ID   TRAP1_MOUSE             Reviewed;         706 AA.
AC   Q9CQN1; Q542I4;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Heat shock protein 75 kDa, mitochondrial;
DE            Short=HSP 75;
DE   AltName: Full=TNFR-associated protein 1;
DE   AltName: Full=Tumor necrosis factor type 1 receptor-associated protein;
DE            Short=TRAP-1;
DE   Flags: Precursor;
GN   Name=Trap1; Synonyms=Hsp75;
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, and NOD;
RC   TISSUE=Embryonic stem cell, Kidney, and Thymus;
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].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   PROTEIN SEQUENCE OF 391-404, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264; LYS-326; LYS-426 AND
RP   LYS-433, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Chaperone that expresses an ATPase activity. Involved in
CC       maintaining mitochondrial function and polarization, downstream of
CC       PINK1 and mitochondrial complex I. Is a negative regulator of
CC       mitochondrial respiration able to modulate the balance between
CC       oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1
CC       on mitochondrial respiration is probably mediated by modulation of
CC       mitochondrial SRC and inhibition of SDHA. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the intracellular domain of tumor necrosis factor
CC       type 1 receptor. Binds to RB1. Interacts with SRC. Interacts with SDHA.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC       membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; AK002409; BAB22078.1; -; mRNA.
DR   EMBL; AK010341; BAB26865.1; -; mRNA.
DR   EMBL; AK088471; BAC40374.1; -; mRNA.
DR   EMBL; BC022912; AAH22912.1; -; mRNA.
DR   CCDS; CCDS27914.1; -.
DR   RefSeq; NP_080784.1; NM_026508.2.
DR   AlphaFoldDB; Q9CQN1; -.
DR   SMR; Q9CQN1; -.
DR   BioGRID; 212597; 27.
DR   IntAct; Q9CQN1; 3.
DR   STRING; 10090.ENSMUSP00000006137; -.
DR   GlyGen; Q9CQN1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CQN1; -.
DR   PhosphoSitePlus; Q9CQN1; -.
DR   SwissPalm; Q9CQN1; -.
DR   REPRODUCTION-2DPAGE; Q9CQN1; -.
DR   EPD; Q9CQN1; -.
DR   jPOST; Q9CQN1; -.
DR   MaxQB; Q9CQN1; -.
DR   PaxDb; 10090-ENSMUSP00000006137; -.
DR   PeptideAtlas; Q9CQN1; -.
DR   ProteomicsDB; 298209; -.
DR   Pumba; Q9CQN1; -.
DR   Antibodypedia; 3798; 790 antibodies from 42 providers.
DR   DNASU; 68015; -.
DR   Ensembl; ENSMUST00000006137.9; ENSMUSP00000006137.9; ENSMUSG00000005981.12.
DR   GeneID; 68015; -.
DR   KEGG; mmu:68015; -.
DR   UCSC; uc007xzk.1; mouse.
DR   AGR; MGI:1915265; -.
DR   CTD; 10131; -.
DR   MGI; MGI:1915265; Trap1.
DR   VEuPathDB; HostDB:ENSMUSG00000005981; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   GeneTree; ENSGT01020000230401; -.
DR   HOGENOM; CLU_006684_3_1_1; -.
DR   InParanoid; Q9CQN1; -.
DR   OMA; DHTQQNE; -.
DR   OrthoDB; 5485387at2759; -.
DR   PhylomeDB; Q9CQN1; -.
DR   TreeFam; TF315234; -.
DR   BioGRID-ORCS; 68015; 5 hits in 81 CRISPR screens.
DR   ChiTaRS; Trap1; mouse.
DR   PRO; PR:Q9CQN1; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9CQN1; Protein.
DR   Bgee; ENSMUSG00000005981; Expressed in embryonic brain and 247 other cell types or tissues.
DR   ExpressionAtlas; Q9CQN1; baseline and differential.
DR   GO; GO:0071944; C:cell periphery; IDA:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0003723; F:RNA binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:1901856; P:negative regulation of cellular respiration; ISS:UniProtKB.
DR   GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0009386; P:translational attenuation; ISO:MGI.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   Genevisible; Q9CQN1; MM.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Direct protein sequencing; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT         1..60
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           61..706
FT                   /note="Heat shock protein 75 kDa, mitochondrial"
FT                   /id="PRO_0000013605"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XHZ0"
FT   MOD_RES         176
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XHZ0"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12931"
FT   MOD_RES         264
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         326
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         334
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12931"
FT   MOD_RES         426
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         433
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         468
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12931"
FT   MOD_RES         496
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12931"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12931"
SQ   SEQUENCE   706 AA;  80209 MW;  7183CE538CB36464 CRC64;
     MACELRAVLL WGRGLQTVLR APALAGVRRG KPVLHLQKTT VQFRGPTQSL ASGISAGQLY
     STQAAEDKEE ESLHSIISNT EAVRGSVSKH EFQAETKKLL DIVARSLYSE KEVFIRELIS
     NASDALEKLR HKLVCEGQVL PEMEIHLQTD AKKGTITIQD TGIGMTQEEL VSNLGTIARS
     GSKAFLEALQ NQAETSSKII GQFGVGFYSA FMVADKVEVY SRSAAPESPG YQWLSDGSGV
     FEIAEASGVR PGTKIIIHLK SDCKDFASES RVQDVVTKYS NFVSFPLYLN GKRINTLQAI
     WMMDPKDISE FQHEEFYRYI AQAYDKPRFT LHYKTDAPLN IRSIFYVPEM KPSMFDVSRE
     LGSSVALYSR KVLIQTKAAD ILPKWLRFIR GVVDSEDIPL NLSRELLQES ALIRKLRDVL
     QQRLIKFFID QSKKDAEKYA KFFEDYGLFM REGIVTTAEQ DIKEDIAKLL RYESSALPAG
     QLTSLPDYAS RMQAGTRNIY YLCAPNRHLA EHSPYYEAMK QKHTEVLFCY EQFDELTLLH
     LREFDKKKLI SVETDIVVDH YKEEKFEDTS PADERLSEKE TEDLMAWMRN ALGSRVTNVK
     VTFRLDTHPA MVTVLEMGAA RHFLRMQQLA KTQEERAQLL QPTLEINPRH TLIKKLCQLR
     ESEPELAQLL VDQIYENAMI AAGLVDDPRA MVGRLNDLLV KVLEKH
//