CLIC2

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 chloride channel. The redox status of the active cysteine in Cys-X-X-Cys 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.

The active G-site has a dithiol Cys-X-X-Cys motif which mediates glutathione-dependent redox catalysis.

In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor. Displays weak glutathione peroxidase activity (Probable) (PubMed:25581026). Can insert into membranes and form chloride ion channels. Membrane insertion seems to be redox-regulated and may occur only under oxidizing conditions. Modulates the activity of RYR2 and inhibits calcium influx.

Belongs to the chloride channel CLIC family.

Expressed in adult and fetal brain, heart, skeletal muscle, liver, lung, and spleen. Detected in adult stomach and testis. Expressed in fetal thymus and kidney.

• Cytoplasm
• Membrane
• Single-pass membrane protein
• Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain.

Chloride intracellular channel protein 2, Glutaredoxin-like oxidoreductase CLIC2, Glutaredoxin-like peroxidase CLIC2, XAP121, CLIC2

• entrezGene:1193
• omim:300138
• swissprot:O15247

Proteins

28356Da