Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). 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 (By similarity). Required along with other vacuolar ATPase components for the removal of protein aggregates which form in immature oocytes in the distal gonad (PubMed:29168500). This removal occurs as the oocytes mature and move to the proximal gonad, is triggered by the introduction of sperm through mating and occurs before fertilization (PubMed:29168500). The introduction of sperm triggers V-ATPase accumulation in proximal oocytes and induces lysosomal acidification which leads to engulfing of protein aggregates by lysosomes and subsequent clearance of the aggregates (PubMed:29168500). Lysosomal acidification also leads to changes in mitochondrial morphology and function (PubMed:29168500). Mitochondria in distal immature oocytes are fragmented, produce high levels of reactive oxygen species (ROS) and have high membrane potential, indicative of metabolic inactivity (PubMed:29168500). In contrast, mitochondria in proximal mature oocytes are tubular with lower ROS levels and membrane potential, indicative of an active metabolic state required for aggregate mobilization before clearance (PubMed:29168500). Plays a role in the processing and secretion of the aspartic protease hrg-7 from the intestine (PubMed:28581477). During embryonic development, the V-ATPase is required to repress fusion of epidermal cells probably by negatively regulating eff-1-mediated cell fusion (PubMed:15866168). Involved in receptor-mediated endocytosis (PubMed:16785323). V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (By similarity). The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity). The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits vah-19/Ac45 and vah-20/PRR (By similarity). Adult H-shaped excretory cell and rectum. High levels during embryogenesis, moderate levels during L1 and adult stages and very low levels during L2-L4 stages. RNAi-mediated knockdown causes embryonic lethality (PubMed:16785323). RNAi-mediated knockdown results in increased protein aggregation in the oocytes of sperm-deficient young adult females which is not eliminated by mating (PubMed:29168500). RNAi-mediated knockdown causes hyperfusion of embryonic epidermal cells (PubMed:15866168). RNAi-mediated knockdown results in the accumulation of the aspartic protease hrg-7 in its immature uncleaved form and in the intestine (PubMed:28581477). Causes defects in alae formation in the few surviving larvae and impairs yolk uptake by the oocytes from the pseudoceolomic cavities (PubMed:16785323). Causes an increase in the section of the excretory canal, which often has multiple lumens and abnormal whorls (PubMed:16785323). Belongs to the V-ATPase proteolipid subunit family.