Hspd1
entrez
63868
canonical
uniprot
P63039
canonical
ensembl
ENSRNOG00000014525
resolver
ensembl
ENSRNOG00055004630
resolver
ensembl
ENSRNOG00060024687
resolver
ensembl
ENSRNOG00065003073
resolver
ensp
ENSRNOP00000063666
resolver
ensp
ENSRNOP00055005506
resolver
ensp
ENSRNOP00060035384
resolver
ensp
ENSRNOP00065003096
resolver
enst
ENSRNOT00000066589
resolver
enst
ENSRNOT00055007348
resolver
enst
ENSRNOT00060042708
resolver
enst
ENSRNOT00065004330
resolver
genesymbol
Hspd1
resolver
genesymbol_syn
Hsp60
resolver
uniprot
A0A482IDN3
resolver
uniprot
P19226
resolver
uniprot
P19227
resolver
uniprot
P97602
resolver
uniprot_entry
A0A482IDN3_RAT
resolver
uniprot_entry
CH60_RAT
resolver
uniprot_sec
P19226
resolver
uniprot_sec
P19227
resolver
uniprot_sec
P97602
resolver
amino_acid_sequence
MLRLPTVLRQMRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQAHDLGKVGEVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
uniprot
proteins
ec_number
5.6.1.7
uniprot
proteins
function
FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P10809}.
uniprot
proteins
mass_dalton
60955
uniprot
proteins
protein_family
Chaperonin (HSP60) family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1976241
uniprot
proteins
pubmed
1979858
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
573
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P10809}.
uniprot
proteins