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 a cytosolic V1 domain and a transmembrane 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 gene encodes the regulatory H subunit of the V1 domain which is required for catalysis of ATP but not the assembly of V-ATPase. Three alternatively spliced transcript variants encode two isoforms of the H subunit.[7]
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.
Nishi T, Forgac M (Feb 2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps".Nature Reviews Molecular Cell Biology.3 (2):94–103.doi:10.1038/nrm729.PMID11836511.S2CID21122465.
Pedersen PL (Oct 2002). "Transport ATPases in biological systems and relationship to human disease: a brief overview".Journal of Bioenergetics and Biomembranes.34 (5):327–32.doi:10.1023/A:1021249701287.PMID12539959.S2CID38318926.