Recombinant Human 10 kDa heat shock protein, mitochondrial (HSPE1)

Uniprot Id

P61604

Target Species

Human

Target Name

HSPE1

Target Full Name

10 kDa heat shock protein, mitochondrial

Target 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.

Target Subcellular Location

Mitochondrion matrix.

Target Protein Families

GroES chaperonin family

Target Research Area

Neuroscience

Target Synonyms

10 kDa chaperonin; 10 kDa heat shock protein mitochondrial; 10 kDa heat shock protein; mitochondrial; CH10_HUMAN; Chaperonin 10; Chaperonin 10 homolog; CPN10; cpn10 homolog; Early pregnancy factor; Early-pregnancy factor; EPF; GROES; GroES homolog; Heat shock 10kD protein 1 chaperonin 10; Heat shock 10kDa protein 1; Heat shock 10kDa protein 1 chaperonin 10; Heat shock protein family E (Hsp10) member; Heat-shock 10-kD protein; Hsp10; Hspe1

Target Background

This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.