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Q06185

- ATP5I_MOUSE

UniProt

Q06185 - ATP5I_MOUSE

Protein

ATP synthase subunit e, mitochondrial

Gene

Atp5i

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. Minor subunit located with subunit a in the membrane.

    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

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit e, mitochondrial
    Short name:
    ATPase subunit e
    Gene namesi
    Name:Atp5i
    Synonyms:Atp5k, Lfm-1, Lfm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:106636. Atp5k.

    Subcellular locationi

    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

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 7170ATP synthase subunit e, mitochondrialPRO_0000071685Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ06185.
    PaxDbiQ06185.
    PRIDEiQ06185.

    PTM databases

    PhosphoSiteiQ06185.

    Expressioni

    Tissue specificityi

    Mammary gland, liver, kidney, heart, spleen, brain and lung.

    Gene expression databases

    ArrayExpressiQ06185.
    BgeeiQ06185.
    GenevestigatoriQ06185.

    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

    BioGridi198259. 1 interaction.
    IntActiQ06185. 1 interaction.
    MINTiMINT-1840518.
    STRINGi10090.ENSMUSP00000051222.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase e subunit family.Curated

    Phylogenomic databases

    eggNOGiNOG81326.
    GeneTreeiENSGT00390000005102.
    HOGENOMiHOG000231826.
    HOVERGENiHBG050613.
    InParanoidiQ06185.
    KOiK02129.
    OMAiSACYSAN.
    OrthoDBiEOG7MD4T1.
    PhylomeDBiQ06185.
    TreeFamiTF314719.

    Family and domain databases

    InterProiIPR008386. ATPase_F0-cplx_esu_mt.
    [Graphical view]
    PfamiPF05680. ATP-synt_E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q06185-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVPPVQVSPL IKFGRYSALI IGMAYGAKRY SYLKPRAEEE RRIAAEEKKR   50
    LDELKRIERE LAEAQDDSIL K 71
    Length:71
    Mass (Da):8,236
    Last modified:January 23, 2007 - v2
    Checksum:i0379C3E14C098F12
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131F → S in AAC52713. (PubMed:8702853)Curated
    Sequence conflicti48 – 481K → R in AAC52713. (PubMed:8702853)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S52977 mRNA. Translation: AAB24947.1.
    U59283 Genomic DNA. Translation: AAC52713.1.
    BC028438 mRNA. Translation: AAH28438.1.
    CCDSiCCDS39204.1.
    PIRiJC1412.
    RefSeqiNP_031533.2. NM_007507.2.
    UniGeneiMm.136093.

    Genome annotation databases

    EnsembliENSMUST00000049628; ENSMUSP00000051222; ENSMUSG00000050856.
    GeneIDi11958.
    KEGGimmu:11958.
    UCSCiuc008yoa.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S52977 mRNA. Translation: AAB24947.1 .
    U59283 Genomic DNA. Translation: AAC52713.1 .
    BC028438 mRNA. Translation: AAH28438.1 .
    CCDSi CCDS39204.1.
    PIRi JC1412.
    RefSeqi NP_031533.2. NM_007507.2.
    UniGenei Mm.136093.

    3D structure databases

    ProteinModelPortali Q06185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198259. 1 interaction.
    IntActi Q06185. 1 interaction.
    MINTi MINT-1840518.
    STRINGi 10090.ENSMUSP00000051222.

    PTM databases

    PhosphoSitei Q06185.

    Proteomic databases

    MaxQBi Q06185.
    PaxDbi Q06185.
    PRIDEi Q06185.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049628 ; ENSMUSP00000051222 ; ENSMUSG00000050856 .
    GeneIDi 11958.
    KEGGi mmu:11958.
    UCSCi uc008yoa.1. mouse.

    Organism-specific databases

    CTDi 11958.
    MGIi MGI:106636. Atp5k.

    Phylogenomic databases

    eggNOGi NOG81326.
    GeneTreei ENSGT00390000005102.
    HOGENOMi HOG000231826.
    HOVERGENi HBG050613.
    InParanoidi Q06185.
    KOi K02129.
    OMAi SACYSAN.
    OrthoDBi EOG7MD4T1.
    PhylomeDBi Q06185.
    TreeFami TF314719.

    Miscellaneous databases

    NextBioi 280081.
    PROi Q06185.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06185.
    Bgeei Q06185.
    Genevestigatori Q06185.

    Family and domain databases

    InterProi IPR008386. ATPase_F0-cplx_esu_mt.
    [Graphical view ]
    Pfami PF05680. ATP-synt_E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "F1F0-ATPase subunit e gene isolated in a screen for diet regulated genes."
      Elliott T.S., Swartz D.A., Paisley E.A., Mangian H.J., Visek W.J., Kaput J.
      Biochem. Biophys. Res. Commun. 190:167-174(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Mammary gland.
    2. "The e subunit gene of murine F1F0-ATP synthase. Genomic sequence, chromosomal mapping, and diet regulation."
      Swartz D.A., Park E.I., Visek W.J., Kaput J.
      J. Biol. Chem. 271:20942-20948(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/cJ.
    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: C57BL/6J.
      Tissue: Mammary gland.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 16-28 AND 60-71, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    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-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiATP5I_MOUSE
    AccessioniPrimary (citable) accession number: Q06185
    Secondary accession number(s): P70342
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 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