PMA1 H(+)-exporting P2-type ATPase PMA1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: PMA1
Gene description: H(+)-exporting P2-type ATPase PMA1
Primary source: SGD:S000002976
Locus tag: YGL008C
See related: AllianceGenome:SGD:S000002976
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: KTI10
Summary: Enables P-type proton-exporting transporter activity. Involved in positive regulation of TORC1 signaling; proteasome storage granule assembly; and proton transmembrane transport. Located in eisosome; membrane raft; and plasma membrane. Human ortholog(s) of this gene implicated in Hailey-Hailey disease. Orthologous to human ATP2C1 (ATPase secretory pathway Ca2+ transporting 1) and ATP2C2 (ATPase secretory pathway Ca2+ transporting 2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See PMA1 in Genome Data Viewer

Location:: chromosome: VII

Exon count:: 1

Sequence:: Chromosome: VII; NC_001139.9 (479910..482666, complement)

Chromosome VII - NC_001139.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Uncovering diffusive states of the yeast membrane protein, Pma1, and how labeling method can change diffusive behavior.
Title: Uncovering diffusive states of the yeast membrane protein, Pma1, and how labeling method can change diffusive behavior.
An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response.
Title: An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response.
A Genome-Wide Screen Reveals That Endocytic Genes Are Important for Pma1p Asymmetry during Cell Division in Saccharomyces cerevisiae.
Title: A Genome-Wide Screen Reveals That Endocytic Genes Are Important for Pma1p Asymmetry during Cell Division in Saccharomyces cerevisiae.
Point mutations in the different domains of the Saccharomyces cerevisiae plasma membrane PMA1 ATPase cause redistribution among fractions of inorganic polyphosphates.
Title: Point mutations in the different domains of the Saccharomyces cerevisiae plasma membrane PMA1 ATPase cause redistribution among fractions of inorganic polyphosphates.
Structure and activation mechanism of the hexameric plasma membrane H(+)-ATPase.
Title: Structure and activation mechanism of the hexameric plasma membrane H(+)-ATPase.
Results show that H(+) influx coupled to nutrient uptake stimulates Target of Rapamycin Complex 1 (TORC1) activity and that plasma membrane H(+)-ATPase (Pma1) is a key actor in this mechanism.
Title: The yeast H(+)-ATPase Pma1 promotes Rag/Gtr-dependent TORC1 activation in response to H(+)-coupled nutrient uptake.
Pma1 physically interacts with Exo1.
Title: Two novel effectors of trafficking and maturation of the yeast plasma membrane H(+) -ATPase.
These data confirm the important role of Asp739 and Arg811 residues for the biogenesis and function of the enzyme, suggesting their importance for defining H+ transport determinants but ruling out, however, the existence of a strong ionic bond (salt bridge) between these two residues and/or importance of such bridge for structure-function relationships in Pma1 H+-ATPase.
Title: Functioning of Yeast Pma1 H+-ATPase under Changing Charge: Role of Asp739 and Arg811 Residues.
These results indicate changes in the cell lipid composition. Western blot analysis showed the induction of Pma1 level by IM. RT-PCR revealed an increased PMA1 expression after IM treatment.
Title: Quaternary ammonium salt N-(dodecyloxycarboxymethyl)-N,N,N-trimethyl ammonium chloride induced alterations in Saccharomyces cerevisiae physiology.
Therefore, H(+) extrusion by Pma1 may be important for Ca(2+) influx through Cch1/Mid1. These results suggest that Pma1 interacts physically with Cch1/Mid1 Ca(2+) channels to enhance their activity via its H(+) -pumping activity
Title: Coupling of a voltage-gated Ca(2+) channel homologue with a plasma membrane H(+) -ATPase in yeast.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATPase-coupled monoatomic cation transmembrane transporter activity	IEA Inferred from Electronic Annotation more info
enables P-type ion transporter activity	IEA Inferred from Electronic Annotation more info
enables P-type proton-exporting transporter activity	IBA Inferred from Biological aspect of Ancestor more info
enables P-type proton-exporting transporter activity	IDA Inferred from Direct Assay more info	PubMed
enables P-type proton-exporting transporter activity	IEA Inferred from Electronic Annotation more info
enables inorganic cation transmembrane transporter activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in inorganic cation transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of TORC1 signaling	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proteasome storage granule assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proton export across plasma membrane	IEA Inferred from Electronic Annotation more info
involved_in proton transmembrane transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in proton transmembrane transport	IDA Inferred from Direct Assay more info	PubMed
involved_in proton transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in regulation of intracellular pH	IBA Inferred from Biological aspect of Ancestor more info
involved_in transmembrane transport	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytosol	HDA more info	PubMed
located_in eisosome	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in membrane raft	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed
located_in plasma membrane	HDA more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: H(+)-exporting P2-type ATPase PMA1

NP_011507.1

EC 7.1.2.1

Plasma membrane P2-type H+-ATPase; pumps protons out of cell; major regulator of cytoplasmic pH and plasma membrane potential; long-lived hexameric protein asymmetrically distributed at plasma membrane between mother cells and buds; accumulates at high levels in mother cells during aging, buds emerge with very low levels of Pma1p, newborn cells have low levels of Pma1p; Hsp30p plays a role in Pma1p regulation; interactions with Std1p appear to propagate [GAR+]

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001139.9 Reference assembly

Range

479910..482666 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180873.1 → NP_011507.1 TPA: H(+)-exporting P2-type ATPase PMA1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_011507.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VUC9, P05030

UniProtKB/TrEMBL

A0A8H4C2T0, A6ZUY5, B3LIM3, C7GK65, N1P3Q6

Conserved Domains (1) summary

cd02076
Location:87 → 874

P-type_ATPase_H; plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+)-ATPases