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P19483

- ATPA_BOVIN

UniProt

P19483 - ATPA_BOVIN

Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP5A1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      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. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei413 – 4131Required for activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi212 – 2198ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    4. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. ATP synthesis coupled proton transport Source: InterPro

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit alpha, mitochondrial
    Gene namesi
    Name:ATP5A1
    Synonyms:ATP5A2
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Mitochondrion inner membrane By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
    Note: Colocalizes with HRG on the cell surface of T-cells.By similarity

    GO - Cellular componenti

    1. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    2. plasma membrane Source: UniProtKB-SubCell
    3. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343Mitochondrion1 PublicationAdd
    BLAST
    Chaini44 – 553510ATP synthase subunit alpha, mitochondrialPRO_0000002423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441Pyrrolidone carboxylic acid
    Modified residuei76 – 761PhosphoserineBy similarity
    Glycosylationi76 – 761O-linked (GlcNAc)By similarity
    Modified residuei123 – 1231N6-acetyllysineBy similarity
    Modified residuei126 – 1261N6-acetyllysineBy similarity
    Modified residuei132 – 1321N6-acetyllysineBy similarity
    Modified residuei161 – 1611N6-acetyllysine; alternateBy similarity
    Modified residuei161 – 1611N6-succinyllysine; alternateBy similarity
    Modified residuei166 – 1661PhosphoserineBy similarity
    Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
    Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
    Modified residuei230 – 2301N6-acetyllysine; alternateBy similarity
    Modified residuei230 – 2301N6-succinyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
    Modified residuei240 – 2401N6-acetyllysineBy similarity
    Modified residuei261 – 2611N6-acetyllysine; alternateBy similarity
    Modified residuei261 – 2611N6-succinyllysine; alternateBy similarity
    Modified residuei305 – 3051N6-acetyllysine; alternateBy similarity
    Modified residuei305 – 3051N6-succinyllysine; alternateBy similarity
    Modified residuei427 – 4271N6-acetyllysine; alternateBy similarity
    Modified residuei427 – 4271N6-succinyllysine; alternateBy similarity
    Modified residuei434 – 4341N6-acetyllysineBy similarity
    Modified residuei498 – 4981N6-acetyllysine; alternateBy similarity
    Modified residuei498 – 4981N6-succinyllysine; alternateBy similarity
    Modified residuei506 – 5061N6-acetyllysine; alternateBy similarity
    Modified residuei506 – 5061N6-succinyllysine; alternateBy similarity
    Modified residuei531 – 5311N6-acetyllysine; alternateBy similarity
    Modified residuei531 – 5311N6-succinyllysine; alternateBy similarity
    Modified residuei539 – 5391N6-acetyllysine; alternateBy similarity
    Modified residuei539 – 5391N6-succinyllysine; alternateBy similarity
    Modified residuei541 – 5411N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylated on lysine residues. BLOC1S1 is required for acetylation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP19483.
    PRIDEiP19483.

    2D gel databases

    UCD-2DPAGEP19483.

    Expressioni

    Tissue specificityi

    Heart and liver.

    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. Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). 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. Interacts with BLOC1S1. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficency.3 Publications

    Protein-protein interaction databases

    DIPiDIP-35479N.
    IntActiP19483. 4 interactions.
    MINTiMINT-5006839.
    STRINGi9913.ENSBTAP00000003259.

