PPA1/YHR026W Summary Help

PPA1 BASIC INFORMATION

Standard Name PPA1 (see Nomenclature conflict Note)
Systematic Name YHR026W
Alias VMA16
Feature Type ORF, Verified
Description Subunit c'' of the vacuolar ATPase, which functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain (1, 2, 3 and see Summary Paragraph)
Name Description Protein of Proton ATPase
GO Annotations All PPA1 GO evidence and references
    View Computational GO annotations for PPA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All PPA1 Phenotype details and references
Classical genetics
null
unspecified
Large-scale survey
null
Interactions PPA1 All interactions details and references
  View additional details at BioGRID
51 total interaction(s) for 49 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-Western: 2
  • Co-fractionation: 1
  • PCA: 31
  • Two-hybrid: 2
Genetic Interactions
  • Dosage Lethality: 2
  • Dosage Rescue: 2
  • Negative Genetic: 2
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 3
Sequence Information
ChrVIII:160837 to 161478 | ORF Map | GBrowse
Gbrowse
Genetic position: 27 cM
Last Update Coordinates: 2005-11-07 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..642 160837..161478 2005-11-07 1996-07-31
Post-translational Modifications PhosphoGRID | PhosphoPep Database
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000001068

PPA1 RESOURCES

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Expression Summary histogram

ADDITIONAL INFORMATION for PPA1

NOMENCLATURE CONFLICT NOTE

NameRelevanceDescription
IPP1Nomenclature conflictPPA1 has been used in the literature to refer to both IPP1/YBR011C, which encodes an inorganic pyrophosphatase and PPA1/YHR026W, which encodes a vacuolar ATPase.

SUMMARY PARAGRAPH for PPA1

PPA1 encodes the c'' subunit of the yeast V-ATPase V0 domain (4). 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 1, 5, 6 and 2.

The V0 c (Cup5p), c' (Tfp3p), and c'' subunits are highly hydrophobic integral membrane proteolipids, and have similar amino acid sequences; all three are required for V-ATPase activity (1, 2). 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 (7, 4). The remaining V-ATPase subunits do not assemble onto the vacuolar membrane in the absence of Ppa1p (4). Point mutations have identified amino acid residues in Ppa1p that are likely to be involved in proton transport(4).

V-ATPases have been identified in numerous eukaryotes; c'' homologs have been identified in Arabidopsis, mouse and human (1, 2, 8). PPA1/YHR026W and IPP1/YBR011C have been refered to as PPA1 in the literature.

Last updated: 2000-05-18

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for PPA1]

1) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
2) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808
3) 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
4) 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
5) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
6) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
7) 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
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