ATP6V0D1
Description
The ATP6V0D1 (ATPase H+ transporting V0 subunit d1) is a protein-coding gene located on chromosome 16.
ATP6V0D1 is a gene that encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for intracellular processes such as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic 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. ATP6V0D1 encodes the D subunit, which is ubiquitously found.
ATP6V0D1, also known as V-type proton ATPase subunit d 1, is a subunit of the V0 complex of vacuolar (H+)-ATPase (V-ATPase). V-ATPase is a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and, in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. ATP6V0D1 may play a role in coupling of proton transport and ATP hydrolysis. In aerobic conditions, ATP6V0D1 is involved in intracellular iron homeostasis, triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes and leading to HIF1A hydroxylation and subsequent proteasomal degradation. ATP6V0D1 may also play a role in cilium biogenesis through regulation of the transport and localization of proteins to the cilium.
ATP6V0D1 is also known as ATP6D, ATP6DV, P39, VATX, VMA6, VPATPD.