    Structurei

    Secondary structure

    1
    553
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi53 – 608
    Turni68 – 703
    Beta strandi71 – 788
    Beta strandi81 – 866
    Beta strandi95 – 984
    Beta strandi103 – 1097
    Beta strandi114 – 1207
    Helixi122 – 1243
    Beta strandi130 – 1323
    Beta strandi139 – 1435
    Helixi144 – 1463
    Beta strandi150 – 1523
    Beta strandi153 – 1553
    Beta strandi159 – 1613
    Beta strandi167 – 1737
    Beta strandi179 – 1824
    Beta strandi187 – 1893
    Helixi194 – 1996
    Beta strandi209 – 2135
    Helixi218 – 22811
    Helixi230 – 2334
    Beta strandi234 – 2363
    Turni238 – 2403
    Beta strandi243 – 2508
    Helixi253 – 26513
    Helixi269 – 2713
    Beta strandi272 – 2776
    Helixi283 – 30220
    Beta strandi306 – 3127
    Helixi314 – 32714
    Helixi334 – 3363
    Helixi341 – 3499
    Beta strandi353 – 3553
    Helixi357 – 3593
    Beta strandi363 – 3719
    Beta strandi373 – 3753
    Helixi380 – 3889
    Beta strandi389 – 3957
    Helixi397 – 4026
    Turni410 – 4123
    Beta strandi414 – 4174
    Helixi418 – 4214
    Helixi424 – 44118
    Helixi444 – 4463
    Beta strandi447 – 4493
    Beta strandi451 – 4533
    Helixi455 – 47016
    Helixi481 – 49212
    Turni493 – 4986
    Helixi501 – 5033
    Helixi504 – 51714
    Helixi520 – 52910
    Helixi534 – 55118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BMFX-ray2.85A/B/C44-553[»]
    1COWX-ray3.10A/B/C45-553[»]
    1E1QX-ray2.61A/B/C44-553[»]
    1E1RX-ray2.50A/B/C44-553[»]
    1E79X-ray2.40A/B/C44-553[»]
    1EFRX-ray3.10A/B/C45-553[»]
    1H8EX-ray2.00A/B/C44-553[»]
    1H8HX-ray2.90A/B/C44-553[»]
    1NBMX-ray3.00A/B/C44-553[»]
    1OHHX-ray2.80A/B/C44-553[»]
    1QO1X-ray3.90A/B/C44-553[»]
    1W0JX-ray2.20A/B/C44-553[»]
    1W0KX-ray2.85A/B/C44-553[»]
    2CK3X-ray1.90A/B/C44-553[»]
    2JDIX-ray1.90A/B/C44-553[»]
    2JIZX-ray2.30A/B/C/H/I/J44-553[»]
    2JJ1X-ray2.70A/B/C/H/I/J44-553[»]
    2JJ2X-ray2.40A/B/C/H/I/J44-553[»]
    2JMXNMR-B44-68[»]
    2V7QX-ray2.10A/B/C45-553[»]
    2W6EX-ray6.50A/B/C1-553[»]
    2W6FX-ray6.00A/B/C1-553[»]
    2W6GX-ray6.00A/B/C1-553[»]
    2W6HX-ray5.00A/B/C1-553[»]
    2W6IX-ray4.00A/B/C1-553[»]
    2W6JX-ray3.84A/B/C1-553[»]
    2WSSX-ray3.20A/B/C/J/K/L44-553[»]
    2XNDX-ray3.50A/B/C62-553[»]
    4ASUX-ray2.60A/B/C44-553[»]
    ProteinModelPortaliP19483.
    SMRiP19483. Positions 59-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19483.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0056.
    HOGENOMiHOG000130111.
    InParanoidiP19482.
    KOiK02132.

    Family and domain databases

    Gene3Di2.40.30.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01346. ATP_synth_alpha_bact.
    InterProiIPR020003. ATPase_a/bsu_AS.
    IPR023366. ATPase_asu-like.
    IPR005294. ATPase_F1-cplx_asu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00962. atpA. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P19483-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE    50
    VSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS 100
    GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV 150
    VDALGNAIDG KGPIGSKARR RVGLKAPGII PRISVREPMQ TGIKAVDSLV 200
    PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG 250
    QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 300
    RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 350
    RAAKMNDAFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF 400
    YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG 450
    SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE 500
    PSKITKFENA FLSHVISQHQ ALLSKIRTDG KISEESDAKL KEIVTNFLAG 550
    FEA 553
    Length:553
    Mass (Da):59,720
    Last modified:February 1, 1991 - v1
    Checksum:i188E9531B3B815E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41V → M in AAI16060. 1 PublicationCurated
    Sequence conflicti6 – 61V → I in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti31 – 333IAA → VGT in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti41 – 411S → T in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti51 – 511V → M in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti144 – 1441E → D in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti164 – 1641I → V in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti168 – 1681A → I in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti358 – 3581A → S in AAA30399. (PubMed:2896000)Curated
    Sequence conflicti524 – 5241S → G in AAI16060. 1 PublicationCurated
    Sequence conflicti524 – 5241S → G AA sequence (PubMed:2864455)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22465 mRNA. Translation: AAB59266.1.
    X64565 Genomic DNA. Translation: CAA45865.1.
    BC116059 mRNA. Translation: AAI16060.1.
    M19680 mRNA. Translation: AAA30399.1.
    PIRiA27693.
    S27201. PWBOA.
    RefSeqiNP_777109.1. NM_174684.2.
    UniGeneiBt.7194.

    Genome annotation databases

    GeneIDi282578.
    KEGGibta:282578.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22465 mRNA. Translation: AAB59266.1 .
    X64565 Genomic DNA. Translation: CAA45865.1 .
    BC116059 mRNA. Translation: AAI16060.1 .
    M19680 mRNA. Translation: AAA30399.1 .
    PIRi A27693.
    S27201. PWBOA.
    RefSeqi NP_777109.1. NM_174684.2.
    UniGenei Bt.7194.

