PMA1/YGL008C Summary Help

Standard Name PMA1 1, 2
Systematic Name YGL008C
Alias KTI10 3
Feature Type ORF, Verified
Description Plasma membrane H+-ATPase; pumps protons out of the cell; major regulator of cytoplasmic pH and plasma membrane potential; P2-type ATPase; Hsp30p plays a role in Pma1p regulation; interactions with Std1p appear to propagate [GAR+] (4, 5, 6, 7, 8 and see Summary Paragraph)
Name Description Plasma Membrane ATPase
Chromosomal Location
ChrVII:482666 to 479910 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -2 cM
Gene Ontology Annotations All PMA1 GO evidence and references
  View Computational GO annotations for PMA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 16 genes
Classical genetics
Large-scale survey
reduction of function
338 total interaction(s) for 256 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 44
  • Affinity Capture-RNA: 11
  • Affinity Capture-Western: 13
  • Biochemical Activity: 2
  • Co-fractionation: 11
  • Co-localization: 3
  • Co-purification: 2
  • PCA: 2
  • Protein-RNA: 6

Genetic Interactions
  • Dosage Lethality: 2
  • Dosage Rescue: 1
  • Negative Genetic: 149
  • Phenotypic Suppression: 1
  • Positive Genetic: 62
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1
  • Synthetic Rescue: 27

Expression Summary
Length (a.a.) 918
Molecular Weight (Da) 99,618
Isoelectric Point (pI) 4.81
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:482666 to 479910 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -2 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2757 482666..479910 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 SGDIDS000002976

PMA1 is an essential gene that encodes the major plasma membrane H+-ATPase in S. cerevisiae (4). By hydrolyzing ATP, Pma1p pumps H+ ions out of the cell, which creates an electrochemical proton gradient that regulates proper cytoplasmic pH and drives the secondary import of nutrients across the plasma membrane (reviewed in 9 and 10).

Pma1p is an abundant 100 kDa protein with 10 membrane-embedded domains (reviewed in 9 and 10). Its abundance, combined with its function as a prominent housekeeping gene, has led to its use as a marker for stress, secretion, and plasma membrane biogenesis (11 and reviewed in 12).

Pma1p is highly regulated by glucose, both transcriptionally and postranslationally (13). The presence of glucose induces a 2- to 4-fold increase in PMA1 expression, mediated by the transcription factors Rap1p and Gcr1p (14, 15). Glucose also triggers a rapid 5- to 10-fold increase in ATPase catalytic activity via Ptk2p-mediated phosphorylation of a serine residue in the Pma1p C-terminus (13, 16, 17). In contrast, phosphorylation of Pma1p by serine/threonine kinase (Yck1p and Yck2p), in the presence of glucose, is correlated with decreased proton pump activity (18). Glucose addition induces a Pma1p conformational change that is correlated with enzyme activity; moreover, glucose disrupts complexes between acetylated tubulin (Tub1p, Tub2p, and Tub3p) and Pma1p that are known to inhibit H+-ATPase activity (19 and references contained therein, 20). Finally, PMA1 transcription may be regulated by the cell cycle as its promoter is also a binding site for the transcription factor Mcm1p (21).

Pma1p homologs have been identified in A. thaliana and other fungi such as C. albicans and S. pombe (22, 23, 24). Additionally, H+-ATPase homologs in pathogenic fungi are being studied as targets for antifungal reagents (25 and reviewed in 26).

