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 27-MAR-2024, entry version 224. 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, RC Pancreas, 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 ATP5MPL (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}. 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; 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; 109. DR IntAct; Q03265; 33. DR MINT; Q03265; -. DR STRING; 10090.ENSMUSP00000026495; -. DR CarbonylDB; Q03265; -. DR GlyCosmos; Q03265; 1 site, No reported glycans. DR GlyGen; Q03265; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q03265; -. DR MetOSite; Q03265; -. DR PhosphoSitePlus; Q03265; -. DR SwissPalm; Q03265; -. DR REPRODUCTION-2DPAGE; IPI00130280; -. DR REPRODUCTION-2DPAGE; Q03265; -. DR CPTAC; non-CPTAC-3765; -. DR EPD; Q03265; -. DR jPOST; Q03265; -. DR MaxQB; Q03265; -. DR PaxDb; 10090-ENSMUSP00000026495; -. DR PeptideAtlas; Q03265; -. DR ProteomicsDB; 277216; -. DR Pumba; Q03265; -. DR Antibodypedia; 22447; 421 antibodies from 35 providers. DR DNASU; 11946; -. DR Ensembl; ENSMUST00000026495.15; ENSMUSP00000026495.9; ENSMUSG00000025428.16. DR GeneID; 11946; -. DR KEGG; mmu:11946; -. DR UCSC; uc008fru.1; mouse. DR AGR; MGI:88115; -. DR CTD; 498; -. DR MGI; MGI:88115; Atp5f1a. DR VEuPathDB; HostDB:ENSMUSG00000025428; -. DR eggNOG; KOG1353; Eukaryota. DR GeneTree; ENSGT00550000074846; -. DR InParanoid; Q03265; -. DR OMA; INQRDNW; -. DR OrthoDB; 1102723at2759; -. 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 77 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 117 other cell types or tissues. DR ExpressionAtlas; Q03265; baseline and differential. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl. 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: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; IEA:Ensembl. 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:0006754; P:ATP biosynthetic 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; 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 SWISS-2DPAGE; Q03265; -. DR UCD-2DPAGE; Q03265; -. DR Genevisible; Q03265; MM. 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 //