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Q9DB20

- ATPO_MOUSE

UniProt

Q9DB20 - ATPO_MOUSE

Protein

ATP synthase subunit O, mitochondrial

Gene

Atp5o

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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. 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

    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

    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

    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.1 Publication
    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

    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.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.
    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

    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: October 1, 2014
    This is version 105 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