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 24-JAN-2024, entry version 202. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-11001; -. DR EMDB; EMD-11039; -. DR EMDB; EMD-11040; -. DR EMDB; EMD-11228; -. DR EMDB; EMD-11229; -. DR EMDB; EMD-11230; -. DR EMDB; EMD-11342; -. DR EMDB; EMD-11368; -. DR EMDB; EMD-11369; -. DR EMDB; EMD-11428; -. DR EMDB; EMD-11429; -. DR EMDB; EMD-11430; -. DR SMR; P19483; -. DR CORUM; P19483; -. DR DIP; DIP-35479N; -. DR IntAct; P19483; 9. DR MINT; P19483; -. DR STRING; 9913.ENSBTAP00000003259; -. DR GlyCosmos; P19483; 1 site, No reported glycans. DR PaxDb; 9913-ENSBTAP00000003259; -. DR PeptideAtlas; P19483; -. DR GeneID; 282578; -. DR KEGG; bta:282578; -. DR CTD; 498; -. DR eggNOG; KOG1353; Eukaryota. DR InParanoid; P19483; -. 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; cd18116; ATP-synt_F1_alpha_N; 1. DR CDD; cd01132; F1-ATPase_alpha_CD; 1. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_nt-bd_dom. 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 NCBIfam; TIGR00962; atpA; 1. DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. DR UCD-2DPAGE; P19483; -. 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 //