Q12349 · ATP14_YEAST

Function

function

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. Minor subunit located with subunit a in the membrane.

Miscellaneous

Present with 6140 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 Componentmitochondrial inner membrane
Cellular Componentmitochondrion
Cellular Componentproton-transporting ATP synthase complex, coupling factor F(o)
Biological Processcristae formation
Biological Processmitochondrial proton-transporting ATP synthase complex assembly
Biological Processproton motive force-driven ATP synthesis
Biological Processproton transmembrane transport

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP synthase subunit H, mitochondrial

Gene names

    • Name
      ATP14
    • ORF names
      L8003.20
    • Ordered locus names
      YLR295C

Organism names

Accessions

  • Primary accession
    Q12349
  • Secondary accessions
    • D6VYU0

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-32Mitochondrion
ChainPRO_000000252533-124ATP synthase subunit H, mitochondrial

Proteomic databases

PTM databases

Interaction

Subunit

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.

Complex viewer

View interactors in UniProtKB
View CPX-3281 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region89-124Disordered
Compositional bias102-116Acidic residues

Sequence similarities

Belongs to the ATPase h subunit family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    124
  • Mass (Da)
    14,128
  • Last updated
    1996-11-01 v1
  • Checksum
    7AE196CFB250ACBB
MFPIASRRILLNASVLPLRLCNRNFTTTRISYNVIQDLYLRELKDTKLAPSTLQDAEGNVKPWNPPQKPNLPELELQGPEALKAYTEQNVETAHVAKESEEGESEPIEEDWLVLDDAEETKESH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias102-116Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U51673
EMBL· GenBank· DDBJ
AAC49436.1
EMBL· GenBank· DDBJ
Genomic DNA
U17243
EMBL· GenBank· DDBJ
AAB67340.1
EMBL· GenBank· DDBJ
Genomic DNA
AY558215
EMBL· GenBank· DDBJ
AAS56541.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006945
EMBL· GenBank· DDBJ
DAA09606.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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