Overview
| Uniprot ID | S4R3N1 |
|---|
| Protein Name | 10 kDa heat shock protein, mitochondrial |
|---|
| Gene Name | HSPE1-MOB4 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 56 |
VGSGSKGKDFYNWPD |
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
MAGQAFRKFL
20
PLFDRVLVER
30
SAAETVTKGG
40
IMLPEKSQGK
50
VLQATVVAVG
60
SGSKGKDFYN
70
WPDESFDEMD
80
STLAVQQYIQ
90
QNIRADCSNI
100
DKILEPPEGQ
110
DEGVWKYEHL
120
RQFCLELNGL
130
AVKLQSECHP
140
DTCTQMTATE
150
QWIFLCAAHK
160
TPKECPAIDY
170
TRHTLDGAAC
180
LLNSNKYFPS
190
RVSIKESSVA
200
KLGSVCRRIY
210
RIFSHAYFHH
220
RQIFDEYENE
230
TFLCHRFTKF
240
VMKYNLMSKD
250
NLIVPILEEE
260
VQNSVSGESE
A
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0032580 |
Golgi cisterna membrane |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0044183 |
protein folding chaperone |
Reference
PMID: N/A