TRAP1_MOUSE
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 03-AUG-2022, entry version 165.
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; 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, Pancreas,
RC 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; 25.
DR IntAct; Q9CQN1; 3.
DR STRING; 10090.ENSMUSP00000006137; -.
DR iPTMnet; Q9CQN1; -.
DR PhosphoSitePlus; Q9CQN1; -.
DR SwissPalm; Q9CQN1; -.
DR REPRODUCTION-2DPAGE; Q9CQN1; -.
DR EPD; Q9CQN1; -.
DR jPOST; Q9CQN1; -.
DR MaxQB; Q9CQN1; -.
DR PaxDb; Q9CQN1; -.
DR PeptideAtlas; Q9CQN1; -.
DR PRIDE; Q9CQN1; -.
DR ProteomicsDB; 298209; -.
DR Antibodypedia; 3798; 729 antibodies from 42 providers.
DR DNASU; 68015; -.
DR Ensembl; ENSMUST00000006137; ENSMUSP00000006137; ENSMUSG00000005981.
DR GeneID; 68015; -.
DR KEGG; mmu:68015; -.
DR UCSC; uc007xzk.1; mouse.
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; YTRKVLI; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q9CQN1; -.
DR TreeFam; TF315234; -.
DR BioGRID-ORCS; 68015; 5 hits in 76 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 244 other tissues.
DR ExpressionAtlas; Q9CQN1; baseline and differential.
DR Genevisible; Q9CQN1; MM.
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: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 Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 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_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
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
