P31412 · VATC_YEAST

Function

function

Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:10781598, PubMed:11777935, PubMed:1730668, PubMed:8416931).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:8416931).
Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (PubMed:15792803).
Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section (PubMed:15792803).

Miscellaneous

Present with 21114 molecules/cell in log phase SD medium.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentfungal-type vacuole membrane
Cellular ComponentGolgi membrane
Cellular Componentproton-transporting V-type ATPase complex
Cellular Componentvacuolar proton-transporting V-type ATPase complex
Cellular Componentvacuolar proton-transporting V-type ATPase, V1 domain
Molecular FunctionATP binding
Molecular Functionproton-transporting ATPase activity, rotational mechanism
Biological Processendosomal lumen acidification
Biological ProcessGolgi lumen acidification
Biological Processproton transmembrane transport
Biological Processvacuolar acidification

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 3.A.2.2.3the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

Names & Taxonomy

Protein names

  • Recommended name
    V-type proton ATPase subunit C
  • Short names
    V-ATPase subunit C
  • Alternative names
    • V-ATPase 42 kDa subunit
    • Vacuolar proton pump subunit C

Gene names

    • Name
      VMA5
    • Synonyms
      VAT3, VATC
    • ORF names
      YKL410
    • Ordered locus names
      YKL080W

Organism names

Accessions

  • Primary accession
    P31412
  • Secondary accessions
    • D6VXK7

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis255Is rapidly degraded and disrupts stable ATPase assembly.

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00002093582-392V-type proton ATPase subunit C

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1) (PubMed:25971514).
Interacts directly with VMA4 (PubMed:15751969).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P31412VMA6 P323665EBI-20260, EBI-20201
View interactors in UniProtKB
View CPX-1192 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the V-ATPase C subunit family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    392
  • Mass (Da)
    44,189
  • Last updated
    2007-01-23 v4
  • Checksum
    0CD1B814046C377E
MATALYTANDFILISLPQNAQPVTAPGSKTDSWFNETLIGGRAFVSDFKIPEFKIGSLDTLIVESEELSKVDNQIGASIGKIIEILQGLNETSTNAYRTLPINNMPVPEYLENFQWQTRKFKLDKSIKDLITLISNESSQLDADVRATYANYNSAKTNLAAAERKKTGDLSVRSLHDIVKPEDFVLNSEHLTTVLVAVPKSLKSDFEKSYETLSKNVVPASASVIAEDAEYVLFNVHLFKKNVQEFTTAAREKKFIPREFNYSEELIDQLKKEHDSAASLEQSLRVQLVRLAKTAYVDVFINWFHIKALRVYVESVLRYGLPPHFNIKIIAVPPKNLSKCKSELIDAFGFLGGNAFMKDKKGKINKQDTSLHQYASLVDTEYEPFVMYIINL

Sequence caution

The sequence AAA34440.1 differs from that shown. Reason: Frameshift

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M77143
EMBL· GenBank· DDBJ
AAA34440.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift
X75560
EMBL· GenBank· DDBJ
CAA53237.1
EMBL· GenBank· DDBJ
Genomic DNA
Z28080
EMBL· GenBank· DDBJ
CAA81917.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006944
EMBL· GenBank· DDBJ
DAA09077.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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