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P05631

- ATPG_BOVIN

UniProt

P05631 - ATPG_BOVIN

Protein

ATP synthase subunit gamma, mitochondrial

Gene

ATP5C1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (01 Jun 1994)
      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. protein binding Source: UniProtKB
    2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    3. 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

    Enzyme and pathway databases

    ReactomeiREACT_212639. Formation of ATP by chemiosmotic coupling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit gamma, mitochondrial
    Alternative name(s):
    F-ATPase gamma subunit
    Gene namesi
    Name:ATP5C1
    Synonyms:ATP5C
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 13

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    2. 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 – 2525Mitochondrion2 PublicationsAdd
    BLAST
    Chaini26 – 298273ATP synthase subunit gamma, mitochondrialPRO_0000002684Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391N6-acetyllysineBy similarity
    Modified residuei49 – 491N6-succinyllysineBy similarity
    Modified residuei55 – 551N6-acetyllysineBy similarity
    Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
    Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
    Modified residuei154 – 1541N6-acetyllysine; alternateBy similarity
    Modified residuei154 – 1541N6-succinyllysine; alternateBy similarity
    Modified residuei197 – 1971N6-acetyllysineBy similarity
    Modified residuei270 – 2701N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP05631.
    PRIDEiP05631.

    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 MP68.3 Publications

    Protein-protein interaction databases

    DIPiDIP-47546N.
    IntActiP05631. 1 interaction.
    MINTiMINT-5006919.
    STRINGi9913.ENSBTAP00000018505.

    Structurei

    Secondary structure

    1
    298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 6942
    Turni74 – 763
    Helixi77 – 793
    Beta strandi93 – 964
    Helixi106 – 1105
    Beta strandi115 – 1173
    Turni118 – 1203
    Beta strandi130 – 1345
    Helixi135 – 1406
    Helixi143 – 1453
    Helixi146 – 1483
    Beta strandi149 – 1546
    Beta strandi157 – 1593
    Helixi163 – 17210
    Turni175 – 1773
    Beta strandi181 – 19010
    Beta strandi192 – 1943
    Beta strandi195 – 2039
    Turni207 – 2104
    Helixi213 – 2175
    Turni223 – 2253
    Turni227 – 2293
    Helixi232 – 29564

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BMFX-ray2.85G26-297[»]
    1COWX-ray3.10G26-297[»]
    1E1QX-ray2.61G26-297[»]
    1E1RX-ray2.50G26-297[»]
    1E79X-ray2.40G26-297[»]
    1EFRX-ray3.10G26-297[»]
    1H8EX-ray2.00G26-297[»]
    1H8HX-ray2.90G26-297[»]
    1NBMX-ray3.00G26-297[»]
    1OHHX-ray2.80G26-297[»]
    1QO1X-ray3.90G26-297[»]
    1W0JX-ray2.20G26-297[»]
    1W0KX-ray2.85G26-297[»]
    2CK3X-ray1.90G26-297[»]
    2JDIX-ray1.90G26-298[»]
    2JIZX-ray2.30G/N26-297[»]
    2JJ1X-ray2.70G/N26-297[»]
    2JJ2X-ray2.40G/N26-297[»]
    2V7QX-ray2.10G26-297[»]
    2W6EX-ray6.50G1-298[»]
    2W6FX-ray6.00G1-298[»]
    2W6GX-ray6.00G1-298[»]
    2W6HX-ray5.00G1-298[»]
    2W6IX-ray4.00G1-298[»]
    2W6JX-ray3.84G1-298[»]
    2WSSX-ray3.20G/P26-297[»]
    2XNDX-ray3.50G26-297[»]
    4ASUX-ray2.60G26-298[»]
    ProteinModelPortaliP05631.
    SMRiP05631. Positions 26-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05631.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase gamma chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0224.
    GeneTreeiENSGT00390000006837.
    HOGENOMiHOG000215911.
    HOVERGENiHBG000933.
    InParanoidiP05631.
    KOiK02136.
    OMAiMATLKDX.
    OrthoDBiEOG7QK0D3.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Liver (identifier: P05631-1) [UniParc]FASTAAdd to Basket

    Also known as: L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFSRAGVAGL SAWTVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM    50
    VAAAKYARAE RELKPARVYG VGSLALYEKA DIKTPEDKKK HLIIGVSSDR 100
    GLCGAIHSSV AKQMKSEAAN LAAAGKEVKI IGVGDKIRSI LHRTHSDQFL 150
    VTFKEVGRRP PTFGDASVIA LELLNSGYEF DEGSIIFNRF RSVISYKTEE 200
    KPIFSLDTIS SAESMSIYDD IDADVLRNYQ EYSLANIIYY SLKESTTSEQ 250
    SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD 298
    Length:298
    Mass (Da):33,072
    Last modified:June 1, 1994 - v3
    Checksum:iC1F41767CDABAD92
    GO
    Isoform Heart (identifier: P05631-2) [UniParc]FASTAAdd to Basket

    Also known as: H

    The sequence of this isoform differs from the canonical sequence as follows:
         298-298: Missing.

    Show »
    Length:297
    Mass (Da):32,957
    Checksum:i241767CDABAD92D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti249 – 2491E → G in AAI02467. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei298 – 2981Missing in isoform Heart. CuratedVSP_000438

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55389 mRNA. Translation: CAA39064.1.
    M22463 Genomic DNA. Translation: AAA30398.1.
    BC102466 mRNA. Translation: AAI02467.1.
    PIRiA32019. PWBOG.
    RefSeqiNP_001068604.1. NM_001075136.2.
    XP_005214178.1. XM_005214121.1. [P05631-2]
    XP_005214179.1. XM_005214122.1. [P05631-2]
    UniGeneiBt.20727.

