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P97450

- ATP5J_MOUSE

UniProt

P97450 - ATP5J_MOUSE

Protein

ATP synthase-coupling factor 6, mitochondrial

Gene

Atp5j

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.

    GO - Molecular functioni

    1. ATPase activity Source: Ensembl
    2. hydrogen ion transmembrane transporter activity Source: InterPro

    GO - Biological processi

    1. ATP synthesis coupled proton transport Source: InterPro

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase-coupling factor 6, mitochondrial
    Short name:
    ATPase subunit F6
    Gene namesi
    Name:Atp5j
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:107777. Atp5j.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    3. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: InterPro
    4. mitochondrion Source: MGI

    Keywords - Cellular componenti

    CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3232MitochondrionBy similarityAdd
    BLAST
    Chaini33 – 10876ATP synthase-coupling factor 6, mitochondrialPRO_0000002529Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411N6-acetyllysine1 Publication
    Modified residuei46 – 461N6-acetyllysine1 Publication
    Modified residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei84 – 841N6-acetyllysine; alternate1 Publication
    Modified residuei84 – 841N6-succinyllysine; alternate1 Publication
    Modified residuei94 – 941N6-acetyllysine; alternate1 Publication
    Modified residuei94 – 941N6-succinyllysine; alternate1 Publication
    Modified residuei99 – 991N6-acetyllysine; alternate1 Publication
    Modified residuei99 – 991N6-succinyllysine; alternate1 Publication
    Modified residuei105 – 1051N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP97450.
    PaxDbiP97450.
    PRIDEiP97450.

    2D gel databases

    SWISS-2DPAGEP97450.

    PTM databases

    PhosphoSiteiP97450.

    Expressioni

    Gene expression databases

    ArrayExpressiP97450.
    BgeeiP97450.
    GenevestigatoriP97450.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). 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

    IntActiP97450. 2 interactions.
    MINTiMINT-1843958.
    STRINGi10090.ENSMUSP00000023608.

    Structurei

    3D structure databases

    ProteinModelPortaliP97450.
    SMRiP97450. Positions 36-101.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG265662.
    GeneTreeiENSGT00390000008902.
    HOGENOMiHOG000261672.
    HOVERGENiHBG062261.
    InParanoidiP97450.
    KOiK02131.
    OMAiSESTWIN.
    OrthoDBiEOG754HRZ.
    PhylomeDBiP97450.
    TreeFamiTF318998.

    Family and domain databases

    InterProiIPR008387. ATPase_F0-cplx_f6su_mt.
    IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
    [Graphical view]
    PANTHERiPTHR12441. PTHR12441. 1 hit.
    PfamiPF05511. ATP-synt_F6. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
    SUPFAMiSSF111357. SSF111357. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P97450-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLQRIFRLS SVLRSAVSVH LKRNIGVTAV AFNKELDPVQ KLFVDKIREY    50
    KSKRQASGGP VDIGPEYQQD LDRELYKLKQ MYGKGEMDTF PTFKFDDPKF 100
    EVIDKPQS 108
    Length:108
    Mass (Da):12,496
    Last modified:May 1, 1997 - v1
    Checksum:iE2A2E63F7F23CEBF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77128 mRNA. Translation: AAB19213.1.
    AK078484 mRNA. Translation: BAC37301.1.
    BC010766 mRNA. Translation: AAH10766.1.
    CCDSiCCDS28283.1.
    PIRiPD0444.
    RefSeqiNP_058035.1. NM_016755.2.
    XP_006522938.1. XM_006522875.1.
    XP_006522939.1. XM_006522876.1.
    XP_006522940.1. XM_006522877.1.
    XP_006522941.1. XM_006522878.1.
    UniGeneiMm.353.

    Genome annotation databases

    EnsembliENSMUST00000023608; ENSMUSP00000023608; ENSMUSG00000022890.
    ENSMUST00000114191; ENSMUSP00000109829; ENSMUSG00000022890.
    ENSMUST00000114193; ENSMUSP00000109831; ENSMUSG00000022890.
    GeneIDi11957.
    KEGGimmu:11957.
    UCSCiuc007zth.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77128 mRNA. Translation: AAB19213.1 .
    AK078484 mRNA. Translation: BAC37301.1 .
    BC010766 mRNA. Translation: AAH10766.1 .
    CCDSi CCDS28283.1.
    PIRi PD0444.
    RefSeqi NP_058035.1. NM_016755.2.
    XP_006522938.1. XM_006522875.1.
    XP_006522939.1. XM_006522876.1.
    XP_006522940.1. XM_006522877.1.
    XP_006522941.1. XM_006522878.1.
    UniGenei Mm.353.

    3D structure databases

    ProteinModelPortali P97450.
    SMRi P97450. Positions 36-101.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97450. 2 interactions.
    MINTi MINT-1843958.
    STRINGi 10090.ENSMUSP00000023608.

    PTM databases

    PhosphoSitei P97450.

    2D gel databases

    SWISS-2DPAGE P97450.

    Proteomic databases

    MaxQBi P97450.
    PaxDbi P97450.
    PRIDEi P97450.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023608 ; ENSMUSP00000023608 ; ENSMUSG00000022890 .
    ENSMUST00000114191 ; ENSMUSP00000109829 ; ENSMUSG00000022890 .
    ENSMUST00000114193 ; ENSMUSP00000109831 ; ENSMUSG00000022890 .
    GeneIDi 11957.
    KEGGi mmu:11957.
    UCSCi uc007zth.1. mouse.

    Organism-specific databases

    CTDi 522.
    MGIi MGI:107777. Atp5j.

    Phylogenomic databases

    eggNOGi NOG265662.
    GeneTreei ENSGT00390000008902.
    HOGENOMi HOG000261672.
    HOVERGENi HBG062261.
    InParanoidi P97450.
    KOi K02131.
    OMAi SESTWIN.
    OrthoDBi EOG754HRZ.
    PhylomeDBi P97450.
    TreeFami TF318998.

    Miscellaneous databases

    ChiTaRSi ATP5J. mouse.
    NextBioi 280077.
    PROi P97450.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97450.
    Bgeei P97450.
    Genevestigatori P97450.

    Family and domain databases

    InterProi IPR008387. ATPase_F0-cplx_f6su_mt.
    IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
    [Graphical view ]
    PANTHERi PTHR12441. PTHR12441. 1 hit.
    Pfami PF05511. ATP-synt_F6. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
    SUPFAMi SSF111357. SSF111357. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Rocha D., Anderson E., Botcherby M., Jordan B., Carrier A.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
    2. "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.
    3. "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].
      Strain: FVB/N.
      Tissue: Colon.
    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-84; LYS-94 AND LYS-99, 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-41; LYS-46; LYS-79; LYS-84; LYS-94; LYS-99 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiATP5J_MOUSE
    AccessioniPrimary (citable) accession number: P97450
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 111 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, 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