Structural highlights
Function
VPP2_YEAST Subunit 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:7514599, PubMed:11278748). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:11278748, PubMed:7514599). Is present only in Golgi- and endosome-residing V-ATPase complexes; enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform and do not dissociate V1 and V0 in response to glucose depletion (PubMed:11278748, PubMed:7514599).[1] [2]
See Also
References
- ↑ Kawasaki-Nishi S, Nishi T, Forgac M. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J Biol Chem. 2001 May 25;276(21):17941-8. Epub 2001 Mar 2. PMID:11278748 doi:http://dx.doi.org/10.1074/jbc.M010790200
- ↑ Manolson MF, Wu B, Proteau D, Taillon BE, Roberts BT, Hoyt MA, Jones EW. STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p. J Biol Chem. 1994 May 13;269(19):14064-74. PMID:7514599
