Family

Heat shock protein Hsp33 (IPR000397)

Short name: Heat_shock_Hsp33

Family relationships

None.

Description

Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function [PMID: 10025400].

GO terms

Biological Process

GO:0006457 protein folding

Molecular Function

GO:0051082 unfolded protein binding

Cellular Component

GO:0005737 cytoplasm

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PIRSF
HAMAP
Pfam