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Q9CQQ7

- AT5F1_MOUSE

UniProt

Q9CQQ7 - AT5F1_MOUSE

Protein

ATP synthase F(0) complex subunit B1, mitochondrial

Gene

Atp5f1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (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. ATPase activity Source: Ensembl
    2. hydrogen ion transmembrane transporter activity Source: InterPro

    GO - Biological processi

    1. ATP synthesis coupled proton transport Source: RefGenome

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase F(0) complex subunit B1, mitochondrial
    Alternative name(s):
    ATP synthase subunit b
    Short name:
    ATPase subunit b
    Gene namesi
    Name:Atp5f1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1100495. Atp5f1.

    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: RefGenome
    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 – 4242MitochondrionBy similarityAdd
    BLAST
    Chaini43 – 256214ATP synthase F(0) complex subunit B1, mitochondrialPRO_0000002514Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311N6-succinyllysine1 Publication
    Modified residuei139 – 1391N6-acetyllysine1 Publication
    Modified residuei154 – 1541N6-acetyllysine1 Publication
    Modified residuei162 – 1621N6-acetyllysine1 Publication
    Modified residuei221 – 2211N6-acetyllysine1 Publication
    Modified residuei225 – 2251N6-acetyllysine1 Publication
    Modified residuei233 – 2331N6-acetyllysine1 Publication
    Modified residuei244 – 2441N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9CQQ7.
    PaxDbiQ9CQQ7.
    PRIDEiQ9CQQ7.

    PTM databases

    PhosphoSiteiQ9CQQ7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CQQ7.
    BgeeiQ9CQQ7.
    GenevestigatoriQ9CQQ7.

    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

    BioGridi198256. 2 interactions.
    IntActiQ9CQQ7. 3 interactions.
    MINTiMINT-1841503.
    STRINGi10090.ENSMUSP00000088168.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CQQ7.
    SMRiQ9CQQ7. Positions 121-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic ATPase B chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG245616.
    GeneTreeiENSGT00390000001958.
    HOGENOMiHOG000007163.
    HOVERGENiHBG050604.
    InParanoidiQ9CQQ7.
    KOiK02127.
    OMAiVINHETF.
    OrthoDBiEOG7V4B02.
    PhylomeDBiQ9CQQ7.
    TreeFamiTF313250.

    Family and domain databases

    InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
    IPR013837. ATPase_F0_sub_B/B_chain.
    [Graphical view]
    PANTHERiPTHR12733. PTHR12733. 1 hit.
    PfamiPF05405. Mt_ATP-synt_B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9CQQ7-1 [UniParc]FASTAAdd to Basket

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    MLSRVVLSAA ATAAPCLKNA AALGPGVLQA TRAFHTGQPR LAPLPPLPEY    50
    GGKVRLGLIP EEFFQFLYPK TGVTGPYVLG TGLSLYFLSK EIYVITPETF 100
    STISVVGLIV YVIKKYGASF GEFIDKLNEE KIAQLEEVKQ SSMKQIQDAI 150
    DMEKAQQALV QKRHYLFDVQ RNNIALALEV TYRERLHKAY KEVKNRLDYH 200
    ISVQNMMRRK EEEHMIDWVE KHVVKSISVQ QEKETIAKCI EDLKLLAKKA 250
    QAQPIM 256
    Length:256
    Mass (Da):28,949
    Last modified:June 1, 2001 - v1
    Checksum:i6B385AE4DE6CB784
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002960 mRNA. Translation: BAB22481.1.
    AK011312 mRNA. Translation: BAB27538.1.
    CCDSiCCDS17714.1.
    RefSeqiNP_033855.2. NM_009725.3.
    XP_006500997.1. XM_006500934.1.
    UniGeneiMm.251152.

    Genome annotation databases

    EnsembliENSMUST00000118209; ENSMUSP00000113022; ENSMUSG00000000563.
    GeneIDi11950.
    KEGGimmu:11950.
    UCSCiuc008qvl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002960 mRNA. Translation: BAB22481.1 .
    AK011312 mRNA. Translation: BAB27538.1 .
    CCDSi CCDS17714.1.
    RefSeqi NP_033855.2. NM_009725.3.
    XP_006500997.1. XM_006500934.1.
    UniGenei Mm.251152.

    3D structure databases

    ProteinModelPortali Q9CQQ7.
    SMRi Q9CQQ7. Positions 121-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198256. 2 interactions.
    IntActi Q9CQQ7. 3 interactions.
    MINTi MINT-1841503.
    STRINGi 10090.ENSMUSP00000088168.

    PTM databases

    PhosphoSitei Q9CQQ7.

    Proteomic databases

    MaxQBi Q9CQQ7.
    PaxDbi Q9CQQ7.
    PRIDEi Q9CQQ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000118209 ; ENSMUSP00000113022 ; ENSMUSG00000000563 .
    GeneIDi 11950.
    KEGGi mmu:11950.
    UCSCi uc008qvl.1. mouse.

    Organism-specific databases

    CTDi 515.
    MGIi MGI:1100495. Atp5f1.

    Phylogenomic databases

    eggNOGi NOG245616.
    GeneTreei ENSGT00390000001958.
    HOGENOMi HOG000007163.
    HOVERGENi HBG050604.
    InParanoidi Q9CQQ7.
    KOi K02127.
    OMAi VINHETF.
    OrthoDBi EOG7V4B02.
    PhylomeDBi Q9CQQ7.
    TreeFami TF313250.

    Miscellaneous databases

    ChiTaRSi ATP5F1. mouse.
    NextBioi 280069.
    PROi Q9CQQ7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CQQ7.
    Bgeei Q9CQQ7.
    Genevestigatori Q9CQQ7.

    Family and domain databases

    InterProi IPR008688. ATPase_B_chain/sub_B/MI25.
    IPR013837. ATPase_F0_sub_B/B_chain.
    [Graphical view ]
    PANTHERi PTHR12733. PTHR12733. 1 hit.
    Pfami PF05405. Mt_ATP-synt_B. 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: Brain and Embryo.
    2. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 71-90; 115-139; 145-154; 164-183 AND 195-221, 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-131, 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-139; LYS-154; LYS-162; LYS-221; LYS-225; LYS-233 AND LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiAT5F1_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 103 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