V-type proton ATPase 16 kDa proteolipid subunit c (ATP6V0C)

V-type proton ATPase 16 kDa proteolipid subunit c (ATP6V0C) is the c-subunit of the V0 sector of vacuolar H+-ATPase (V-ATPase), a multi-subunit enzyme complex responsible for ATP-dependent proton translocation across intracellular membranes in eukaryotes[1][4][6]. This action acidifies organelles like lysosomes, endosomes, and secretory vesicles, which is critical for numerous cellular processes including protein degradation, receptor-mediated endocytosis, synaptic vesicle loading, and pH regulation[1][3][5][7]. ATP6V0C forms the proteolipid c-ring structure within the V0 domain, acting as the core proton-conducting channel[3][7]. Disruption or mutation of ATP6V0C impairs organelle acidification and is associated with neurological defects (including epilepsy and febrile seizures) and has been implicated in cancer-related chemoresistance and cell migration[3][5]. Though V-ATPase inhibitors exist, selective targeting of ATP6V0C remains challenging due to its essential and ubiquitous roles[5][7].

Other names

ATP6CATP6LATPLVATLVma3VPPCEPEO3V-ATPase 16 kDa proteolipid subunit cVacuolar proton pump 16 kDa proteolipid subunit cATPase, H+ transporting, lysosomal 16 kDa, V0 subunit cH(+)-transporting two-sector ATPase 16 kDa subunitVacuolar ATP synthase 16 kDa proteolipid subunitVacuolar H+ ATPase proton channel subunit

Inhibition of proton translocation; Disruption of organelle acidification; Blockade of autophagic flux and lysosomal function