2rpw

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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rpw RCSB], [http://www.ebi.ac.uk/pdbsum/2rpw PDBsum]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rpw RCSB], [http://www.ebi.ac.uk/pdbsum/2rpw PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/VPH1_YEAST VPH1_YEAST]] Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. 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. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 13:30, 25 December 2014

Structure of a peptide derived from H+-V-ATPase subunit a

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