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Protein

ATP synthase subunit O, mitochondrial

Gene

Atp5o

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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

  1. drug binding Source: MGI
  2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
  3. steroid binding Source: Ensembl

GO - Biological processi

  1. ATP catabolic process Source: MGI
  2. mitochondrial ATP synthesis coupled proton transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_245290. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit O, mitochondrial
Alternative name(s):
Oligomycin sensitivity conferral protein
Short name:
OSCP
Gene namesi
Name:Atp5o
Synonyms:D12Wsu28e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:106341. Atp5o.

Subcellular locationi

Mitochondrion By similarity. Mitochondrion inner membrane By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  3. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: Ensembl
  4. mitochondrion Source: MGI
  5. myelin sheath Source: UniProtKB
  6. nucleus Source: MGI
  7. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionBy similarityAdd
BLAST
Chaini24 – 213190ATP synthase subunit O, mitochondrialPRO_0000002647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-acetyllysine1 Publication
Modified residuei60 – 601N6-acetyllysine1 Publication
Modified residuei70 – 701N6-acetyllysine1 Publication
Modified residuei73 – 731N6-acetyllysine1 Publication
Modified residuei90 – 901N6-succinyllysine1 Publication
Modified residuei100 – 1001N6-acetyllysine; alternate1 Publication
Modified residuei100 – 1001N6-succinyllysine; alternate1 Publication
Modified residuei158 – 1581N6-acetyllysine; alternate1 Publication
Modified residuei158 – 1581N6-succinyllysine; alternate1 Publication
Modified residuei162 – 1621N6-acetyllysine; alternate1 Publication
Modified residuei162 – 1621N6-succinyllysine; alternate1 Publication
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei176 – 1761N6-acetyllysine1 Publication
Modified residuei192 – 1921N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-succinyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-70 and Lys-158 is observed in liver mitochondria from fasted mice but not from fed mice.
Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9DB20.
PaxDbiQ9DB20.
PRIDEiQ9DB20.

PTM databases

PhosphoSiteiQ9DB20.

Expressioni

Gene expression databases

BgeeiQ9DB20.
ExpressionAtlasiQ9DB20. baseline and differential.
GenevestigatoriQ9DB20.

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. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 (By similarity).By similarity

Protein-protein interaction databases

BioGridi205752. 2 interactions.
IntActiQ9DB20. 6 interactions.
MINTiMINT-1840730.

Structurei

3D structure databases

ProteinModelPortaliQ9DB20.
SMRiQ9DB20. Positions 24-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase delta chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0712.
GeneTreeiENSGT00390000015060.
HOGENOMiHOG000075825.
HOVERGENiHBG004309.
InParanoidiQ9DB20.
KOiK02137.
OMAiKPPVQVF.
PhylomeDBiQ9DB20.
TreeFamiTF106241.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact.
InterProiIPR020781. ATPase_OSCP/d_CS.
IPR026015. 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.
PROSITEiPS00389. ATPASE_DELTA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DB20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPAASGLS RQVRSFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS
60 70 80 90 100
KEKKLDQVEK ELLRVGQLLK DPKVSLAVLN PYIKRTVKVK SLNDITKREK
110 120 130 140 150
FSPLTANLMN LLAENGRLGN TQGIISAFST IMSVHRGEVP CTVTTASPLD
160 170 180 190 200
DAVLSELKTV LKSFLSPNQI LKLEIKTDPS IMGGMIVRIG EKYVDMSAKS
210
KIQKLSKAMR EML
Length:213
Mass (Da):23,364
Last modified:June 1, 2001 - v1
Checksum:i1B0DAD4CCFCCB086
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005309 mRNA. Translation: BAB23945.1.
BC012241 mRNA. Translation: AAH12241.1.
CCDSiCCDS28331.1.
RefSeqiNP_613063.1. NM_138597.2.
XP_006543820.1. XM_006543757.1.
UniGeneiMm.41.

Genome annotation databases

EnsembliENSMUST00000023677; ENSMUSP00000023677; ENSMUSG00000022956.
GeneIDi102641678.
28080.
KEGGimmu:102641678.
mmu:28080.
UCSCiuc007zys.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005309 mRNA. Translation: BAB23945.1.
BC012241 mRNA. Translation: AAH12241.1.
CCDSiCCDS28331.1.
RefSeqiNP_613063.1. NM_138597.2.
XP_006543820.1. XM_006543757.1.
UniGeneiMm.41.

3D structure databases

ProteinModelPortaliQ9DB20.
SMRiQ9DB20. Positions 24-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205752. 2 interactions.
IntActiQ9DB20. 6 interactions.
MINTiMINT-1840730.

PTM databases

PhosphoSiteiQ9DB20.

Proteomic databases

MaxQBiQ9DB20.
PaxDbiQ9DB20.
PRIDEiQ9DB20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023677; ENSMUSP00000023677; ENSMUSG00000022956.
GeneIDi102641678.
28080.
KEGGimmu:102641678.
mmu:28080.
UCSCiuc007zys.1. mouse.

Organism-specific databases

CTDi539.
MGIiMGI:106341. Atp5o.

Phylogenomic databases

eggNOGiCOG0712.
GeneTreeiENSGT00390000015060.
HOGENOMiHOG000075825.
HOVERGENiHBG004309.
InParanoidiQ9DB20.
KOiK02137.
OMAiKPPVQVF.
PhylomeDBiQ9DB20.
TreeFamiTF106241.

Enzyme and pathway databases

ReactomeiREACT_245290. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

NextBioi306620.
PROiQ9DB20.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB20.
ExpressionAtlasiQ9DB20. baseline and differential.
GenevestigatoriQ9DB20.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact.
InterProiIPR020781. ATPase_OSCP/d_CS.
IPR026015. 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.
PROSITEiPS00389. ATPASE_DELTA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 27-51; 65-84; 99-158; 163-172 AND 177-188, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-100; LYS-158; LYS-162 AND LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-60; LYS-70; LYS-73; LYS-100; LYS-158; LYS-162; LYS-172 AND LYS-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATPO_MOUSE
AccessioniPrimary (citable) accession number: Q9DB20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.