ATPA_BOVIN
ID ATPA_BOVIN Reviewed; 553 AA.
AC P19483; P05629; P19482; Q1JQC4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit alpha {ECO:0000250|UniProtKB:P25705};
DE Flags: Precursor;
GN Name=ATP5F1A {ECO:0000250|UniProtKB:P25705}; Synonyms=ATP5A1, ATP5A2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2527557; DOI=10.1021/bi00437a029;
RA Walker J.E., Powell S.J., Vinas O., Runswick M.J.;
RT "ATP synthase from bovine mitochondria: complementary DNA sequence of the
RT import precursor of a heart isoform of the alpha subunit.";
RL Biochemistry 28:4702-4708(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1420306; DOI=10.1016/0167-4781(92)90160-2;
RA Pierce D.J., Jordan E.M., Breen G.A.M.;
RT "Structural organization of a nuclear gene for the alpha-subunit of the
RT bovine mitochondrial ATP synthase complex.";
RL Biochim. Biophys. Acta 1132:265-275(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-359.
RC TISSUE=Liver;
RX PubMed=2896000; DOI=10.1016/s0006-291x(88)80709-5;
RA Breen G.A.M.;
RT "Bovine liver cDNA clones encoding a precursor of the alpha-subunit of the
RT mitochondrial ATP synthase complex.";
RL Biochem. Biophys. Res. Commun. 152:264-269(1988).
RN [5]
RP PROTEIN SEQUENCE OF 44-552, PYROGLUTAMATE FORMATION AT GLN-44, SUBCELLULAR
RP LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=2864455; DOI=10.1016/0022-2836(85)90313-4;
RA Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D.,
RA Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.;
RT "Primary structure and subunit stoichiometry of F1-ATPase from bovine
RT mitochondria.";
RL J. Mol. Biol. 184:677-701(1985).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=95168; DOI=10.1007/bf02785056;
RA Sikerwar S.S., Malhotra S.K.;
RT "Visualization of mitochondrial coupling factor F1(ATPase) by freeze-
RT drying.";
RL Cell Biophys. 1:55-63(1979).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=14633978; DOI=10.1093/emboj/cdg608;
RA Rubinstein J.L., Walker J.E., Henderson R.;
RT "Structure of the mitochondrial ATP synthase by electron cryomicroscopy.";
RL EMBO J. 22:6182-6192(2003).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=23407638; DOI=10.1098/rsob.120160;
RA Runswick M.J., Bason J.V., Montgomery M.G., Robinson G.C., Fearnley I.M.,
RA Walker J.E.;
RT "The affinity purification and characterization of ATP synthase complexes
RT from mitochondria.";
RL Open Biol. 3:120160-120160(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
RN [11] {ECO:0007744|PDB:1BMF}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 44-553 IN COMPLEX WITH ATP
RP ANALOG, AND SUBUNIT.
RX PubMed=8065448; DOI=10.1038/370621a0;
RA Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.;
RT "Structure at 2.8-A resolution of F1-ATPase from bovine heart
RT mitochondria.";
RL Nature 370:621-628(1994).
RN [12] {ECO:0007744|PDB:1EFR}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 44-553 IN COMPLEX WITH ATP
RP ANALOG, AND SUBUNIT.
RX PubMed=8790345; DOI=10.1073/pnas.93.18.9420;
RA Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G.,
RA Walker J.E.;
RT "The structure of bovine F1-ATPase complexed with the peptide antibiotic
RT efrapeptin.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996).
RN [13] {ECO:0007744|PDB:1NBM}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 44-553 IN COMPLEX WITH ATP, AND
RP SUBUNIT.
RX PubMed=9687365; DOI=10.1016/s0969-2126(98)00085-9;
RA Orriss G.L., Leslie A.G., Braig K., Walker J.E.;
RT "Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan:
RT the structure provides further support for a rotary catalytic mechanism.";
RL Structure 6:831-837(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-553 IN COMPLEX WITH ATPIF1;
RP ATP5F1B AND ATP5F1C.
RX PubMed=12923572; DOI=10.1038/nsb966;
RA Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "The structure of bovine F1-ATPase in complex with its regulatory protein
RT IF1.";
RL Nat. Struct. Biol. 10:744-750(2003).
RN [15] {ECO:0007744|PDB:2V7Q}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 45-553 IN COMPLEX WITH ATP;
RP ATPIF1; ATP5F1B; ATP5F1C; ATP5F1D AND ATP5F1E.
RX PubMed=17895376; DOI=10.1073/pnas.0707326104;
RA Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits. Subunit
CC alpha does not bear the catalytic high-affinity ATP-binding sites.
