VMA16/YHR026W Summary Help

Standard Name VMA16 1
Systematic Name YHR026W
Alias PPA1 2
Feature Type ORF, Verified
Description Subunit c'' of the vacuolar ATPase; v-ATPase functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain (3, 4, 5 and see Summary Paragraph)
Name Description Vacuolar Membrane Atpase
Chromosomal Location
ChrVIII:160844 to 161485 | ORF Map | GBrowse
Genetic position: 27 cM
Gene Ontology Annotations All VMA16 GO evidence and references
  View Computational GO annotations for VMA16
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Classical genetics
Large-scale survey
58 total interaction(s) for 54 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 2
  • Co-fractionation: 1
  • PCA: 32
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Lethality: 3
  • Dosage Rescue: 2
  • Negative Genetic: 2
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 6

Expression Summary
Length (a.a.) 213
Molecular Weight (Da) 22,595
Isoelectric Point (pI) 8.35
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVIII:160844 to 161485 | ORF Map | GBrowse
Genetic position: 27 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..642 160844..161485 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001068

VMA16 encodes the c'' subunit of the yeast V-ATPase V0 domain (1). Vacuolar (H )-ATPases (V-ATPases) are ATP-dependent proton pumps that acidify intracellular vacuolar compartments. Vacuolar acidification is important for many cellular processes, including endocytosis, targeting of newly synthesized lysosomal enzymes, and other molecular targeting processes. The V-ATPase consists of two separable domains. The V1 domain has eight known subunits, is peripherally associated with the vacuolar membrane, and catalyzes ATP hydrolysis. The V0 domain is an integral membrane structure of five subunits, and transports protons across the membrane. The structure, function, and assembly of V-ATPases are reviewed in references 3, 6, 7 and 4.

The V0 c (Vma3p), c' (Vma11p), and c'' subunits are highly hydrophobic integral membrane proteolipids, and have similar amino acid sequences; all three are required for V-ATPase activity (3, 4). The ppa1 null mutant is inviable in some strain backgrounds; in other strains it is viable but lacks vacuolar (H )-ATPase activity, and is defective in vacuolar acidification (2, 1). The remaining V-ATPase subunits do not assemble onto the vacuolar membrane in the absence of Vma16p (1). Point mutations have identified amino acid residues in Vma16p that are likely to be involved in proton transport(1).

V-ATPases have been identified in numerous eukaryotes; c'' homologs have been identified in Arabidopsis, mouse and human (3, 4, 8). VMA16/YHR026W and IPP1/YBR011C have been refered to as PPA1 in the literature.

Last updated: 2000-05-18 Contact SGD

References cited on this page View Complete Literature Guide for VMA16
1) Hirata R, et al.  (1997) VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase. J Biol Chem 272(8):4795-803
2) Apperson M, et al.  (1990) A yeast protein, homologous to the proteolipid of the chromaffin granule proton-ATPase, is important for cell growth. Biochem Biophys Res Commun 168(2):574-9
3) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
4) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808
5) Nishi T, et al.  (2003) The first putative transmembrane segment of subunit c" (Vma16p) of the yeast V-ATPase is not necessary for function. J Biol Chem 278(8):5821-7
6) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
7) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
8) Nishigori H, et al.  (1998) Identification and characterization of the gene encoding a second proteolipid subunit of human vacuolar H(+)-ATPase (ATP6F). Genomics 50(2):222-8