ID   CH60_CANLF              Reviewed;          13 AA.
AC   P49818;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=60 kDa heat shock protein, mitochondrial;
DE            EC=5.6.1.7 {ECO:0000250|UniProtKB:P10809};
DE   AltName: Full=60 kDa chaperonin;
DE   AltName: Full=Chaperonin 60;
DE            Short=CPN60;
DE   AltName: Full=Heat shock protein 60;
DE            Short=HSP-60;
DE            Short=Hsp60;
DE   Flags: Fragment;
GN   Name=HSPD1; Synonyms=HSP60;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=9504812; DOI=10.1002/elps.1150181514;
RA   Dunn M.J., Corbett J.M., Wheeler C.H.;
RT   "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT   heart proteins.";
RL   Electrophoresis 18:2795-2802(1997).
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   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   UCD-2DPAGE; P49818; -.
DR   Proteomes; UP000002254; 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.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Isomerase;
KW   Mitochondrion; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..>13
FT                   /note="60 kDa heat shock protein, mitochondrial"
FT                   /id="PRO_0000063636"
FT   NON_TER         13
SQ   SEQUENCE   13 AA;  1385 MW;  C6571E012DBFE879 CRC64;
     AKDVXFGXDA RAL