ATPA_MOUSE
ID ATPA_MOUSE Reviewed; 553 AA.
AC Q03265; Q3TFN0; Q3THN8; Q3TPR0; Q3TPV3; Q3TZU3; Q3UIR7; Q543Y6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 215.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916601; DOI=10.1006/bbrc.1993.1195;
RA Yotov W.V., St Arnaud R.;
RT "Cloning and functional expression analysis of the alpha subunit of mouse
RT ATP synthase.";
RL Biochem. Biophys. Res. Commun. 191:142-148(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Heart, Hippocampus, Liver, Spinal cord, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 24-42; 46-83; 89-123; 133-161; 176-182; 195-204;
RP 208-214; 219-230; 241-252; 254-261; 263-270; 306-316; 323-329; 335-347;
RP 403-416; 435-463; 467-503; 507-527 AND 540-553.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15648052; DOI=10.1002/pmic.200401066;
RA Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA Hart G.W., Burlingame A.L.;
RT "Quantitative analysis of both protein expression and serine / threonine
RT post-translational modifications through stable isotope labeling with
RT dithiothreitol.";
RL Proteomics 5:388-398(2005).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH S100A1.
RX PubMed=17438143; DOI=10.1128/mcb.02045-06;
RA Boerries M., Most P., Gledhill J.R., Walker J.E., Katus H.A., Koch W.J.,
RA Aebi U., Schoenenberger C.A.;
RT "Ca2+ -dependent interaction of S100A1 with F1-ATPase leads to an increased
RT ATP content in cardiomyocytes.";
RL Mol. Cell. Biol. 27:4365-4373(2007).
RN [7]
RP INTERACTION WITH CLN5 AND PPT1.
RX PubMed=19941651; DOI=10.1186/1471-2121-10-83;
RA Lyly A., von Schantz C., Heine C., Schmiedt M.L., Sipilae T., Jalanko A.,
RA Kyttaelae A.;
RT "Novel interactions of CLN5 support molecular networking between neuronal
RT ceroid lipofuscinosis proteins.";
RL BMC Cell Biol. 10:83-83(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-106 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539,
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239;
RP LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161;
RP LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434;
RP LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 (By
CC similarity). Binds the bacterial siderophore enterobactin and can
CC promote mitochondrial accumulation of enterobactin-derived iron ions
CC (By similarity). {ECO:0000250|UniProtKB:P19483,
CC ECO:0000250|UniProtKB:P25705}.
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). CF(0) has three main
CC subunits: a, b and c (By similarity). Interacts with ATPAF2. Interacts
CC with HRG; the interaction occurs on the surface of T-cells and alters
CC the cell morphology when associated with concanavalin (in vitro).
CC Interacts with PLG (angiostatin peptide); the interaction inhibits most
CC of the angiogenic properties of angiostatin (By similarity). Component
CC of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E,
CC ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B,
CC ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity).
CC Interacts with BLOC1S1 (By similarity). Interacts with BCL2L1 isoform
CC BCL-X(L); the interaction mediates the association of BCL2L1 isoform
CC BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and
CC enhances neurons metabolic efficiency (By similarity). Interacts with
CC CLN5 and PPT1 (PubMed:19941651). Interacts with S100A1; this
CC interaction increases F1-ATPase activity (PubMed:17438143). Interacts
CC with ABCB7; this interaction allows the regulation of cellular iron
CC homeostasis and cellular reactive oxygen species (ROS) levels in
CC cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P15999,
CC ECO:0000250|UniProtKB:P19483, ECO:0000250|UniProtKB:P25705,
CC ECO:0000269|PubMed:17438143, ECO:0000269|PubMed:19941651}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17438143}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17438143}; Matrix side
CC {ECO:0000250|UniProtKB:P19483}. 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 -!- PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation
CC (By similarity). Acetylation of Lys-132, Lys-230 and Lys-498 is
CC observed in liver mitochondria from fasted mice but not from fed mice.
CC {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; L01062; AAA37271.1; -; mRNA.
DR EMBL; AK043976; BAC31722.1; -; mRNA.
DR EMBL; AK076572; BAC36399.1; -; mRNA.
DR EMBL; AK146797; BAE27439.1; -; mRNA.
DR EMBL; AK150426; BAE29549.1; -; mRNA.
DR EMBL; AK150843; BAE29901.1; -; mRNA.
DR EMBL; AK151004; BAE30027.1; -; mRNA.
DR EMBL; AK151128; BAE30136.1; -; mRNA.
DR EMBL; AK151224; BAE30216.1; -; mRNA.
DR EMBL; AK151920; BAE30798.1; -; mRNA.
DR EMBL; AK152054; BAE30910.1; -; mRNA.
DR EMBL; AK152890; BAE31573.1; -; mRNA.
DR EMBL; AK157529; BAE34114.1; -; mRNA.
DR EMBL; AK159540; BAE35167.1; -; mRNA.
DR EMBL; AK159491; BAE35125.1; -; mRNA.
DR EMBL; AK159758; BAE35349.1; -; mRNA.
DR EMBL; AK160043; BAE35585.1; -; mRNA.
