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== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/VPP1_YEAST VPP1_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: | + | [https://www.uniprot.org/uniprot/VPP1_YEAST VPP1_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:11278748, PubMed:1491220, PubMed:8798414). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:11278748, PubMed:1491220). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:11278748, PubMed:8798414).<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</ref> |
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Current revision
Solution structure of TM7 bound to DPC micelles
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