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VMA3 H(+)-transporting V0 sector ATPase subunit c [ Saccharomyces cerevisiae S288C ]

Gene ID: 856686, updated on 6-Jul-2026
Official Symbol
VMA3
Official Full Name
H(+)-transporting V0 sector ATPase subunit c
Primary source
SGD:S000000753
Locus tag
YEL027W
See related
AllianceGenome:SGD:S000000753; FungiDB:YEL027W; VEuPathDB:YEL027W
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
CLS7; CUP5; GEF2
Summary
Predicted to enable proton transmembrane transporter activity. Involved in several processes, including intracellular monoatomic cation homeostasis; protein targeting to vacuole; and vacuole organization. Located in membrane. Used to study epilepsy and intellectual disability. Human ortholog(s) of this gene implicated in early-onset epilepsy 3 and thyroid gland carcinoma. Orthologous to human ATP6V0C (ATPase H+ transporting V0 subunit c). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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Try the new Transcripts and proteins table
See VMA3 in Genome Data Viewer
Location:
chromosome: V
Exon count:
1
Sequence:
Chromosome: V; NC_001137.3 (100769..101251)

Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene tRNA-Met Neighboring gene RNA binding protein SNU13 Neighboring gene uncharacterized protein

Genomic Sequence:
NC_001137.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Functional properties of a hybrid vacuolar H(+)-ATPase in Saccharomyces cells expressing the Nephrops 16-kDa proteolipid. Harrison MA, et al. Eur J Biochem, 1994 Apr 1. PMID 8168500
  2. Analysis of intracellular pH in the yeast Saccharomyces cerevisiae under elevated hydrostatic pressure: a study in baro- (piezo-) physiology. Abe F, et al. Extremophiles, 1998 Aug. PMID 9783169
  3. Vacuolar acidification in Saccharomyces cerevisiae induced by elevated hydrostatic pressure is transient and is mediated by vacuolar H+-ATPase. Abe F, et al. Extremophiles, 1997 May. PMID 9680307
  4. Helical interactions and membrane disposition of the 16-kDa proteolipid subunit of the vacuolar H(+)-ATPase analyzed by cysteine replacement mutagenesis. Harrison MA, et al. J Biol Chem, 1999 Sep 3. PMID 10464277
  5. E5 transforming proteins of papillomaviruses do not disturb the activity of the vacuolar H(+)-ATPase. Ashby ADM, et al. J Gen Virol, 2001 Oct. PMID 11562529

See all (138) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Taken together, we have proposed a working model to describe how Vma3p protects cells against apoptosis through the regulation of HXK2 expression.
    Title: Vma3p protects cells from programmed cell death through the regulation of Hxk2p expression.
  2. These findings suggest a role for vacuolar proton translocation ATPase in the regulation of the cell wall stress response and the prevention of endogenous oxidative stress in response to ethanol.
    Title: Vacuolar H+-ATPase Protects Saccharomyces cerevisiae Cells against Ethanol-Induced Oxidative and Cell Wall Stresses.
  3. Peptides corresponding to 2nd & 4th transmembrane domains (TM2 & TM4) of proteolipid subunit c (Vma3p) & of putative 7th transmembrane domain (TM7) of subunit a (Vph1p) are predominantly, alpha-helical in membranes of dioleoyl phosphatidylcholine.
    Title: Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables proton transmembrane transporter activity IEA
Inferred from Electronic Annotation
more info
  
enables proton transmembrane transporter activity TAS
Traceable Author Statement
more info
 PubMed 
enables proton-transporting ATPase activity, rotational mechanism IC
Inferred by Curator
more info
 PubMed 
enables proton-transporting ATPase activity, rotational mechanism IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in Golgi lumen acidification NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in endocytosis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in endosomal lumen acidification NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in intracellular copper ion homeostasis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in intracellular iron ion homeostasis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein targeting to vacuole IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in proton transmembrane transport IC
Inferred by Curator
more info
 PubMed 
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 vacuolar acidification IC
Inferred by Curator
more info
 PubMed 
involved_in vacuolar acidification IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in vacuolar acidification NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in vacuole organization IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in Golgi membrane NAS
Non-traceable Author Statement
more info
 PubMed 
located_in fungal-type vacuole membrane NAS
Non-traceable Author Statement
more info
 PubMed 
is_active_in membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in membrane IDA
Inferred from Direct Assay
more info
 PubMed 
part_of proton-transporting V-type ATPase complex IPI
Inferred from Physical Interaction
more info
 PubMed 
part_of proton-transporting V-type ATPase, V0 domain IEA
Inferred from Electronic Annotation
more info
  
part_of proton-transporting two-sector ATPase complex, proton-transporting domain IEA
Inferred from Electronic Annotation
more info
  
located_in vacuolar membrane EXP
Inferred from Experiment
more info
 PubMed 
located_in vacuolar membrane IEA
Inferred from Electronic Annotation
more info
  
part_of vacuolar proton-transporting V-type ATPase complex IPI
Inferred from Physical Interaction
more info
 PubMed 
part_of vacuolar proton-transporting V-type ATPase, V0 domain IDA
Inferred from Direct Assay
more info
 PubMed 
part_of vacuolar proton-transporting V-type ATPase, V0 domain TAS
Traceable Author Statement
more info
 PubMed 
Preferred Names
H(+)-transporting V0 sector ATPase subunit c
NP_010887.3
  • Proteolipid subunit c of the V0 domain of vacuolar H(+)-ATPase; dicyclohexylcarbodiimide binding subunit; required for vacuolar acidification and important for copper and iron metal ion homeostasis

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Genome Annotation

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

Reference assembly

Genomic

  1. NC_001137.3 Reference assembly

    Range
    100769..101251
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001178842.3 → NP_010887.3  H(+)-transporting V0 sector ATPase subunit c

    See identical proteins and their annotated locations for NP_010887.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D3DLM1, P25515
    UniProtKB/TrEMBL
    B3LRY8
    Conserved Domains (2) summary
    TIGR01100
    Location:11 → 116
    V_ATP_synt_C; vacuolar ATP synthase 16 kDa proteolipid subunit
    cd18176
    Location:84 → 151
    ATP-synt_Vo_c_ATP6C_rpt2; V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P25515.1

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