DR EMBL; AK164110; BAE37632.1; -; mRNA.
DR EMBL; AK164193; BAE37675.1; -; mRNA.
DR EMBL; AK166709; BAE38962.1; -; mRNA.
DR EMBL; AK166812; BAE39039.1; -; mRNA.
DR EMBL; AK167159; BAE39300.1; -; mRNA.
DR EMBL; AK167863; BAE39881.1; -; mRNA.
DR EMBL; AK168198; BAE40158.1; -; mRNA.
DR EMBL; AK168617; BAE40482.1; -; mRNA.
DR EMBL; AK168879; BAE40697.1; -; mRNA.
DR EMBL; AK168890; BAE40707.1; -; mRNA.
DR EMBL; AK168932; BAE40744.1; -; mRNA.
DR EMBL; AK169080; BAE40864.1; -; mRNA.
DR EMBL; AK169084; BAE40868.1; -; mRNA.
DR EMBL; AK169105; BAE40887.1; -; mRNA.
DR EMBL; AK169142; BAE40921.1; -; mRNA.
DR EMBL; AK169300; BAE41056.1; -; mRNA.
DR EMBL; AK169308; BAE41063.1; -; mRNA.
DR EMBL; AK169414; BAE41160.1; -; mRNA.
DR EMBL; BC014854; AAH14854.1; -; mRNA.
DR CCDS; CCDS29358.1; -.
DR PIR; JC1473; JC1473.
DR RefSeq; NP_031531.1; NM_007505.2.
DR AlphaFoldDB; Q03265; -.
DR SMR; Q03265; -.
DR BioGRID; 198253; 105.
DR IntAct; Q03265; 33.
DR MINT; Q03265; -.
DR STRING; 10090.ENSMUSP00000026495; -.
DR CarbonylDB; Q03265; -.
DR GlyGen; Q03265; 1 site.
DR iPTMnet; Q03265; -.
DR PhosphoSitePlus; Q03265; -.
DR SwissPalm; Q03265; -.
DR REPRODUCTION-2DPAGE; IPI00130280; -.
DR REPRODUCTION-2DPAGE; Q03265; -.
DR SWISS-2DPAGE; Q03265; -.
DR UCD-2DPAGE; Q03265; -.
DR CPTAC; non-CPTAC-3765; -.
DR EPD; Q03265; -.
DR jPOST; Q03265; -.
DR MaxQB; Q03265; -.
DR PaxDb; Q03265; -.
DR PeptideAtlas; Q03265; -.
DR PRIDE; Q03265; -.
DR ProteomicsDB; 277216; -.
DR Antibodypedia; 22447; 348 antibodies from 35 providers.
DR DNASU; 11946; -.
DR Ensembl; ENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
DR GeneID; 11946; -.
DR KEGG; mmu:11946; -.
DR UCSC; uc008fru.1; mouse.
DR CTD; 11946; -.
DR MGI; MGI:88115; Atp5a1.
DR VEuPathDB; HostDB:ENSMUSG00000025428; -.
DR eggNOG; KOG1353; Eukaryota.
DR GeneTree; ENSGT00550000074846; -.
DR InParanoid; Q03265; -.
DR OMA; MEVFTQF; -.
DR OrthoDB; 470054at2759; -.
DR PhylomeDB; Q03265; -.
DR TreeFam; TF300321; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 11946; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Atp5a1; mouse.
DR PRO; PR:Q03265; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q03265; protein.
DR Bgee; ENSMUSG00000025428; Expressed in heart and 115 other tissues.
DR ExpressionAtlas; Q03265; baseline and differential.
DR Genevisible; Q03265; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); ISO:MGI.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; ISO:MGI.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0043532; F:angiostatin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IMP:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
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 Acetylation; ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW Direct protein sequencing; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Methylation; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT CHAIN 44..553
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000002425"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT BINDING 473..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT SITE 413
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 76
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:15648052"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
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:0007744|PubMed:23576753"
FT MOD_RES 161
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:23576753"
FT MOD_RES 167
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:24129315"
FT MOD_RES 230
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 230
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 240
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 261
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 261
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 305
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 305
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 427
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 427
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 434
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 498
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 498
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 506
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 506
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 531
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 531
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 539
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 539
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 541
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CARBOHYD 76
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="S -> T (in Ref. 2; BAE37632)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="D -> Y (in Ref. 2; BAE34114)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="F -> L (in Ref. 2; BAE34114)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="K -> N (in Ref. 2; BAE34114)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="S -> Y (in Ref. 2; BAE34114)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="Y -> C (in Ref. 2; BAE40868)"
FT /evidence="ECO:0000305"
FT CONFLICT 422..456
FT /note="Missing (in Ref. 2; BAE27439)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="A -> T (in Ref. 2; BAE40158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 59753 MW; CF35B4FBA7ED431D CRC64;
MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE MSSILEERIL
GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG
NDKLIKEGDV VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII
PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK
KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDSFG
GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA
AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA
IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVISQHQ SLLGNIRSDG KISEQSDAKL
KEIVTNFLAG FEP
