CLIC, N-terminal domain
IPR053823
Definition
This entry represents the N-terminal domain of chloride ion channels CLIC and related sequences. The chloride intracellular channel (CLICs) belong to the glutathione-S-transferase (GSTs) superfamily, highly conserved in vertebrates which usually possess six distinct paralogues (CLIC1-CLIC6) [[cite:PMID:20085760], [cite:PMID:15147738], [cite:PMID:11551966]]. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division and apoptosis. CLIC proteins can exist as both soluble globular proteins and integral membrane proteins with ion channel function [[cite:PMID:12202911], [cite:PMID:16176272]]. Membrane insertion is redox-regulated PMID:14613939 and has a strong pH dependence PMID:11978800; the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. This redox-controlled structural rearrangement exposes a large hydrophobic surface that may represent the docking interface of CLIC1 in its membrane-bound state [[cite:PMID:14613939], [cite:PMID:16581025]]. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity.
6 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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