TRAP1_RAT
ID TRAP1_RAT Reviewed; 706 AA.
AC Q5XHZ0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PROTEIN SEQUENCE OF 307-318 AND 442-451, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND THR-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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; BC083909; AAH83909.1; -; mRNA.
DR RefSeq; NP_001034090.1; NM_001039001.1.
DR AlphaFoldDB; Q5XHZ0; -.
DR SMR; Q5XHZ0; -.
DR IntAct; Q5XHZ0; 1.
DR MINT; Q5XHZ0; -.
DR STRING; 10116.ENSRNOP00000008966; -.
DR iPTMnet; Q5XHZ0; -.
DR PhosphoSitePlus; Q5XHZ0; -.
DR jPOST; Q5XHZ0; -.
DR PaxDb; Q5XHZ0; -.
DR PRIDE; Q5XHZ0; -.
DR GeneID; 287069; -.
DR KEGG; rno:287069; -.
DR UCSC; RGD:1359733; rat.
DR CTD; 10131; -.
DR RGD; 1359733; Trap1.
DR VEuPathDB; HostDB:ENSRNOG00000005418; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_3_1_1; -.
DR InParanoid; Q5XHZ0; -.
DR OMA; YTRKVLI; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q5XHZ0; -.
DR TreeFam; TF315234; -.
DR PRO; PR:Q5XHZ0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000005418; Expressed in liver and 19 other tissues.
DR Genevisible; Q5XHZ0; RN.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IPI: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; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009386; P:translational attenuation; ISO:RGD.
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_0000273250"
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:0007744|PubMed:16641100"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12931"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQN1"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQN1"
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:0000250|UniProtKB:Q12931"
FT MOD_RES 433
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQN1"
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; 80461 MW; AE64073BAEE5681C CRC64;
MARELRALLL WGRGLQSALR APALAGVRRG KPVLHLQKTT VHFRDPTQSL ASGISAGQLY
STQAAEDKKE EALHSIISNT EAVQGSVSKH EFQAETKKLL DIVARSLYSE KEVFIRELIS
NASDALEKLR HKRVCEGQVL PEMEIHLQTD AEKGTITIQD TGIGMTKEEL VSNLGTIARS
GSKAFLEALQ HQAETSSRII GQFGVGFYSA FMVADKVEVY SRPAAPESPG YQWLSDGSGV
FEIAEASGVR PGTKIIIHLK SDCKDFANES RVQDVVTKYS NFVSFPLYLN GRRINTLQAI
WMMDPKDISE FQHEEFYRYI AQAYDKPRFI LHYKTDAPLN IRSIFYVPEM KPSMFDVSRE
LGSSVALYSR KVLIQTKATD ILPKWLRFVR GVVDSEDIPL NLSRELLQES ALIRKLRDVL
QQRLIKFFID QSKKDAEKYA KFFEDYGLFM REGIVTTAEQ DIKEDIAKLL RYESSALPAG
QLTSLSDYAS RMQAGTRNIY YLCAPNRHLA EHSPYYEAMK QKQTEVLFCY EQFDELTLLH
LREFDKKKLI SVETDIVVDH YKEEKFEDTS PAGERLSEKE TEELMAWMRN ALGSRVTNVK
VTFRLDTHPA MVTVLEMGAA RHFLRMQQLA KTQEERAQLL QPTLEINPRH TLIKKLNQLR
EREPELAQLL VDQIYENAMI AAGLVDDPRA MVGRLNDLLV KALERH
