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Q9DB20

- ATPO_MOUSE

UniProt

Q9DB20 - ATPO_MOUSE

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Protein

ATP synthase subunit O, mitochondrial

Gene
Atp5o, D12Wsu28e
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. ATP synthesis coupled proton transport Source: InterPro
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: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 UniRule annotation

GO - Cellular componenti

  1. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  2. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: Ensembl
  3. mitochondrion 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 – 2323Mitochondrion By similarityAdd
BLAST
Chaini24 – 213190ATP synthase subunit O, mitochondrialUniRule annotationPRO_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-acetyllysine By 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.UniRule annotation
Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3 By similarity.UniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9DB20.
PaxDbiQ9DB20.
PRIDEiQ9DB20.

PTM databases

PhosphoSiteiQ9DB20.

Expressioni

Gene expression databases

ArrayExpressiQ9DB20.
BgeeiQ9DB20.
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.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9DB20.
SMRiQ9DB20. Positions 24-212.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0712.
GeneTreeiENSGT00390000015060.
HOGENOMiHOG000075825.
HOVERGENiHBG004309.
InParanoidiQ9DB20.
KOiK02137.
OMAiVICSVTT.
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

MAAPAASGLS RQVRSFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS    50
KEKKLDQVEK ELLRVGQLLK DPKVSLAVLN PYIKRTVKVK SLNDITKREK 100
FSPLTANLMN LLAENGRLGN TQGIISAFST IMSVHRGEVP CTVTTASPLD 150
DAVLSELKTV LKSFLSPNQI LKLEIKTDPS IMGGMIVRIG EKYVDMSAKS 200
KIQKLSKAMR EML 213
Length:213
Mass (Da):23,364
Last modified:June 1, 2001 - v1
Checksum:i1B0DAD4CCFCCB086
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK005309 mRNA. Translation: BAB23945.1 .
BC012241 mRNA. Translation: AAH12241.1 .
CCDSi CCDS28331.1.
RefSeqi NP_613063.1. NM_138597.2.
XP_006543820.1. XM_006543757.1.
UniGenei Mm.41.

3D structure databases

ProteinModelPortali Q9DB20.
SMRi Q9DB20. Positions 24-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205752. 2 interactions.
IntActi Q9DB20. 6 interactions.
MINTi MINT-1840730.

PTM databases

PhosphoSitei Q9DB20.

Proteomic databases

MaxQBi Q9DB20.
PaxDbi Q9DB20.
PRIDEi Q9DB20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023677 ; ENSMUSP00000023677 ; ENSMUSG00000022956 .
GeneIDi 102641678.
28080.
KEGGi mmu:102641678.
mmu:28080.
UCSCi uc007zys.1. mouse.

Organism-specific databases

CTDi 539.
MGIi MGI:106341. Atp5o.

Phylogenomic databases

eggNOGi COG0712.
GeneTreei ENSGT00390000015060.
HOGENOMi HOG000075825.
HOVERGENi HBG004309.
InParanoidi Q9DB20.
KOi K02137.
OMAi VICSVTT.
PhylomeDBi Q9DB20.
TreeFami TF106241.

Miscellaneous databases

ChiTaRSi ATP5O. mouse.
NextBioi 306620.
PROi Q9DB20.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9DB20.
Bgeei Q9DB20.
Genevestigatori Q9DB20.

Family and domain databases

Gene3Di 1.10.520.20. 1 hit.
HAMAPi MF_01416. ATP_synth_delta_bact.
InterProi IPR020781. ATPase_OSCP/d_CS.
IPR026015. ATPase_OSCP/delta_N.
IPR000711. ATPase_OSCP/dsu.
[Graphical view ]
PANTHERi PTHR11910. PTHR11910. 1 hit.
Pfami PF00213. OSCP. 1 hit.
[Graphical view ]
PRINTSi PR00125. ATPASEDELTA.
SUPFAMi SSF47928. SSF47928. 1 hit.
TIGRFAMsi TIGR01145. ATP_synt_delta. 1 hit.
PROSITEi PS00389. ATPASE_DELTA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 104 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