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Q9D3D9

- ATPD_MOUSE

UniProt

Q9D3D9 - ATPD_MOUSE

Protein

ATP synthase subunit delta, mitochondrial

Gene

Atp5d

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (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 turnover 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 of the central stalk which is part of the complex rotary element. 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 delta, mitochondrial
    Alternative name(s):
    F-ATPase delta subunit
    Gene namesi
    Name:Atp5d
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1913293. Atp5d.

    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 – 2222MitochondrionBy similarityAdd
    BLAST
    Chaini23 – 168146ATP synthase subunit delta, mitochondrialPRO_0000002662Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei136 – 1361N6-acetyllysine; alternate1 Publication
    Modified residuei136 – 1361N6-succinyllysine; alternate1 Publication
    Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Modified residuei165 – 1651N6-acetyllysine; alternate1 Publication
    Modified residuei165 – 1651N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9D3D9.
    PaxDbiQ9D3D9.
    PRIDEiQ9D3D9.

    2D gel databases

    UCD-2DPAGEQ9D3D9.

    PTM databases

    PhosphoSiteiQ9D3D9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D3D9.
    BgeeiQ9D3D9.
    GenevestigatoriQ9D3D9.

    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 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

    BioGridi211172. 3 interactions.
    IntActiQ9D3D9. 6 interactions.
    MINTiMINT-4126883.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D3D9.
    SMRiQ9D3D9. Positions 37-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase epsilon chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0355.
    GeneTreeiENSGT00390000017576.
    HOGENOMiHOG000216023.
    HOVERGENiHBG001856.
    InParanoidiQ9D3D9.
    KOiK02134.
    OMAiLPHQAIF.
    OrthoDBiEOG7RNK2T.
    PhylomeDBiQ9D3D9.
    TreeFamiTF313029.

    Family and domain databases

    Gene3Di2.60.15.10. 1 hit.
    HAMAPiMF_00530. ATP_synth_epsil_bac.
    InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    IPR020547. ATPase_F1_dsu/esu_C.
    [Graphical view]
    PANTHERiPTHR13822. PTHR13822. 1 hit.
    PfamiPF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view]
    ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsiTIGR01216. ATP_synt_epsi. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9D3D9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPASLLRHP GLRRLMLQAR TYAEAAAAPA PAAGPGQMSF TFASPTQVFF    50
    DSANVKQVDV PTLTGAFGIL ASHVPTLQVL RPGLVVVHTE DGTTTKYFVS 100
    SGSVTVNADS SVQLLAEEAV TLDMLDLGAA RANLEKAQSE LSGAADEAAR 150
    AEIQIRIEAN EALVKALE 168
    Length:168
    Mass (Da):17,600
    Last modified:June 1, 2001 - v1
    Checksum:iEC3DF1B581B630E9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018011 mRNA. Translation: BAB31035.1.
    BC008273 mRNA. Translation: AAH08273.1.
    CCDSiCCDS24010.1.
    RefSeqiNP_079589.2. NM_025313.2.
    UniGeneiMm.278560.

    Genome annotation databases

    EnsembliENSMUST00000003156; ENSMUSP00000003156; ENSMUSG00000003072.
    ENSMUST00000105367; ENSMUSP00000101006; ENSMUSG00000003072.
    GeneIDi66043.
    KEGGimmu:66043.
    UCSCiuc007gby.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018011 mRNA. Translation: BAB31035.1 .
    BC008273 mRNA. Translation: AAH08273.1 .
    CCDSi CCDS24010.1.
    RefSeqi NP_079589.2. NM_025313.2.
    UniGenei Mm.278560.

    3D structure databases

    ProteinModelPortali Q9D3D9.
    SMRi Q9D3D9. Positions 37-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211172. 3 interactions.
    IntActi Q9D3D9. 6 interactions.
    MINTi MINT-4126883.

    PTM databases

    PhosphoSitei Q9D3D9.

    2D gel databases

    UCD-2DPAGE Q9D3D9.

    Proteomic databases

    MaxQBi Q9D3D9.
    PaxDbi Q9D3D9.
    PRIDEi Q9D3D9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003156 ; ENSMUSP00000003156 ; ENSMUSG00000003072 .
    ENSMUST00000105367 ; ENSMUSP00000101006 ; ENSMUSG00000003072 .
    GeneIDi 66043.
    KEGGi mmu:66043.
    UCSCi uc007gby.2. mouse.

    Organism-specific databases

    CTDi 513.
    MGIi MGI:1913293. Atp5d.

    Phylogenomic databases

    eggNOGi COG0355.
    GeneTreei ENSGT00390000017576.
    HOGENOMi HOG000216023.
    HOVERGENi HBG001856.
    InParanoidi Q9D3D9.
    KOi K02134.
    OMAi LPHQAIF.
    OrthoDBi EOG7RNK2T.
    PhylomeDBi Q9D3D9.
    TreeFami TF313029.

    Miscellaneous databases

    ChiTaRSi ATP5D. mouse.
    NextBioi 320454.
    PROi Q9D3D9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D3D9.
    Bgeei Q9D3D9.
    Genevestigatori Q9D3D9.

    Family and domain databases

    Gene3Di 2.60.15.10. 1 hit.
    HAMAPi MF_00530. ATP_synth_epsil_bac.
    InterProi IPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    IPR020547. ATPase_F1_dsu/esu_C.
    [Graphical view ]
    PANTHERi PTHR13822. PTHR13822. 1 hit.
    Pfami PF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view ]
    ProDomi PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsi TIGR01216. ATP_synt_epsi. 1 hit.
    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: Thymus.
    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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 137-150 AND 157-165, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    4. "A proteomics approach to identify the ubiquitinated proteins in mouse heart."
      Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K., Choi H.W., Park Z.-Y., Yoo Y.J.
      Biochem. Biophys. Res. Commun. 357:731-736(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-136.
      Tissue: Heart.
    5. "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-136 AND LYS-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "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-136 AND LYS-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiATPD_MOUSE
    AccessioniPrimary (citable) accession number: Q9D3D9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 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