    Genome annotation databases

    EnsembliENSBTAT00000018505; ENSBTAP00000018505; ENSBTAG00000013930. [P05631-1]
    GeneIDi327668.
    KEGGibta:327668.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55389 mRNA. Translation: CAA39064.1 .
    M22463 Genomic DNA. Translation: AAA30398.1 .
    BC102466 mRNA. Translation: AAI02467.1 .
    PIRi A32019. PWBOG.
    RefSeqi NP_001068604.1. NM_001075136.2.
    XP_005214178.1. XM_005214121.1. [P05631-2 ]
    XP_005214179.1. XM_005214122.1. [P05631-2 ]
    UniGenei Bt.20727.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BMF X-ray 2.85 G 26-297 [» ]
    1COW X-ray 3.10 G 26-297 [» ]
    1E1Q X-ray 2.61 G 26-297 [» ]
    1E1R X-ray 2.50 G 26-297 [» ]
    1E79 X-ray 2.40 G 26-297 [» ]
    1EFR X-ray 3.10 G 26-297 [» ]
    1H8E X-ray 2.00 G 26-297 [» ]
    1H8H X-ray 2.90 G 26-297 [» ]
    1NBM X-ray 3.00 G 26-297 [» ]
    1OHH X-ray 2.80 G 26-297 [» ]
    1QO1 X-ray 3.90 G 26-297 [» ]
    1W0J X-ray 2.20 G 26-297 [» ]
    1W0K X-ray 2.85 G 26-297 [» ]
    2CK3 X-ray 1.90 G 26-297 [» ]
    2JDI X-ray 1.90 G 26-298 [» ]
    2JIZ X-ray 2.30 G/N 26-297 [» ]
    2JJ1 X-ray 2.70 G/N 26-297 [» ]
    2JJ2 X-ray 2.40 G/N 26-297 [» ]
    2V7Q X-ray 2.10 G 26-297 [» ]
    2W6E X-ray 6.50 G 1-298 [» ]
    2W6F X-ray 6.00 G 1-298 [» ]
    2W6G X-ray 6.00 G 1-298 [» ]
    2W6H X-ray 5.00 G 1-298 [» ]
    2W6I X-ray 4.00 G 1-298 [» ]
    2W6J X-ray 3.84 G 1-298 [» ]
    2WSS X-ray 3.20 G/P 26-297 [» ]
    2XND X-ray 3.50 G 26-297 [» ]
    4ASU X-ray 2.60 G 26-298 [» ]
    ProteinModelPortali P05631.
    SMRi P05631. Positions 26-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47546N.
    IntActi P05631. 1 interaction.
    MINTi MINT-5006919.
    STRINGi 9913.ENSBTAP00000018505.

    Chemistry

    ChEMBLi CHEMBL612444.

    Proteomic databases

    PaxDbi P05631.
    PRIDEi P05631.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000018505 ; ENSBTAP00000018505 ; ENSBTAG00000013930 . [P05631-1 ]
    GeneIDi 327668.
    KEGGi bta:327668.

    Organism-specific databases

    CTDi 509.

    Phylogenomic databases

    eggNOGi COG0224.
    GeneTreei ENSGT00390000006837.
    HOGENOMi HOG000215911.
    HOVERGENi HBG000933.
    InParanoidi P05631.
    KOi K02136.
    OMAi MATLKDX.
    OrthoDBi EOG7QK0D3.
    TreeFami TF105765.

    Enzyme and pathway databases

    Reactomei REACT_212639. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    EvolutionaryTracei P05631.
    NextBioi 20810133.

    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. "ATP synthase from bovine mitochondria: complementary DNA sequence of the mitochondrial import precursor of the gamma-subunit and the genomic sequence of the mature protein."
      Dyer M.R., Gay N.J., Powell S.J., Walker J.E.
      Biochemistry 28:3670-3680(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.
    3. "Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria."
      Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.
      J. Mol. Biol. 184:677-701(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 174-297, PROTEIN SEQUENCE OF 26-297.
    4. "Identification of the subunits of F1F0-ATPase from bovine heart mitochondria."
      Walker J.E., Lutter R., Dupuis A., Runswick M.J.
      Biochemistry 30:5369-5378(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-30.
      Tissue: Heart.
    5. "Tissue-specific isoforms of the bovine mitochondrial ATP synthase gamma-subunit."
      Matsuda C., Endo H., Hirata H., Morosawa H., Nakanishi M., Kagawa Y.
      FEBS Lett. 325:281-284(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 286-298, ALTERNATIVE SPLICING.
      Tissue: Heart and Liver.
    6. "Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
      Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
      FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
    7. "Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria."
      Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.
      Nature 370:621-628(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    8. "The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin."
      Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G., Walker J.E.
      Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
    9. "Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism."
      Orriss G.L., Leslie A.G., Braig K., Walker J.E.
      Structure 6:831-837(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    10. "The structure of bovine F1-ATPase in complex with its regulatory protein IF1."
      Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.
      Nat. Struct. Biol. 10:744-750(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-297 IN COMPLEX WITH ATPIF1; ATP5A1 AND ATP5B.
    11. "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria."
      Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.
      Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-297 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5B; ATP5D AND ATP5E.

    Entry informationi

    Entry nameiATPG_BOVIN
    AccessioniPrimary (citable) accession number: P05631
    Secondary accession number(s): Q3T0B4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3