Q22494 · VATH2_CAEEL

  • Protein
    Probable V-type proton ATPase subunit H 2
  • Gene
    vha-15
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

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 (By similarity).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity).

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 Componentvacuolar proton-transporting V-type ATPase, V1 domain
Molecular Functionproton-transporting ATPase activity, rotational mechanism

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 3.A.2.2.7the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

Names & Taxonomy

Protein names

  • Recommended name
    Probable V-type proton ATPase subunit H 2
  • Short names
    V-ATPase subunit H 2
  • Alternative names
    • Vacuolar proton pump subunit H 2

Gene names

    • Name
      vha-15
    • ORF names
      T14F9.1

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q22494

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001241991-470Probable V-type proton ATPase subunit H 2

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (By similarity).
The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity).
The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits vah-19/Ac45 and vah-20/PRR (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the V-ATPase H subunit family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    470
  • Mass (Da)
    54,213
  • Last updated
    1996-11-01 v1
  • MD5 Checksum
    E31B3180275A8F47AB1DDE2ADEF6ECD7
MAEVPHHNIPAVDMLNATSRLQLEAQELRNNKPNWGSYFRSQMIQEDDYNFITSFENAKSKEERDQVLAANNANGQAAKTMANLITQVAKDQNVRYVLTLFDDMLQEDKSRVELFHSAAARQKRTVWSQYLGILQRQDNFIVNQMSSIIAKLACFGTTRMEGQDLQYYFSFLKEQLKNSTTNDYMNTTARCLQMMLRHDEYRHEFVDSDGVQTLVTALNGKTNFQLQYQLIFAVWCLTFNADIARKAPSLGLIQALGDILSESTKEKVIRIILASFVNILSKVDEREVKREAALQMVQCKTLKTLELMDAKKYDDPDLEDDVKFLTEELTLSVHDLSSYDEYYSEVRSGRLQWSPVHKSEKFWRENASKFNDKQFEVVKILIKLLESSHDPLILCVASHDIGEYVRHYPRGKTVVEQYQGKAAVMRLLTAEDPNVRYHALLAVQKLMVHNWEYLGKQLDSDVQTDTVAVK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX284606
EMBL· GenBank· DDBJ
CCD68940.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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