Last updated: 2006-04-27 Contact SGD

References cited on this page View Complete Literature Guide for PMA1
1) Balzi, E.  (1989) Personal Communication, Mortimer Map Edition 10
2) McCusker, J.H.  (1987) Pleiotropic drug resistance mutations in Saccharomyces cerevisiae. Ph.D. Thesis
3) Butler AR, et al.  (1994) Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest induced by Kluyveromyces lactis toxin. Mol Cell Biol 14(9):6306-16
4) Serrano R, et al.  (1986) Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases. Nature 319(6055):689-93
5) Perlin DS, et al.  (1988) Membrane potential defect in hygromycin B-resistant pma1 mutants of Saccharomyces cerevisiae. J Biol Chem 263(34):18118-22
6) Serrano R  (1978) Characterization of the plasma membrane ATPase of Saccharomyces cerevisiae. Mol Cell Biochem 22(1):51-63
7) Meena RC, et al.  (2011) Regulation of Saccharomyces cerevisiae Plasma membrane H+-ATPase (Pma1) by Dextrose and Hsp30 during Exposure to Thermal Stress Indian J Microbiol 51(2):153-158
8) Crow ET and Li L  (2011) Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol 22(5):452-9
9) Ambesi A, et al.  (2000) Biogenesis and function of the yeast plasma-membrane H(+)-ATPase. J Exp Biol 203(Pt 1):155-60
10) Morsomme P, et al.  (2000) Mutagenic study of the structure, function and biogenesis of the yeast plasma membrane H(+)-ATPase. Biochim Biophys Acta 1469(3):133-57
11) Schmitt M, et al.  (2006) Use of PMA1 as a housekeeping biomarker for assessment of toxicant-induced stress in Saccharomyces cerevisiae. Appl Environ Microbiol 72(2):1515-22
12) Ferreira T, et al.  (2002) Quality control in the yeast secretory pathway: a misfolded PMA1 H+-ATPase reveals two checkpoints. J Biol Chem 277(23):21027-40
13) Serrano R  (1983) In vivo glucose activation of the yeast plasma membrane ATPase. FEBS Lett 156(1):11-4
14) Rao R, et al.  (1993) Transcriptional regulation by glucose of the yeast PMA1 gene encoding the plasma membrane H(+)-ATPase. Yeast 9(10):1075-84
15) Garcia-Arranz M, et al.  (1994) Transcriptional control of yeast plasma membrane H(+)-ATPase by glucose. Cloning and characterization of a new gene involved in this regulation. J Biol Chem 269(27):18076-82
16) Eraso P, et al.  (2006) Yeast protein kinase Ptk2 localizes at the plasma membrane and phosphorylates in vitro the C-terminal peptide of the H+-ATPase. Biochim Biophys Acta 1758(2):164-70
17) Goossens A, et al.  (2000) Regulation of yeast H(+)-ATPase by protein kinases belonging to a family dedicated to activation of plasma membrane transporters. Mol Cell Biol 20(20):7654-61
18) Estrada E, et al.  (1996) Phosphorylation of yeast plasma membrane H+-ATPase by casein kinase I. J Biol Chem 271(50):32064-72
19) Lecchi S, et al.  (2005) Conformational changes of yeast plasma membrane H(+)-ATPase during activation by glucose: role of threonine-912 in the carboxy-terminal tail. Biochemistry 44(50):16624-32
20) Campetelli AN, et al.  (2005) Activation of the plasma membrane H-ATPase of Saccharomyces cerevisiae by glucose is mediated by dissociation of the H(+)-ATPase-acetylated tubulin complex. FEBS J 272(22):5742-52
21) Kuo MH and Grayhack E  (1994) A library of yeast genomic MCM1 binding sites contains genes involved in cell cycle control, cell wall and membrane structure, and metabolism. Mol Cell Biol 14(1):348-59
22) Harper JF, et al.  (1989) Molecular cloning and sequence of cDNA encoding the plasma membrane proton pump (H+-ATPase) of Arabidopsis thaliana. Proc Natl Acad Sci U S A 86(4):1234-8
23) Monk BC, et al.  (1991) Cloning and characterization of the plasma membrane H(+)-ATPase from Candida albicans. J Bacteriol 173(21):6826-36
24) Ghislain M, et al.  (1987) Mutation of a conserved glycine residue modifies the vanadate sensitivity of the plasma membrane H+-ATPase from Schizosaccharomyces pombe. J Biol Chem 262(36):17549-55
25) Soteropoulos P, et al.  (2000) Molecular characterization of the plasma membrane H(+)-ATPase, an antifungal target in Cryptococcus neoformans. Antimicrob Agents Chemother 44(9):2349-55
26) Monk BC and Perlin DS  (1994) Fungal plasma membrane proton pumps as promising new antifungal targets. Crit Rev Microbiol 20(3):209-23