| 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 (Probable). |
| Protein Name | 60 Kda Heat Shock Protein - Mitochondrial60 Kda ChaperoninChaperonin 60Cpn60Heat Shock Protein 60Hsp-60Hsp60Heat Shock Protein Family D Member 1Hucha60Mitochondrial Matrix Protein P1P60 Lymphocyte Protein |
| Database Links | Reactome: R-HSA-1268020Reactome: R-HSA-8869496Reactome: R-HSA-9837999Reactome: R-HSA-9841251 |
| Cellular Localisation | Mitochondrion Matrix |
| Alternative Protein Names | 60 Kda Heat Shock Protein - Mitochondrial protein60 Kda Chaperonin proteinChaperonin 60 proteinCpn60 proteinHeat Shock Protein 60 proteinHsp-60 proteinHsp60 proteinHeat Shock Protein Family D Member 1 proteinHucha60 proteinMitochondrial Matrix Protein P1 proteinP60 Lymphocyte Protein proteinHSPD1 proteinHSP60 protein |
Information sourced from Uniprot.org