    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 A/B/C 44-553 [» ]
    1COW X-ray 3.10 A/B/C 45-553 [» ]
    1E1Q X-ray 2.61 A/B/C 44-553 [» ]
    1E1R X-ray 2.50 A/B/C 44-553 [» ]
    1E79 X-ray 2.40 A/B/C 44-553 [» ]
    1EFR X-ray 3.10 A/B/C 45-553 [» ]
    1H8E X-ray 2.00 A/B/C 44-553 [» ]
    1H8H X-ray 2.90 A/B/C 44-553 [» ]
    1NBM X-ray 3.00 A/B/C 44-553 [» ]
    1OHH X-ray 2.80 A/B/C 44-553 [» ]
    1QO1 X-ray 3.90 A/B/C 44-553 [» ]
    1W0J X-ray 2.20 A/B/C 44-553 [» ]
    1W0K X-ray 2.85 A/B/C 44-553 [» ]
    2CK3 X-ray 1.90 A/B/C 44-553 [» ]
    2JDI X-ray 1.90 A/B/C 44-553 [» ]
    2JIZ X-ray 2.30 A/B/C/H/I/J 44-553 [» ]
    2JJ1 X-ray 2.70 A/B/C/H/I/J 44-553 [» ]
    2JJ2 X-ray 2.40 A/B/C/H/I/J 44-553 [» ]
    2JMX NMR - B 44-68 [» ]
    2V7Q X-ray 2.10 A/B/C 45-553 [» ]
    2W6E X-ray 6.50 A/B/C 1-553 [» ]
    2W6F X-ray 6.00 A/B/C 1-553 [» ]
    2W6G X-ray 6.00 A/B/C 1-553 [» ]
    2W6H X-ray 5.00 A/B/C 1-553 [» ]
    2W6I X-ray 4.00 A/B/C 1-553 [» ]
    2W6J X-ray 3.84 A/B/C 1-553 [» ]
    2WSS X-ray 3.20 A/B/C/J/K/L 44-553 [» ]
    2XND X-ray 3.50 A/B/C 62-553 [» ]
    4ASU X-ray 2.60 A/B/C 44-553 [» ]
    ProteinModelPortali P19483.
    SMRi P19483. Positions 59-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35479N.
    IntActi P19483. 4 interactions.
    MINTi MINT-5006839.
    STRINGi 9913.ENSBTAP00000003259.

    2D gel databases

    UCD-2DPAGE P19483.

    Proteomic databases

    PaxDbi P19483.
    PRIDEi P19483.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 282578.
    KEGGi bta:282578.

    Organism-specific databases

    CTDi 498.

    Phylogenomic databases

    eggNOGi COG0056.
    HOGENOMi HOG000130111.
    InParanoidi P19482.
    KOi K02132.

    Miscellaneous databases

    EvolutionaryTracei P19483.
    NextBioi 20806299.

    Family and domain databases

    Gene3Di 2.40.30.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_01346. ATP_synth_alpha_bact.
    InterProi IPR020003. ATPase_a/bsu_AS.
    IPR023366. ATPase_asu-like.
    IPR005294. ATPase_F1-cplx_asu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00962. atpA. 1 hit.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ATP synthase from bovine mitochondria: complementary DNA sequence of the import precursor of a heart isoform of the alpha subunit."
      Walker J.E., Powell S.J., Vinas O., Runswick M.J.
      Biochemistry 28:4702-4708(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "Structural organization of a nuclear gene for the alpha-subunit of the bovine mitochondrial ATP synthase complex."
      Pierce D.J., Jordan E.M., Breen G.A.M.
      Biochim. Biophys. Acta 1132:265-275(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Ascending colon.
    4. "Bovine liver cDNA clones encoding a precursor of the alpha-subunit of the mitochondrial ATP synthase complex."
      Breen G.A.M.
      Biochem. Biophys. Res. Commun. 152:264-269(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-359.
      Tissue: Liver.
    5. "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: PROTEIN SEQUENCE OF 44-552.
      Tissue: Heart.
    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 44-553 IN COMPLEX WITH ATPIF1; ATP5B AND ATP5C1.
    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 45-553 IN COMPLEX WITH ATPIF1; ATP5B; ATP5C1; ATP5D AND ATP5E.

    Entry informationi

    Entry nameiATPA_BOVIN
    AccessioniPrimary (citable) accession number: P19483
    Secondary accession number(s): P05629, P19482, Q1JQC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 147 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

    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