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The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (By similarity). Plays a redundant role in the efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress (By similarity). The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (By similarity). Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (PubMed:36522427, PubMed:36928458). May play a role in adipogenesis (PubMed:15184384, PubMed:15564382, PubMed:21804215)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chloride(in) = chloride(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29823"},{"database":"ChEBI","id":"CHEBI:17996"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36522427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36928458"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"iodide(out) = iodide(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66324"},{"database":"ChEBI","id":"CHEBI:16382"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"taurine(out) = taurine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66328"},{"database":"ChEBI","id":"CHEBI:507393"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2',3'-cGAMP(out) = 2',3'-cGAMP(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66320"},{"database":"ChEBI","id":"CHEBI:143093"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66321"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:66322"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24782309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29769723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36522427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36928458"}],"value":"Heterohexamer; oligomerizes with other LRRC8 proteins (LRRC8A, LRRC8B, LRRC8D and/or LRRC8E) to form a heterohexamer (PubMed:24782309, PubMed:29769723, PubMed:36522427, PubMed:36928458). Homoheptamer; inactive, likely because it is not targeted to the plasma membrane in the absence of LRRC8A (PubMed:36522427). In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist (PubMed:36522427)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}],"value":"In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29769723"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15184384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15564382"}],"value":"Expressed at very low levels in adipose tissue"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15184384"}],"value":"Induced during the earliest stages of adipogenesis"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IWT6"}],"value":"The volume-regulated anion channel (VRAC) channel forms a trimer of dimers, with symmetry mismatch between the pore-forming domain and the cytosolic LRR repeats, a topology similar to gap junction proteins"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TDW0"}],"value":"The cytoplasmic N-terminus preceding the first transmembrane (residues 1-22) regulates volume-regulated anion channel (VRAC) conductance, ion permeability and inactivation gating"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21804215"}],"value":"Mice do not show remarkable changes in body weight or the weight of white adipose tissue on a chow diet, but display significantly lower body weights and fat mass than wild-type mice when fed a high-fat diet. Moreover, improved insulin resistance induced by the high-fat diet is observed"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the LRRC8 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":803,"modifier":"EXACT"}},"description":"Volume-regulated anion channel subunit LRRC8C","featureId":"PRO_0000076248"},{"type":"Topological 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