V-type proton ATPase subunit d1 (ATP6V0D1)

V-type proton ATPase subunit d1 (ATP6V0D1) is a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme complex that physically resides within cellular membranes and orchestrates the acidification of organelles such as lysosomes, endosomes, and secretory vesicles[1][2][3]. This subunit is part of the V0 (membrane-bound) domain of V-ATPase, contributing to the proton translocation mechanism which is coupled to ATP hydrolysis in the V1 (cytosolic) domain[1][3]. Acidification generated by V-ATPase is vital for key cellular processes including proteolytic activation, protein sorting, synaptic function, and autophagy, as well as regulating iron metabolism and ciliary trafficking[2][3]. ATP6V0D1 is ubiquitously expressed, and its efficient coupling of ATP hydrolysis to proton movement distinguishes it from other d subunit isoforms. Dysfunction of V-ATPase, including ATP6V0D1, is implicated in cancer, neurodegeneration, and skeletal disease, with broad but non-specific small-molecule inhibitors like bafilomycin A1 known to target the complex but not individual subunits[3].

Other names

V-ATPase subunit d1V-type proton ATPase subunit d 1ATP6DP39ATP6DVVATXVPATPDVMA632 kDa accessory protein40 kDa accessory proteinAC39 subunitVacuolar proton pump subunit d 1H(+)-transporting two-sector ATPase subunit DATPase, H+ transporting, lysosomal 38kDaV0 subunit d1V-ATPase subunit DV-ATPase subunit D1

Inhibition of proton transport/ATPase activity (e.g., by Bafilomycin A1 blocks acidification required for endolysosomal function and autophagy)