CC Binds the bacterial siderophore enterobactin and can promote
CC mitochondrial accumulation of enterobactin-derived iron ions (By
CC similarity). {ECO:0000250|UniProtKB:P25705,
CC ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:23407638}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1) (PubMed:2864455,
CC PubMed:17570365, PubMed:23407638). CF(0) has three main subunits: a, b
CC and c (PubMed:2864455, PubMed:17570365, PubMed:23407638). Interacts
CC with ATPAF2 (By similarity). Interacts with HRG; the interaction occurs
CC on the surface of T-cells and alters the cell morphology when
CC associated with concanavalin (in vitro) (By similarity). Component of
CC an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD,
CC ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
CC ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (PubMed:2864455,
CC PubMed:17570365, PubMed:23407638, PubMed:25851905). Interacts with
CC BLOC1S1. Interacts with BCL2L1 isoform BCL-X(L); the interaction
CC mediates the association of BCL2L1 isoform BCL-X(L) with the
CC mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons
CC metabolic efficiency. Interacts with CLN5 and PPT1 (By similarity).
CC Interacts with S100A1; this interaction increases F1-ATPase activity
CC (By similarity). Interacts with ABCB7; this interaction allows the
CC regulation of cellular iron homeostasis and cellular reactive oxygen
CC species (ROS) levels in cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:P15999, ECO:0000250|UniProtKB:P25705,
CC ECO:0000250|UniProtKB:Q03265, ECO:0000269|PubMed:12923572,
CC ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:17895376,
CC ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:25851905,
CC ECO:0000269|PubMed:2864455}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638,
CC ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:95168}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14633978,
CC ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455,
CC ECO:0000269|PubMed:95168}; Matrix side {ECO:0000269|PubMed:14633978,
CC ECO:0000269|PubMed:95168}. Cell membrane
CC {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P25705}; Extracellular side
CC {ECO:0000250|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell
CC surface of T-cells. {ECO:0000250|UniProtKB:P25705}.
CC -!- TISSUE SPECIFICITY: Heart muscle (at protein level) (PubMed:2864455).
CC Heart and liver. {ECO:0000269|PubMed:2864455}.
CC -!- PTM: Acetylated on lysine residues. BLOC1S1 is required for
CC acetylation. {ECO:0000250|UniProtKB:P25705}.
CC -!- MISCELLANEOUS: The siderophore enterobactin (Ent) produced by enteric
CC bacteria binds Fe(3+) and helps bacteria scavenge iron ions from the
CC environment. As a consequence, the mammalian siderocalin LCN2 plays an
CC important role in defense against bacterial infections by sequestering
CC iron bound to microbial siderophores. LCN2 can also bind iron bound to
CC endogenous or nutrient-derived iron chelators and plays an important
CC role in cellular iron homeostasis. Enterobactin produced by non-
CC pathogenic E.coli strains can facilitate mitochondrial iron
CC assimilation, suggesting that iron bound to siderophores from non-
CC pathogenic bacteria may contribute to iron absorption by the host.
CC {ECO:0000250|UniProtKB:P25705}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; M22465; AAB59266.1; -; mRNA.
DR EMBL; X64565; CAA45865.1; -; Genomic_DNA.
DR EMBL; BC116059; AAI16060.1; -; mRNA.
DR EMBL; M19680; AAA30399.1; -; mRNA.
DR PIR; A27693; A27693.
DR PIR; S27201; PWBOA.
DR RefSeq; NP_777109.1; NM_174684.2.
DR PDB; 1BMF; X-ray; 2.85 A; A/B/C=44-553.
DR PDB; 1COW; X-ray; 3.10 A; A/B/C=45-553.
DR PDB; 1E1Q; X-ray; 2.61 A; A/B/C=44-553.
DR PDB; 1E1R; X-ray; 2.50 A; A/B/C=44-553.
DR PDB; 1E79; X-ray; 2.40 A; A/B/C=44-553.
DR PDB; 1EFR; X-ray; 3.10 A; A/B/C=45-553.
DR PDB; 1H8E; X-ray; 2.00 A; A/B/C=44-553.
DR PDB; 1H8H; X-ray; 2.90 A; A/B/C=44-553.
DR PDB; 1NBM; X-ray; 3.00 A; A/B/C=44-553.
DR PDB; 1OHH; X-ray; 2.80 A; A/B/C=44-553.
DR PDB; 1QO1; X-ray; 3.90 A; A/B/C=44-553.
DR PDB; 1W0J; X-ray; 2.20 A; A/B/C=44-553.
DR PDB; 1W0K; X-ray; 2.85 A; A/B/C=44-553.
