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M9NWJ9 · M9NWJ9_DROME

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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.

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 Componentproton-transporting ATP synthase complex, coupling factor F(o)
Molecular Functionproton transmembrane transporter activity
Biological Processproton motive force-driven ATP synthesis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    ATP synthase subunit a

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Strains
    • BDX8
    • BE19
    • BE5
    • BE8
    • EVO18
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    M9NWJ9

Organism-specific databases

Subcellular Location

Membrane
; Multi-pass membrane protein
Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane48-69Helical
Transmembrane76-96Helical
Transmembrane102-122Helical
Transmembrane134-153Helical

Keywords

Expression

Gene expression databases

Interaction

Subunit

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

Family & Domains

Sequence similarities

Belongs to the ATPase A chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    196
  • Mass (Da)
    21,980
  • Last updated
    2013-06-26 v1
  • MD5 Checksum
    BD44631D8D9248AF6C18082689E97D5B
TFLGLLMIPSIYWLMPSRYNIMWNSILLTLHKEFKTLLGPSGHNGSTFIFISLFSLILFNNFMGLFPYIFTSTSHLTLTLSLALPLWLCFMLYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYILVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLY

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue196

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JX467081
EMBL· GenBank· DDBJ
AFQ23283.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467083
EMBL· GenBank· DDBJ
AFQ23285.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467084
EMBL· GenBank· DDBJ
AFQ23286.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467085
EMBL· GenBank· DDBJ
AFQ23287.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467086
EMBL· GenBank· DDBJ
AFQ23288.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467087
EMBL· GenBank· DDBJ
AFQ23289.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467088
EMBL· GenBank· DDBJ
AFQ23290.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467089
EMBL· GenBank· DDBJ
AFQ23291.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467090
EMBL· GenBank· DDBJ
AFQ23292.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467091
EMBL· GenBank· DDBJ
AFQ23293.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467092
EMBL· GenBank· DDBJ
AFQ23294.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467093
EMBL· GenBank· DDBJ
AFQ23295.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467094
EMBL· GenBank· DDBJ
AFQ23296.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467097
EMBL· GenBank· DDBJ
AFQ23299.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467098
EMBL· GenBank· DDBJ
AFQ23300.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467099
EMBL· GenBank· DDBJ
AFQ23301.1
EMBL· GenBank· DDBJ
Genomic DNA
JX467100
EMBL· GenBank· DDBJ
AFQ23302.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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