Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP synthase subunit O, mitochondrial

Gene

ATPsynO

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 F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit O, mitochondrial
Alternative name(s):
Oligomycin sensitivity conferral protein
Short name:
OSCP
Gene namesi
Name:ATPsynOImported
Synonyms:OscpImported
ORF Names:CG4307Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0016691. ATPsynO.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
  • mitochondrial proton-transporting ATP synthase, central stalk Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 209ATP synthase subunit O, mitochondrialPRO_0000002650
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiQ24439.
PRIDEiQ24439.

Expressioni

Gene expression databases

BgeeiQ24439.
ExpressionAtlasiQ24439. differential.
GenevisibleiQ24439. 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

BioGridi66909. 30 interactions.
DIPiDIP-23606N.
IntActiQ24439. 6 interactions.
MINTiMINT-1023748.
STRINGi7227.FBpp0082522.

Structurei

3D structure databases

ProteinModelPortaliQ24439.
SMRiQ24439. Positions 23-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase delta chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1662. Eukaryota.
COG0712. LUCA.
GeneTreeiENSGT00390000015060.
InParanoidiQ24439.
KOiK02137.
OMAiMNPHVKR.
OrthoDBiEOG7DZ8M3.
PhylomeDBiQ24439.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact.
InterProiIPR026015. ATPase_OSCP/delta_N.
IPR000711. ATPase_OSCP/dsu.
[Graphical view]
PANTHERiPTHR11910. PTHR11910. 1 hit.
PfamiPF00213. OSCP. 1 hit.
[Graphical view]
PRINTSiPR00125. ATPASEDELTA.
SUPFAMiSSF47928. SSF47928. 1 hit.
TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q24439-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASINKLALL SRTLSSAAAQ ATVKPPVQVF GLEGRYATAL YSAASKLSQL
60 70 80 90 100
DQVEKDLTAL QATIRSDKKL REYVTSPIIN KKVMATALKE ASEKLRFAPA
110 120 130 140 150
TVNLLGLLAD NGRLKKLDTV INAYKTIMAA HRGEVVCEVV TAKPLDASQS
160 170 180 190 200
KQLEGALKSF LKGNESLKIT SRVDPSIIGG LIVSIGDKYV DMSIATKVKL

YTDVIQTAA
Length:209
Mass (Da):22,422
Last modified:December 1, 2000 - v2
Checksum:i50040CE844DFCAB2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911D → N in CAA67980 (PubMed:10071211).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99666 mRNA. Translation: CAA67980.1.
AE014297 Genomic DNA. Translation: AAF55156.1.
AY058261 mRNA. Translation: AAL13490.1.
RefSeqiNP_524358.2. NM_079634.3.
UniGeneiDm.4214.

Genome annotation databases

EnsemblMetazoaiFBtr0083063; FBpp0082522; FBgn0016691.
GeneIDi41845.
KEGGidme:Dmel_CG4307.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99666 mRNA. Translation: CAA67980.1.
AE014297 Genomic DNA. Translation: AAF55156.1.
AY058261 mRNA. Translation: AAL13490.1.
RefSeqiNP_524358.2. NM_079634.3.
UniGeneiDm.4214.

3D structure databases

ProteinModelPortaliQ24439.
SMRiQ24439. Positions 23-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66909. 30 interactions.
DIPiDIP-23606N.
IntActiQ24439. 6 interactions.
MINTiMINT-1023748.
STRINGi7227.FBpp0082522.

Proteomic databases

PaxDbiQ24439.
PRIDEiQ24439.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083063; FBpp0082522; FBgn0016691.
GeneIDi41845.
KEGGidme:Dmel_CG4307.

Organism-specific databases

CTDi41845.
FlyBaseiFBgn0016691. ATPsynO.

Phylogenomic databases

eggNOGiKOG1662. Eukaryota.
COG0712. LUCA.
GeneTreeiENSGT00390000015060.
InParanoidiQ24439.
KOiK02137.
OMAiMNPHVKR.
OrthoDBiEOG7DZ8M3.
PhylomeDBiQ24439.

Miscellaneous databases

GenomeRNAii41845.
PROiQ24439.

Gene expression databases

BgeeiQ24439.
ExpressionAtlasiQ24439. differential.
GenevisibleiQ24439. DM.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact.
InterProiIPR026015. ATPase_OSCP/delta_N.
IPR000711. ATPase_OSCP/dsu.
[Graphical view]
PANTHERiPTHR11910. PTHR11910. 1 hit.
PfamiPF00213. OSCP. 1 hit.
[Graphical view]
PRINTSiPR00125. ATPASEDELTA.
SUPFAMiSSF47928. SSF47928. 1 hit.
TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Ovary.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiATPO_DROME
AccessioniPrimary (citable) accession number: Q24439
Secondary accession number(s): Q9VFA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 131 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.