This gene encodes a component ofvacuolarATPase (V-ATPase), a multisubunit enzyme that mediates acidification ofeukaryotic intracellularorganelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediatedendocytosis, andsynaptic vesicle proton gradient generation. V-ATPase is composed of acytosolic V1 domain and atransmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L.[7]
^van Hille B, Vanek M, Richener H, Green JR, Bilbe G (Nov 1993). "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase".Biochemical and Biophysical Research Communications.197 (1):15–21.doi:10.1006/bbrc.1993.2434.PMID8250920.
Stevens TH, Forgac M (1998). "Structure, function and regulation of the vacuolar (H+)-ATPase".Annual Review of Cell and Developmental Biology.13:779–808.doi:10.1146/annurev.cellbio.13.1.779.PMID9442887.
Hasebe M, Hanada H, Moriyama Y, Maeda M, Futai M (Mar 1992). "Vacuolar type H(+)-ATPase genes: presence of four genes including pseudogenes for the 16-kDa proteolipid subunit in the human genome".Biochemical and Biophysical Research Communications.183 (2):856–63.doi:10.1016/0006-291X(92)90562-Y.PMID1532310.
