Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The B subunit is non-catalytic but combines with other subunits to form the catalytic complex. V-ATPase is responsible for energizing electrophoretic K(+)/2H(+) antiport by generating a transmembrane voltage of more than 200 mV (By similarity). V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein). Detected on macropinosomes and phagosomes, on contractile vacuoles, cytoplasmic cisternae and on the tubular extensions linking these vesicles. Highly expressed during vegetative growth. Down-regulated in starving cells and during development. Down-regulated when cells are exposed to an acid environment. Up-regulated when cells are exposed to high pH. Belongs to the ATPase alpha/beta chains family.