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Q91VR2

- ATPG_MOUSE

UniProt

Q91VR2 - ATPG_MOUSE

Protein

ATP synthase subunit gamma, mitochondrial

Gene

Atp5c1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Dec 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 F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

    GO - Molecular functioni

    1. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

    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 gamma, mitochondrial
    Alternative name(s):
    F-ATPase gamma subunit
    Gene namesi
    Name:Atp5c1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1261437. Atp5c1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    3. mitochondrion Source: MGI
    4. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW

    Keywords - Cellular componenti

    CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2525MitochondrionAdd
    BLAST
    Chaini26 – 298273ATP synthase subunit gamma, mitochondrialPRO_0000002686Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391N6-acetyllysine1 Publication
    Modified residuei49 – 491N6-succinyllysine1 Publication
    Modified residuei55 – 551N6-acetyllysineBy similarity
    Modified residuei115 – 1151N6-acetyllysine; alternate1 Publication
    Modified residuei115 – 1151N6-succinyllysine; alternate1 Publication
    Modified residuei138 – 1381N6-acetyllysine1 Publication
    Modified residuei154 – 1541N6-acetyllysine; alternate1 Publication
    Modified residuei154 – 1541N6-succinyllysine; alternate1 Publication
    Modified residuei197 – 1971N6-acetyllysineBy similarity
    Modified residuei270 – 2701N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ91VR2.
    PaxDbiQ91VR2.
    PRIDEiQ91VR2.

    2D gel databases

    UCD-2DPAGEQ91VR2.

    PTM databases

    PhosphoSiteiQ91VR2.

    Expressioni

    Gene expression databases

    BgeeiQ91VR2.
    GenevestigatoriQ91VR2.

    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

    BioGridi198255. 6 interactions.
    IntActiQ91VR2. 7 interactions.
    MINTiMINT-1842256.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91VR2.
    SMRiQ91VR2. Positions 26-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase gamma chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0224.
    GeneTreeiENSGT00390000006837.
    HOGENOMiHOG000215911.
    HOVERGENiHBG000933.
    InParanoidiQ91VR2.
    KOiK02136.
    OMAiCKEVGRK.
    PhylomeDBiQ91VR2.
    TreeFamiTF105765.

    Family and domain databases

    InterProiIPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view]
    PANTHERiPTHR11693. PTHR11693. 1 hit.
    PfamiPF00231. ATP-synt. 1 hit.
    [Graphical view]
    PRINTSiPR00126. ATPASEGAMMA.
    SUPFAMiSSF52943. SSF52943. 1 hit.
    TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q91VR2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSRASVVGL SACAVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM    50
    VAAAKYARAE RELKPARVYG TGSLALYEKA DIKAPEDKKK HLIIGVSSDR 100
    GLCGAIHSSV AKQMKNEVAA LTAAGKEVMI VGVGEKIKGI LYRTHSDQFL 150
    VSFKDVGRKP PTFGDASVIA LELLNSGYEF DEGSIIFNQF KSVISYKTEE 200
    KPIFSLNTIA TAETMSIYDD IDADVLQNYQ EYNLANLIYY SLKESTTSEQ 250
    SARMTAMDNA SKNASDMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD 298
    Length:298
    Mass (Da):32,886
    Last modified:December 1, 2001 - v1
    Checksum:i9BD63134AEFF3ABA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC010700 mRNA. Translation: AAH10700.1.
    CCDSiCCDS38045.1.
    RefSeqiNP_065640.2. NM_020615.4.
    UniGeneiMm.12677.

    Genome annotation databases

    EnsembliENSMUST00000114897; ENSMUSP00000110547; ENSMUSG00000025781.
    GeneIDi11949.
    KEGGimmu:11949.
    UCSCiuc008ihm.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC010700 mRNA. Translation: AAH10700.1 .
    CCDSi CCDS38045.1.
    RefSeqi NP_065640.2. NM_020615.4.
    UniGenei Mm.12677.

    3D structure databases

    ProteinModelPortali Q91VR2.
    SMRi Q91VR2. Positions 26-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198255. 6 interactions.
    IntActi Q91VR2. 7 interactions.
    MINTi MINT-1842256.

    PTM databases

    PhosphoSitei Q91VR2.

    2D gel databases

    UCD-2DPAGE Q91VR2.

    Proteomic databases

    MaxQBi Q91VR2.
    PaxDbi Q91VR2.
    PRIDEi Q91VR2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000114897 ; ENSMUSP00000110547 ; ENSMUSG00000025781 .
    GeneIDi 11949.
    KEGGi mmu:11949.
    UCSCi uc008ihm.3. mouse.

    Organism-specific databases

    CTDi 509.
    MGIi MGI:1261437. Atp5c1.

    Phylogenomic databases

    eggNOGi COG0224.
    GeneTreei ENSGT00390000006837.
    HOGENOMi HOG000215911.
    HOVERGENi HBG000933.
    InParanoidi Q91VR2.
    KOi K02136.
    OMAi CKEVGRK.
    PhylomeDBi Q91VR2.
    TreeFami TF105765.

    Miscellaneous databases

    ChiTaRSi ATP5C1. mouse.
    NextBioi 280065.
    PROi Q91VR2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91VR2.
    Genevestigatori Q91VR2.

    Family and domain databases

    InterProi IPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view ]
    PANTHERi PTHR11693. PTHR11693. 1 hit.
    Pfami PF00231. ATP-synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00126. ATPASEGAMMA.
    SUPFAMi SSF52943. SSF52943. 1 hit.
    TIGRFAMsi TIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEi PS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 68-79; 91-136; 144-154; 263-277 AND 286-298, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    3. "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-49; LYS-115; LYS-154 AND LYS-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "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-39; LYS-115; LYS-138 AND LYS-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiATPG_MOUSE
    AccessioniPrimary (citable) accession number: Q91VR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 112 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