TRAP1_BOVIN
ID TRAP1_BOVIN Reviewed; 703 AA.
AC Q2TBI4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Interacts with SRC (By
CC similarity). Interacts with SDHA (By similarity). {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; BC110148; AAI10149.1; -; mRNA.
DR RefSeq; NP_001033764.1; NM_001038675.2.
DR AlphaFoldDB; Q2TBI4; -.
DR SMR; Q2TBI4; -.
DR BioGRID; 171097; 1.
DR STRING; 9913.ENSBTAP00000026786; -.
DR PaxDb; Q2TBI4; -.
DR PeptideAtlas; Q2TBI4; -.
DR PRIDE; Q2TBI4; -.
DR Ensembl; ENSBTAT00000026786; ENSBTAP00000026786; ENSBTAG00000020109.
DR GeneID; 514472; -.
DR KEGG; bta:514472; -.
DR CTD; 10131; -.
DR VEuPathDB; HostDB:ENSBTAG00000020109; -.
DR VGNC; VGNC:36283; TRAP1.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_3_1_1; -.
DR InParanoid; Q2TBI4; -.
DR OMA; YTRKVLI; -.
DR OrthoDB; 924636at2759; -.
DR TreeFam; TF315234; -.
DR PRO; PR:Q2TBI4; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000020109; Expressed in cardiac ventricle and 108 other tissues.
DR ExpressionAtlas; Q2TBI4; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
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; IBA:GO_Central.
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:0006457; P:protein folding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 57..703
FT /note="Heat shock protein 75 kDa, mitochondrial"
FT /id="PRO_0000245028"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XHZ0"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5XHZ0"
FT MOD_RES 423
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12931"
FT MOD_RES 430
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQN1"
FT MOD_RES 465
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12931"
FT MOD_RES 493
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12931"
SQ SEQUENCE 703 AA; 79381 MW; B40410E8C77A4C86 CRC64;
MARELRMLLL WGRRLRAPAL AAACGGKPVL CPWRPPAQSW GPPRSLASSF HVGRPFSSQA
AEDQAEAGPL HSVISSLEAV QGSATKHEFQ AETKKLLDIV ARSLYSEKEV FIRELISNAS
DALEKLRHKL VSEGQALPDM EIHLQTDADR GTITIQDTGV GMSREELVSN LGTIARSGSK
AFLDALQNQA EAGSKIIGQF GVGFYSAFMV ADRVEVYSRS VDAGSLGYRW LSDGSGVFEV
AEASGVRTGT KIIIHLKADS REFASEARVR DVVTKYSNFV SFPLYLNGRR MNTLQAIWMM
DPKDVGEGQH EEFYRYVAQA HDRPRYTLHY RTDAPLSIRS IFYVPDAKPS MFDVSRELGS
SVSLYSRKVL IQTKATNILP TWLRFVRGVV DSEDIPLNLS RELLQESALI RKLQGVLQQR
LIKFFTDQSK KDAEKYARFF EDYGLFVREG IVTTAEQEVK EDIAKLLRYE SSALPAGQLT
SLSDYASRMQ AGTRNIYYLC APNRHLAEHS PYYEAMKRKN TEVLFCYEQF DELTLLHLRE
FDKKKLISVE TDIVVDHYKE EKFEDGAPAG DCLSEKETED LMAWMRNALG SRITDVKVTL
RLDTHPAMIT VLEMGAARHF LRMRQLAKTQ EERAQLLQPT LEINPRHVLI KKLSQLRDSE
PDLAQLLVDQ IYENAMITAG LIDDPRPMVG RLNQLLVKAL ERH