DR PDB; 2CK3; X-ray; 1.90 A; A/B/C=44-553.
DR PDB; 2JDI; X-ray; 1.90 A; A/B/C=44-553.
DR PDB; 2JIZ; X-ray; 2.30 A; A/B/C/H/I/J=44-553.
DR PDB; 2JJ1; X-ray; 2.70 A; A/B/C/H/I/J=44-553.
DR PDB; 2JJ2; X-ray; 2.40 A; A/B/C/H/I/J=44-553.
DR PDB; 2JMX; NMR; -; B=44-68.
DR PDB; 2V7Q; X-ray; 2.10 A; A/B/C=45-553.
DR PDB; 2W6E; X-ray; 6.50 A; A/B/C=1-553.
DR PDB; 2W6F; X-ray; 6.00 A; A/B/C=1-553.
DR PDB; 2W6G; X-ray; 6.00 A; A/B/C=1-553.
DR PDB; 2W6H; X-ray; 5.00 A; A/B/C=1-553.
DR PDB; 2W6I; X-ray; 4.00 A; A/B/C=1-553.
DR PDB; 2W6J; X-ray; 3.84 A; A/B/C=1-553.
DR PDB; 2WSS; X-ray; 3.20 A; A/B/C/J/K/L=44-553.
DR PDB; 2XND; X-ray; 3.50 A; A/B/C=62-553.
DR PDB; 4ASU; X-ray; 2.60 A; A/B/C=44-553.
DR PDB; 4TSF; X-ray; 3.20 A; A/B/C=44-553.
DR PDB; 4TT3; X-ray; 3.21 A; A/B/C=44-553.
DR PDB; 4YXW; X-ray; 3.10 A; A/B/C=44-553.
DR PDB; 4Z1M; X-ray; 3.30 A; A/B/C=44-553.
DR PDB; 5ARA; EM; 6.70 A; A/B/C=44-553.
DR PDB; 5ARE; EM; 7.40 A; A/B/C=44-553.
DR PDB; 5ARH; EM; 7.20 A; A/B/C=44-553.
DR PDB; 5ARI; EM; 7.40 A; A/B/C=44-553.
DR PDB; 5FIJ; EM; 7.40 A; A/B/C=44-553.
DR PDB; 5FIK; EM; 6.40 A; A/B/C=44-553.
DR PDB; 5FIL; EM; 7.10 A; A/B/C=44-553.
DR PDB; 6YY0; EM; 3.23 A; A/B/C=44-553.
DR PDB; 6Z1R; EM; 3.29 A; A/B/C=44-553.
DR PDB; 6Z1U; EM; 3.47 A; A/B/C=44-553.
DR PDB; 6ZIQ; EM; 4.33 A; C=44-553.
DR PDB; 6ZIT; EM; 3.49 A; C=44-553.
DR PDB; 6ZIU; EM; 6.02 A; C=44-553.
DR PDB; 6ZPO; EM; 4.00 A; A/B/C=44-553.
DR PDB; 6ZQM; EM; 3.29 A; A/B/C=44-553.
DR PDB; 6ZQN; EM; 4.00 A; A/B/C=44-553.
DR PDB; 7AJB; EM; 9.20 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJC; EM; 11.90 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJD; EM; 9.00 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJE; EM; 9.40 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJF; EM; 8.45 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJG; EM; 10.70 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJH; EM; 9.70 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJI; EM; 11.40 A; A/AA/AB/AC/B/C=44-553.
DR PDB; 7AJJ; EM; 13.10 A; A/AA/AB/AC/B/C=44-553.
DR PDBsum; 1BMF; -.
DR PDBsum; 1COW; -.
DR PDBsum; 1E1Q; -.
DR PDBsum; 1E1R; -.
DR PDBsum; 1E79; -.
DR PDBsum; 1EFR; -.
DR PDBsum; 1H8E; -.
DR PDBsum; 1H8H; -.
DR PDBsum; 1NBM; -.
DR PDBsum; 1OHH; -.
DR PDBsum; 1QO1; -.
DR PDBsum; 1W0J; -.
DR PDBsum; 1W0K; -.
DR PDBsum; 2CK3; -.
DR PDBsum; 2JDI; -.
DR PDBsum; 2JIZ; -.
DR PDBsum; 2JJ1; -.
DR PDBsum; 2JJ2; -.
DR PDBsum; 2JMX; -.
DR PDBsum; 2V7Q; -.
DR PDBsum; 2W6E; -.
DR PDBsum; 2W6F; -.
DR PDBsum; 2W6G; -.
DR PDBsum; 2W6H; -.
