TSPO2_MOUSE
ID TSPO2_MOUSE Reviewed; 162 AA.
AC Q9CRZ8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Translocator protein 2;
DE AltName: Full=Peripheral-type benzodiazepine receptor-like protein 1;
GN Name=Tspo2; Synonyms=Bzrpl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DOMAIN.
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, AND DISRUPTION PHENOTYPE.
RX PubMed=32358067; DOI=10.1074/jbc.ra119.011679;
RA Kiatpakdee B., Sato K., Otsuka Y., Arashiki N., Chen Y., Tsumita T.,
RA Otsu W., Yamamoto A., Kawata R., Yamazaki J., Sugimoto Y., Takada K.,
RA Mohandas N., Inaba M.;
RT "Cholesterol-binding protein TSPO2 coordinates maturation and proliferation
RT of terminally differentiating erythroblasts.";
RL J. Biol. Chem. 295:8048-8063(2020).
CC -!- FUNCTION: Cholesterol-binding protein involved in the redistribution of
CC cholesterol from lipid droplets to the endoplasmic reticulum
CC (PubMed:19729679, PubMed:32358067). Required to meet cholesterol
CC demands during erythropoietic differentiation (PubMed:19729679,
CC PubMed:32358067). May play a role in transport processes at the plasma
CC membrane of erythrocytes, including regulating VDAC-mediated ATP
CC export, and import of the heme precursors protoporphyrin IX and 5-
CC aminolevulinic acid (By similarity). {ECO:0000250|UniProtKB:Q5TGU0,
CC ECO:0000269|PubMed:19729679, ECO:0000269|PubMed:32358067}.
CC -!- SUBUNIT: Homotetramer. May also form homodimer.
CC {ECO:0000250|UniProtKB:Q5TGU0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19729679}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19729679}. Cell membrane
CC {ECO:0000250|UniProtKB:Q5TGU0}; Multi-pass membrane protein.
CC Note=Localizes to the plasma membrane and intracellular membranes in
CC developing and mature erythrocytes. {ECO:0000250|UniProtKB:Q5TGU0}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, bone marrow and spleen. In
CC spleen, detected in red pulp but not in white pulp.
CC {ECO:0000269|PubMed:19729679}.
CC -!- DEVELOPMENTAL STAGE: Not expressed at 10.5 dpc. First detected at 12.5
CC dpc in the primordial liver (PubMed:19729679). Increased hepatic levels
CC are found at 15.5 dpc followed by decline throughout newborn stage P1
CC and postnatal stages P5 and P10 with no hepatic expression in the adult
CC (PubMed:19729679). In bone marrow, expressed during late gestation
CC stages and remains elevated until adulthood (PubMed:19729679). In
CC newborn and adult mice, also expressed in spleen (PubMed:19729679).
CC {ECO:0000269|PubMed:19729679}.
CC -!- DOMAIN: The C-terminal region mediates cholesterol-binding.
CC {ECO:0000269|PubMed:19729679}.
CC -!- DISRUPTION PHENOTYPE: Decreases erythrocyte count and increases
CC reticulocyte count (PubMed:32358067). Abnormal erythroblast cytokinesis
CC and differentiation (PubMed:32358067). Decreases hemoglobin levels in
CC maturing erythroid cells (PubMed:32358067).
CC {ECO:0000269|PubMed:32358067}.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; AK011003; BAB27322.2; -; mRNA.
DR EMBL; BC104344; AAI04345.1; -; mRNA.
DR EMBL; BC104345; AAI04346.1; -; mRNA.
DR CCDS; CCDS28869.1; -.
DR RefSeq; NP_081568.1; NM_027292.2.
DR RefSeq; XP_017173120.1; XM_017317631.1.
DR AlphaFoldDB; Q9CRZ8; -.
DR SMR; Q9CRZ8; -.
DR STRING; 10090.ENSMUSP00000024794; -.
DR PhosphoSitePlus; Q9CRZ8; -.
DR PaxDb; Q9CRZ8; -.
DR PRIDE; Q9CRZ8; -.
DR ProteomicsDB; 297730; -.
DR Antibodypedia; 76908; 4 antibodies from 4 providers.
DR DNASU; 70026; -.
DR Ensembl; ENSMUST00000024794; ENSMUSP00000024794; ENSMUSG00000023995.
DR GeneID; 70026; -.
DR KEGG; mmu:70026; -.
DR UCSC; uc008cxy.1; mouse.
DR CTD; 222642; -.
DR MGI; MGI:1917276; Tspo2.
DR VEuPathDB; HostDB:ENSMUSG00000023995; -.
DR eggNOG; KOG3797; Eukaryota.
DR GeneTree; ENSGT00390000012980; -.
DR InParanoid; Q9CRZ8; -.
DR OMA; RDSLCPE; -.
DR OrthoDB; 1592225at2759; -.
DR PhylomeDB; Q9CRZ8; -.
DR TreeFam; TF342852; -.
DR BioGRID-ORCS; 70026; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Tspo2; mouse.
DR PRO; PR:Q9CRZ8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CRZ8; protein.
DR Bgee; ENSMUSG00000023995; Expressed in bone marrow and 51 other tissues.
DR ExpressionAtlas; Q9CRZ8; baseline and differential.
DR Genevisible; Q9CRZ8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0140485; F:5-aminolevulinic acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0140484; P:5-aminolevulinic acid import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0098739; P:import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0032367; P:intracellular cholesterol transport; IMP:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IMP: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 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..162
FT /note="Translocator protein 2"
FT /id="PRO_0000292006"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 162 AA; 18286 MW; E18816C6B98B64E3 CRC64;
MQLQGPVFVG VPLLGPILIC MLIHQPSSRC EDERKLPWCP PHKVILLVWV TIYSVMGYAS
YLVWKELGGG FRWPLALPLG LYSFQLALSW TFLVLFLAAD SPGLALLDLL LLYGLVASLV
FIWQPINKLA ALLLLPYLAW LTVTTAITYR LWRDSLCPTY QP
