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 (PubMed:32764564). 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 (PubMed:32764564). V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (PubMed:32764564). 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 (PubMed:32764564). 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 ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564). Interacts with the V0 complex V-ATPase subunit a4 ATP6V0A4 (By similarity). Interacts with LASS2 (By similarity). Interacts with RNF182; this interaction leads to ubiquitination and degradation via the proteasome pathway (By similarity). Expressed in brain (at protein level). Ubiquitinated by RNF182, leading to its degradation via the ubiquitin-proteasome pathway. Belongs to the V-ATPase proteolipid subunit family.