V-type proton ATPase subunit D (ATP6V1D)

V-type proton ATPase subunit D (ATP6V1D) is a protein component of the V1 domain of the V-ATPase complex, a multisubunit rotary enzyme that hydrolyzes ATP to transport protons across membranes and acidify intracellular compartments such as lysosomes, endosomes, and secretory vesicles[1][3][4][8]. The subunit D forms part of the central stalk (rotor) of the V1 complex, connecting ATP hydrolysis-driven conformational changes to membrane proton translocation[4][5]. V-ATPase-mediated acidification is essential for diverse cellular processes including protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic signaling[1][3]. Dysregulation or mutation of V-ATPase components, including ATP6V1D, is implicated in cancer, neurodegeneration, and lysosomal storage diseases[3][4][8]. Existing research tools and experimental drugs target the entire complex rather than individual subunits, and direct roles or drug interactions for subunit D remain largely unrefined in current literature[4].

Other names

ATPase H+ transporting V1 subunit DVATDV-ATPase subunit DATP6MVMA8Vacuolar ATPase subunit DATPase, H+ transporting, lysosomal (vacuolar proton pump)ATPase, H+ transporting, lysosomal 34kDa, V1 subunit DV-ATPase 28 kDa accessory proteinVacuolar proton pump subunit DH(+)-transporting two-sector ATPase, subunit MVacuolar proton pump delta polypeptideVacuolar proton-ATPase subunit DVacuolar ATP synthase subunit DVacuolar proton pump D subunitVacuolar H-ATPase subunit DV-ATPase D subunit

Inhibition of proton translocation and organelle acidification through V-ATPase blockage (by inhibitors such as bafilomycin A1 or concanamycin) Disruption of lysosomal and endosomal pH affects trafficking, protein maturation, and cellular signaling.