PMC1/YGL006W Summary Help

Standard Name PMC1 1
Systematic Name YGL006W
Feature Type ORF, Verified
Description Vacuolar Ca2+ ATPase involved in depleting cytosol of Ca2+ ions; prevents growth inhibition by activation of calcineurin in the presence of elevated concentrations of calcium; similar to mammalian PMCA1a (1, 2 and see Summary Paragraph)
Name Description Plasma Membrane Calcium 1, 3
Chromosomal Location
ChrVII:485921 to 489442 | ORF Map | GBrowse
Gene Ontology Annotations All PMC1 GO evidence and references
  View Computational GO annotations for PMC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 10 genes
Classical genetics
Large-scale survey
73 total interaction(s) for 55 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 7
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • PCA: 30

Genetic Interactions
  • Dosage Lethality: 2
  • Dosage Rescue: 4
  • Negative Genetic: 9
  • Phenotypic Enhancement: 6
  • Synthetic Growth Defect: 6
  • Synthetic Lethality: 6

Expression Summary
Length (a.a.) 1,173
Molecular Weight (Da) 130,860
Isoelectric Point (pI) 7.33
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:485921 to 489442 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..3522 485921..489442 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) | TCDB | UniProtKB
Primary SGDIDS000002974

PMC1 encodes a Ca2+ ATPase that transports calcium from the cytoplasm into the vacuole and participates in calcium homeostasis. S. cerevisiae contains two Ca2+ ATPases: Pmc1p and Pmr1p(1). Pmr1p is the principal Ca2+ ATPase that is expressed under normal growth conditions and Pmc1p is induced in the absence of PMR1 or with calcium overload (2).

PMC1 gene is not essential for viability under normal growth conditions and disruption of PMC1 does not affect mating, sporulation or starvation. Deleting PMC1 results in a large reduction of nonexchangeable Ca2+ pool in the vacuole and in high cellular Ca2+ concentrations pmc1 mutants exhibits growth inhibition. Ca2+ sequestration in the vacuole can be restored by the inactivation of calcineurin complex, a Ca2+/calmodulin-dependent protein phosphatase sensitive to the immunosuppressive drug FK506. Simultaneous deletion of CNA1 and CMP2 encoding the catalytic subunits of calcineurin restores the growth of the pmc1 mutants. Disruption of CNB1, the regulatory subunit of calcineurin, also restores the growth of pmc1 mutants (1, 2). Calcineurin decreases Ca2+ tolerance of pmc1 mutants by inhibiting the function of VCX1, which encodes a vacuolar H+/Ca2+ exchanger, possibly at a post-translational level (4).

Transcription of PMC1 and PMR1 is increased upon calcineurin-dependent activation of the transcription factor Crz1p (5, 6). In high Ca2+ environments, the strong up-regulation of PMC1 is necessary for growth, however, when the Ca2+ concentrations subside, the excess Pmc1p activity is negatively regulated by Nyv1p, a vacuolar v-SNARE protein. Overexpression of Nyv1p does not decrease Pmc1p levels but decreases the specific ATP-dependent Ca2+ transport activity of Pmc1p in purified vacuoles by at least 2-fold. Nyv1p binds to Pmc1p and inhibits its Ca2+ transport activity in vivo and in vitro (7).

Pmc1p shares sequence similarity with mammalian PMCA1a, PMC1 in S. pombe and the Ca2+ ATPases of T. brucei and A. thaliana(1, 8, 9).

Last updated: 2006-11-03 Contact SGD

References cited on this page View Complete Literature Guide for PMC1
1) Cunningham KW and Fink GR  (1994) Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca2+ ATPases. J Cell Biol 124(3):351-63
2) Marchi V, et al.  (1999) Induction of vacuolar Ca2+-ATPase and H+/Ca2+ exchange activity in yeast mutants lacking Pmr1, the Golgi Ca2+-ATPase. FEBS Lett 454(3):181-6
3) Shull GE and Greeb J  (1988) Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+,K+- and other cation transport ATPases. J Biol Chem 263(18):8646-57
4) Cunningham KW and Fink GR  (1996) Calcineurin inhibits VCX1-dependent H+/Ca2+ exchange and induces Ca2+ ATPases in Saccharomyces cerevisiae. Mol Cell Biol 16(5):2226-37
5) Stathopoulos AM and Cyert MS  (1997) Calcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeast. Genes Dev 11(24):3432-44
6) Matheos DP, et al.  (1997) Tcn1p/Crz1p, a calcineurin-dependent transcription factor that differentially regulates gene expression in Saccharomyces cerevisiae. Genes Dev 11(24):3445-58
7) Takita Y, et al.  (2001) Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p. J Biol Chem 276(9):6200-6
8) Luo S, et al.  (2004) Trypanosoma brucei plasma membrane-type Ca(2+)-ATPase 1 (TbPMC1) and 2 (TbPMC2) genes encode functional Ca(2+)-ATPases localized to the acidocalcisomes and plasma membrane, and essential for Ca(2+) homeostasis and growth. J Biol Chem 279(14):14427-39
9) Geisler M, et al.  (2000) The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Plant Physiol 124(4):1814-27