Search Results

Overview

Uniprot ID	H0VUC2
Protein Name	10 kDa heat shock protein, mitochondrial
Gene Name	LOC100715002
Organism	Cavia porcellus

Kla Sites from experimental identification

Position	Flanking peptide
56	VGSGSKGKGGEIQPV
8	MAGQAFRKFLPLFDR

Function

Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, 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

Protein Sequence

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005759	mitochondrial matrix
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0044183	protein folding chaperone
Molecular Function	GO:0051087	protein-folding chaperone binding
Molecular Function	GO:0051082	unfolded protein binding

Reference

[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.