12239061;
CC Q5TGU0; Q13323: BIK; NbExp=3; IntAct=EBI-12195249, EBI-700794;
CC Q5TGU0; P19397: CD53; NbExp=3; IntAct=EBI-12195249, EBI-6657396;
CC Q5TGU0; Q07108: CD69; NbExp=3; IntAct=EBI-12195249, EBI-2836595;
CC Q5TGU0; P11912: CD79A; NbExp=3; IntAct=EBI-12195249, EBI-7797864;
CC Q5TGU0; Q9HA82: CERS4; NbExp=3; IntAct=EBI-12195249, EBI-2622997;
CC Q5TGU0; O14493: CLDN4; NbExp=3; IntAct=EBI-12195249, EBI-9316372;
CC Q5TGU0; P34972: CNR2; NbExp=3; IntAct=EBI-12195249, EBI-2835940;
CC Q5TGU0; P29400-2: COL4A5; NbExp=3; IntAct=EBI-12195249, EBI-12211159;
CC Q5TGU0; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-12195249, EBI-18013275;
CC Q5TGU0; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-12195249, EBI-6942903;
CC Q5TGU0; Q9UBT3: DKK4; NbExp=3; IntAct=EBI-12195249, EBI-18030204;
CC Q5TGU0; Q15125: EBP; NbExp=3; IntAct=EBI-12195249, EBI-3915253;
CC Q5TGU0; P52803: EFNA5; NbExp=3; IntAct=EBI-12195249, EBI-1753674;
CC Q5TGU0; P54849: EMP1; NbExp=3; IntAct=EBI-12195249, EBI-4319440;
CC Q5TGU0; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12195249, EBI-781551;
CC Q5TGU0; P30040: ERP29; NbExp=3; IntAct=EBI-12195249, EBI-946830;
CC Q5TGU0; P12314: FCGR1A; NbExp=3; IntAct=EBI-12195249, EBI-2869867;
CC Q5TGU0; O15552: FFAR2; NbExp=3; IntAct=EBI-12195249, EBI-2833872;
CC Q5TGU0; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12195249, EBI-12142257;
CC Q5TGU0; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-12195249, EBI-12175685;
CC Q5TGU0; Q9UJ14: GGT7; NbExp=3; IntAct=EBI-12195249, EBI-1058791;
CC Q5TGU0; O95377: GJB5; NbExp=3; IntAct=EBI-12195249, EBI-3909454;
CC Q5TGU0; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12195249, EBI-13345167;
CC Q5TGU0; O15529: GPR42; NbExp=3; IntAct=EBI-12195249, EBI-18076404;
CC Q5TGU0; P24593: IGFBP5; NbExp=3; IntAct=EBI-12195249, EBI-720480;
CC Q5TGU0; P48051: KCNJ6; NbExp=3; IntAct=EBI-12195249, EBI-12017638;
CC Q5TGU0; P26715: KLRC1; NbExp=3; IntAct=EBI-12195249, EBI-9018187;
CC Q5TGU0; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-12195249, EBI-358888;
CC Q5TGU0; P21145: MAL; NbExp=3; IntAct=EBI-12195249, EBI-3932027;
CC Q5TGU0; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-12195249, EBI-10317612;
CC Q5TGU0; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12195249, EBI-11956541;
CC Q5TGU0; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-12195249, EBI-2858252;
CC Q5TGU0; P11836: MS4A1; NbExp=3; IntAct=EBI-12195249, EBI-2808234;
CC Q5TGU0; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12195249, EBI-716063;
CC Q5TGU0; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-12195249, EBI-949945;
CC Q5TGU0; Q8NC24: RELL2; NbExp=3; IntAct=EBI-12195249, EBI-10269209;
CC Q5TGU0; Q86VR2: RETREG3; NbExp=5; IntAct=EBI-12195249, EBI-10192441;
CC Q5TGU0; Q9NS64: RPRM; NbExp=3; IntAct=EBI-12195249, EBI-1052363;
CC Q5TGU0; Q14973: SLC10A1; NbExp=3; IntAct=EBI-12195249, EBI-3923031;
CC Q5TGU0; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12195249, EBI-18159983;
CC Q5TGU0; O95436-2: SLC34A2; NbExp=3; IntAct=EBI-12195249, EBI-12811757;
CC Q5TGU0; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-12195249, EBI-7225508;
CC Q5TGU0; P30825: SLC7A1; NbExp=3; IntAct=EBI-12195249, EBI-4289564;
CC Q5TGU0; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-12195249, EBI-10819434;
CC Q5TGU0; P27105: STOM; NbExp=3; IntAct=EBI-12195249, EBI-1211440;
CC Q5TGU0; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-12195249, EBI-8032987;
CC Q5TGU0; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-12195249, EBI-2844246;
CC Q5TGU0; Q969K7: TMEM54; NbExp=3; IntAct=EBI-12195249, EBI-3922833;
CC Q5TGU0; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-12195249, EBI-11742770;
CC Q5TGU0; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-12195249, EBI-744988;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19729679}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19729679}. Cell membrane
CC {ECO:0000269|PubMed:27641616, ECO:0000269|PubMed:31989647}; Multi-pass
CC membrane protein. Note=Localizes to the plasma membrane and
CC intracellular membranes in developing and mature erythrocytes.
CC {ECO:0000269|PubMed:27641616, ECO:0000269|PubMed:31989647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5TGU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TGU0-2; Sequence=VSP_026363, VSP_026364;
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes (at protein level).
