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Protein

ATP synthase subunit gamma, mitochondrial

Gene

ATPsyngamma

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled proton transport Source: FlyBase
  • phagocytosis Source: FlyBase
  • proton transport Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene namesi
Name:ATPsyngammaImported
Synonyms:ATPsyn-gammaImported
ORF Names:CG7610Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0020235. ATPsyngamma.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 297ATP synthase subunit gamma, mitochondrialPRO_0000002688
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiO01666.
PRIDEiO01666.

Expressioni

Gene expression databases

BgeeiO01666.
GenevisibleiO01666. DM.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi68371. 45 interactions.
DIPiDIP-23797N.
IntActiO01666. 1 interaction.
MINTiMINT-867633.
STRINGi7227.FBpp0084907.

Structurei

3D structure databases

ProteinModelPortaliO01666.
SMRiO01666. Positions 27-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase gamma chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1531. Eukaryota.
COG0224. LUCA.
GeneTreeiENSGT00390000006837.
InParanoidiO01666.
KOiK02136.
OMAiCGAIHSG.
OrthoDBiEOG7QK0D3.
PhylomeDBiO01666.

Family and domain databases

InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O01666-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMMQRTQLLL PLAMEATMLA QQQRGMATLK MISIRLKSVK NIQKITQSMK
60 70 80 90 100
MVSAAKYARA ERDLKAARPY GIGAQQFFEK TEIQPDEKAE PKKLLIAVTS
110 120 130 140 150
DRGLCGAVHT GVARLIRGEL AQDEANTKVF CVGDKSRAIL SRLYGKNILM
160 170 180 190 200
VANEVGRLPP TFLDASKIAN EVLQTGYDYT EGKIVYNRFK SVVSYQCSTL
210 220 230 240 250
PIFSGSTVEK SEKLAVYDSL DSDVVKSYLE FSLASLIFYT MKEGACSEQS
260 270 280 290
SRMTAMDNAS KNAGEMIDKL TLTFNRTRQA VITRELIEII SGAAALT
Length:297
Mass (Da):32,871
Last modified:December 1, 2000 - v2
Checksum:iB648B8D614E01FCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAN14185.1.
AE014297 Genomic DNA. Translation: AAN14186.1.
AY113454 mRNA. Translation: AAM29459.1.
Y12701 mRNA. Translation: CAA73233.1.
RefSeqiNP_524550.1. NM_079826.4.
NP_733304.1. NM_170425.4.
NP_733305.1. NM_170426.3.
UniGeneiDm.8032.

Genome annotation databases

EnsemblMetazoaiFBtr0085539; FBpp0084905; FBgn0020235.
FBtr0085540; FBpp0084906; FBgn0020235.
FBtr0085541; FBpp0084907; FBgn0020235.
GeneIDi43507.
KEGGidme:Dmel_CG7610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAN14185.1.
AE014297 Genomic DNA. Translation: AAN14186.1.
AY113454 mRNA. Translation: AAM29459.1.
Y12701 mRNA. Translation: CAA73233.1.
RefSeqiNP_524550.1. NM_079826.4.
NP_733304.1. NM_170425.4.
NP_733305.1. NM_170426.3.
UniGeneiDm.8032.

3D structure databases

ProteinModelPortaliO01666.
SMRiO01666. Positions 27-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68371. 45 interactions.
DIPiDIP-23797N.
IntActiO01666. 1 interaction.
MINTiMINT-867633.
STRINGi7227.FBpp0084907.

Proteomic databases

PaxDbiO01666.
PRIDEiO01666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085539; FBpp0084905; FBgn0020235.
FBtr0085540; FBpp0084906; FBgn0020235.
FBtr0085541; FBpp0084907; FBgn0020235.
GeneIDi43507.
KEGGidme:Dmel_CG7610.

Organism-specific databases

CTDi43507.
FlyBaseiFBgn0020235. ATPsyngamma.

Phylogenomic databases

eggNOGiKOG1531. Eukaryota.
COG0224. LUCA.
GeneTreeiENSGT00390000006837.
InParanoidiO01666.
KOiK02136.
OMAiCGAIHSG.
OrthoDBiEOG7QK0D3.
PhylomeDBiO01666.

Miscellaneous databases

ChiTaRSiATPsyn-gamma. fly.
GenomeRNAii43507.
PROiO01666.

Gene expression databases

BgeeiO01666.
GenevisibleiO01666. DM.

Family and domain databases

InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Identification of nuclear genes encoding mitochondrial proteins: isolation of a collection of D. melanogaster cDNAs homologous to sequences in the Human Gene Index database."
    Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R., Barsanti P.
    Mol. Gen. Genet. 261:64-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
    Tissue: Ovary.

Entry informationi

Entry nameiATPG_DROME
AccessioniPrimary (citable) accession number: O01666
Secondary accession number(s): A4V3L6, Q0KHZ7, Q9VAH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: July 6, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.