Overview
| Uniprot ID | A0A8W4FL80 |
|---|
| Protein Name | 10 kDa heat shock protein, mitochondrial |
|---|
| Gene Name | HSPE1 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 27 |
SAAETVTKGGIMLPE |
| 35 |
GGIMLPEKSQGKVLQ |
| 39 |
LPEKSQGKVLQATVV |
| 53 |
VAVGSGSKGKGGEIQ |
| 55 |
VGSGSKGKGGEIQPV |
| 65 |
EIQPVSVKVGDKVLL |
| 69 |
VSVKVGDKVLLPEYG |
| 7 |
*AGQAFRKFLPLFDR |
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
10
AGQAFRKFLP
20
LFDRVLVERS
30
AAETVTKGGI
40
MLPEKSQGKV
50
LQATVVAVGS
60
GSKGKGGEIQ
70
PVSVKVGDKV
80
LLPEYGGTRV
90
VLDDKDYFLF
100
RDGDILGKYV
D
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0044183 |
protein folding chaperone |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.