CC {ECO:0000269|PubMed:27641616}.
CC -!- DEVELOPMENTAL STAGE: Expression levels increase during erythrocyte
CC differentiation. {ECO:0000269|PubMed:27641616}.
CC -!- DOMAIN: The C-terminal region mediates cholesterol-binding.
CC {ECO:0000250|UniProtKB:Q9CRZ8}.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; AL031778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104440; AAI04441.1; -; mRNA.
DR EMBL; BC104441; AAI04442.1; -; mRNA.
DR EMBL; BC137560; AAI37561.1; -; mRNA.
DR EMBL; BC137565; AAI37566.1; -; mRNA.
DR EMBL; BC144710; AAI44711.1; -; mRNA.
DR CCDS; CCDS34444.1; -. [Q5TGU0-1]
DR RefSeq; NP_001010873.1; NM_001010873.2. [Q5TGU0-1]
DR RefSeq; NP_001153198.1; NM_001159726.1. [Q5TGU0-1]
DR RefSeq; XP_011512698.1; XM_011514396.2. [Q5TGU0-1]
DR RefSeq; XP_011512699.1; XM_011514397.2. [Q5TGU0-1]
DR AlphaFoldDB; Q5TGU0; -.
DR SMR; Q5TGU0; -.
DR BioGRID; 128807; 58.
DR IntAct; Q5TGU0; 56.
DR STRING; 9606.ENSP00000362255; -.
DR TCDB; 9.A.24.1.17; the mitochondrial cholesterol/porphyrin/5-aminolevulinic acid uptake translocator protein (tspo) family.
DR iPTMnet; Q5TGU0; -.
DR PhosphoSitePlus; Q5TGU0; -.
DR BioMuta; TSPO2; -.
DR DMDM; 74746518; -.
DR PaxDb; Q5TGU0; -.
DR PRIDE; Q5TGU0; -.
DR Antibodypedia; 76908; 4 antibodies from 4 providers.
DR DNASU; 222642; -.
DR Ensembl; ENST00000373158.6; ENSP00000362252.2; ENSG00000112212.12. [Q5TGU0-2]
DR Ensembl; ENST00000373161.6; ENSP00000362255.1; ENSG00000112212.12. [Q5TGU0-1]
DR Ensembl; ENST00000470917.1; ENSP00000419985.1; ENSG00000112212.12. [Q5TGU0-1]
DR GeneID; 222642; -.
DR KEGG; hsa:222642; -.
DR MANE-Select; ENST00000373161.6; ENSP00000362255.1; NM_001010873.3; NP_001010873.1.
DR UCSC; uc003opj.4; human. [Q5TGU0-1]
DR CTD; 222642; -.
DR GeneCards; TSPO2; -.
DR HGNC; HGNC:21256; TSPO2.
DR HPA; ENSG00000112212; Tissue enriched (bone).
DR MIM; 619409; gene.
DR neXtProt; NX_Q5TGU0; -.
DR OpenTargets; ENSG00000112212; -.
DR PharmGKB; PA165618396; -.
DR VEuPathDB; HostDB:ENSG00000112212; -.
DR eggNOG; KOG3797; Eukaryota.
DR GeneTree; ENSGT00390000012980; -.
DR HOGENOM; CLU_091805_2_1_1; -.
DR InParanoid; Q5TGU0; -.
DR OMA; RDSLCPE; -.
DR OrthoDB; 1592225at2759; -.
DR PhylomeDB; Q5TGU0; -.
DR TreeFam; TF342852; -.
DR PathwayCommons; Q5TGU0; -.
DR SignaLink; Q5TGU0; -.
DR SIGNOR; Q5TGU0; -.
DR BioGRID-ORCS; 222642; 8 hits in 1059 CRISPR screens.
DR GenomeRNAi; 222642; -.
DR Pharos; Q5TGU0; Tbio.
DR PRO; PR:Q5TGU0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5TGU0; protein.
DR Bgee; ENSG00000112212; Expressed in trabecular bone tissue and 105 other tissues.
DR Genevisible; Q5TGU0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0140485; F:5-aminolevulinic acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0140484; P:5-aminolevulinic acid import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0098739; P:import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB.
DR Gene3D; 1.20.1260.100; -; 1.
DR InterPro; IPR038330; TspO/MBR-related_sf.
DR InterPro; IPR004307; TspO_MBR.
DR PANTHER; PTHR10057; PTHR10057; 1.
DR Pfam; PF03073; TspO_MBR; 1.
DR PIRSF; PIRSF005859; PBR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Membrane;
KW Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..170
FT /note="Translocator protein 2"
FT /id="PRO_0000292005"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 59..70
FT /note="YASYLVWKDLGG -> PCCTCCCCMGWW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026363"
FT VAR_SEQ 71..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026364"
SQ SEQUENCE 170 AA; 19129 MW; 8B705EFA0E2E1ABB CRC64;
MRLQGAIFVL LPHLGPILVW LFTRDHMSGW CEGPRMLSWC PFYKVLLLVQ TAIYSVVGYA
SYLVWKDLGG GLGWPLALPL GLYAVQLTIS WTVLVLFFTV HNPGLALLHL LLLYGLVVST
ALIWHPINKL AALLLLPYLA WLTVTSALTY HLWRDSLCPV HQPQPTEKSD