DR PDBsum; 2W6I; -.
DR PDBsum; 2W6J; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 2XND; -.
DR PDBsum; 4ASU; -.
DR PDBsum; 4TSF; -.
DR PDBsum; 4TT3; -.
DR PDBsum; 4YXW; -.
DR PDBsum; 4Z1M; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P19483; -.
DR BMRB; P19483; -.
DR SMR; P19483; -.
DR CORUM; P19483; -.
DR DIP; DIP-35479N; -.
DR IntAct; P19483; 9.
DR MINT; P19483; -.
DR STRING; 9913.ENSBTAP00000003259; -.
DR UCD-2DPAGE; P19483; -.
DR PaxDb; P19483; -.
DR PeptideAtlas; P19483; -.
DR PRIDE; P19483; -.
DR GeneID; 282578; -.
DR KEGG; bta:282578; -.
DR CTD; 498; -.
DR eggNOG; KOG1353; Eukaryota.
DR InParanoid; P19483; -.
DR OrthoDB; 470054at2759; -.
DR BRENDA; 7.1.2.2; 908.
DR EvolutionaryTrace; P19483; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; ATP-binding; Cell membrane;
KW CF(1); Direct protein sequencing; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Methylation; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2864455"
FT CHAIN 44..553
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000002423"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17895376,
FT ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:8790345,
FT ECO:0000269|PubMed:9687365, ECO:0007744|PDB:1BMF,
FT ECO:0007744|PDB:1COW, ECO:0007744|PDB:1E1Q,
FT ECO:0007744|PDB:1E1R, ECO:0007744|PDB:1E79,
FT ECO:0007744|PDB:1EFR, ECO:0007744|PDB:1H8H,
FT ECO:0007744|PDB:1NBM, ECO:0007744|PDB:1OHH,
FT ECO:0007744|PDB:2CK3, ECO:0007744|PDB:2JDI,
FT ECO:0007744|PDB:2JIZ, ECO:0007744|PDB:2JJ1,
FT ECO:0007744|PDB:2JJ2, ECO:0007744|PDB:2V7Q,
FT ECO:0007744|PDB:2WSS, ECO:0007744|PDB:2XND,
FT ECO:0007744|PDB:4TSF, ECO:0007744|PDB:4TT3,
FT ECO:0007744|PDB:4YXW, ECO:0007744|PDB:4Z1M"
FT BINDING 473..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17895376,
FT ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:8790345,
FT ECO:0000269|PubMed:9687365, ECO:0007744|PDB:1BMF,
FT ECO:0007744|PDB:1COW, ECO:0007744|PDB:1E1Q,
FT ECO:0007744|PDB:1E1R, ECO:0007744|PDB:1E79,
FT ECO:0007744|PDB:1EFR, ECO:0007744|PDB:1H8H,
FT ECO:0007744|PDB:1NBM, ECO:0007744|PDB:1OHH,
FT ECO:0007744|PDB:2CK3, ECO:0007744|PDB:2JDI,
FT ECO:0007744|PDB:2JIZ, ECO:0007744|PDB:2JJ1,
FT ECO:0007744|PDB:2JJ2, ECO:0007744|PDB:2V7Q,
FT ECO:0007744|PDB:2WSS, ECO:0007744|PDB:2XND,
FT ECO:0007744|PDB:4TSF, ECO:0007744|PDB:4TT3,
FT ECO:0007744|PDB:4YXW, ECO:0007744|PDB:4Z1M"
FT SITE 413
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2864455"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 76
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15999"
FT MOD_RES 161
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 161
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 167
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 167
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 204
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 230
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 230
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 240
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 261
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 261
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 305
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 305
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 427
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 427
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 434
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 498
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 498
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 506
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 506
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 531
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 531
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 539
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 539
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 541
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT CARBOHYD 76
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="V -> M (in Ref. 3; AAI16060)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="V -> I (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..33
FT /note="IAA -> VGT (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="S -> T (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="V -> M (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="E -> D (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="I -> V (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="A -> I (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> S (in Ref. 4; AAA30399)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> G (in Ref. 3; AAI16060 and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6YY0"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 283..302
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:1W0K"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 424..443
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 455..471
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:1W0K"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 504..517
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 520..528
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 534..551
FT /evidence="ECO:0007829|PDB:1W0K"
SQ SEQUENCE 553 AA; 59720 MW; 188E9531B3B815E0 CRC64;
MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE VSSILEERIL
GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG
NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKARR RVGLKAPGII
PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK
KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG
GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA
AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA
IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVISQHQ ALLSKIRTDG KISEESDAKL
KEIVTNFLAG FEA
