CH60_MESAU
ID CH60_MESAU Reviewed; 271 AA.
AC P86206;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=60 kDa heat shock protein, mitochondrial {ECO:0000250|UniProtKB:P10809};
DE EC=5.6.1.7 {ECO:0000250|UniProtKB:P10809};
DE AltName: Full=60 kDa chaperonin {ECO:0000250|UniProtKB:P10809};
DE AltName: Full=Chaperonin 60 {ECO:0000250|UniProtKB:P10809};
DE Short=CPN60 {ECO:0000250|UniProtKB:P10809};
DE AltName: Full=Heat shock protein 60 {ECO:0000250|UniProtKB:P10809};
DE Short=HSP-60 {ECO:0000250|UniProtKB:P10809};
DE Short=Hsp60 {ECO:0000250|UniProtKB:P10809};
DE AltName: Full=Mitochondrial matrix protein P1 {ECO:0000250|UniProtKB:P10809};
DE Flags: Fragments;
GN Name=HSPD1 {ECO:0000250|UniProtKB:P10809};
GN Synonyms=HSP60 {ECO:0000250|UniProtKB:P10809};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Chaperonin implicated in mitochondrial protein import and
CC macromolecular assembly. Together with Hsp10, facilitates the correct
CC folding of imported proteins. May also prevent misfolding and promote
CC the refolding and proper assembly of unfolded polypeptides generated
CC under stress conditions in the mitochondrial matrix. The functional
CC units of these chaperonins consist of heptameric rings of the large
CC subunit Hsp60, which function as a back-to-back double ring. In a
CC cyclic reaction, Hsp60 ring complexes bind one unfolded substrate
CC protein per ring, followed by the binding of ATP and association with 2
CC heptameric rings of the co-chaperonin Hsp10. This leads to
CC sequestration of the substrate protein in the inner cavity of Hsp60
CC where, for a certain period of time, it can fold undisturbed by other
CC cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits
CC results in the dissociation of the chaperonin rings and the release of
CC ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P10809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7;
CC Evidence={ECO:0000250|UniProtKB:P10809};
CC -!- SUBUNIT: Homoheptamer arranged in a ring structure. The functional
CC units of these chaperonins consist of heptameric rings of the large
CC subunit Hsp60, which function as a back-to-back double ring. Interacts
CC with 2 heptameric Hsp10 rings to form the symmetrical football complex
CC (By similarity). Interacts with HRAS (By similarity). Interacts with
CC ATAD3A. Interacts with ETFBKMT and EEF1AKMT3 (By similarity). Interacts
CC with MFHAS1 (By similarity). {ECO:0000250|UniProtKB:P10809,
CC ECO:0000250|UniProtKB:P63038}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P10809}.
CC -!- TISSUE SPECIFICITY: Detected at higher levels in caput epididymal
CC spermatazoa than in cauda epididymal spermatazoa (at protein level).
CC {ECO:0000269|PubMed:20400973}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000255}.
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DR AlphaFoldDB; P86206; -.
DR SMR; P86206; -.
DR PRIDE; P86206; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Isomerase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN <1..>271
FT /note="60 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000394298"
FT BINDING 50..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 97
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 97
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 112
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 112
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 126
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 126
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 175
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 237
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 270
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT NON_CONS 35..36
FT /evidence="ECO:0000305"
FT NON_CONS 60..61
FT /evidence="ECO:0000305"
FT NON_CONS 84..85
FT /evidence="ECO:0000305"
FT NON_CONS 112..113
FT /evidence="ECO:0000305"
FT NON_CONS 166..167
FT /evidence="ECO:0000305"
FT NON_CONS 218..219
FT /evidence="ECO:0000305"
FT NON_CONS 237..238
FT /evidence="ECO:0000305"
FT NON_CONS 263..264
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 271
SQ SEQUENCE 271 AA; 29037 MW; 67E44F0121B5BC7C CRC64;
ALMLQGVDLL ADAVAVTMGP KGRTVIIEQS WGSPKLVQDV ANNTNEEAGD GTTTATVLAR
GANPVEIRRG VMLAVDAVIA ELKKTLNDEL EIIEGMKFDR GYISPYFINT SKCEFQDAYV
LLSEKKISSV QSIVPALEIA NAHRKPLVII AEDVDGEALS TLVLNRVGLQ VVAVKAPGFG
DNRKNQLKDM AIATGGAVFG EEGLNLNLED VQAHDLGKIQ EITEQLDITT SEYEKEKVTD
ALNATRAAVE EGIVLGGGCA LLRIGIEIIK R
