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CLIC1

Domain

The active G-site contains a monothiol Cys-X-X-Ser motif which mediates glutathione-dependent redox catalysis.

Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as a channel. The redox status of the active cysteine in Cys-X-X-Cys/Ser motif likely determines the capacity to adopt a soluble or membrane-inserted state. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion.

Function

In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor. Reduces selenite and dehydroascorbate and may act as an antioxidant during oxidative stress response (PubMed:25581026, PubMed:37759794). Can insert into membranes and form voltage-dependent multi-ion conductive channels. Membrane insertion seems to be redox-regulated and may occur only under oxidizing conditions. Involved in regulation of the cell cycle.

Post-translational modifications

Hydrogen peroxide treatment causes a conformation change, leading to dimerization and formation of an intramolecular disulfide bond between Cys-24 and Cys-59.

Sequence Similarities

Belongs to the chloride channel CLIC family.

Tissue Specificity

Expression is prominent in heart, placenta, liver, kidney and pancreas.

Cellular localization

Alternative names

G6, NCC27, CLIC1, Chloride intracellular channel protein 1, Chloride channel ABP, Glutaredoxin-like oxidoreductase CLIC1, Glutathione-dependent dehydroascorbate reductase CLIC1, Nuclear chloride ion channel 27, Regulatory nuclear chloride ion channel protein, hRNCC

swissprot:O00299 entrezGene:1192 omim:602872