UniProt Accession

 ATPA_MOUSE; Q03265; Q3TFN0; Q3THN8; Q3TPR0; Q3TPV3; Q3TZU3; Q3UIR7; Q543Y6 

Genbank Protein ID

 L01062; AK043976; AK076572; AK146797; AK150426; AK150843; AK151004; AK151128; AK151224; AK151920; AK152054; AK152890; AK157529; AK159540; AK159491; AK159758; AK160043; AK164110; AK164193; AK166709; AK166812; AK167159; AK167863; AK168198; AK168617; AK168879; AK168890; AK168932; AK169080; AK169084; AK169105; AK169142; AK169300; AK169308; AK169414; BC014854 

Genbank Nucleotide ID

 AAA37271.1; BAC31722.1; BAC36399.1; BAE27439.1; BAE29549.1; BAE29901.1; BAE30027.1; BAE30136.1; BAE30216.1; BAE30798.1; BAE30910.1; BAE31573.1; BAE34114.1; BAE35167.1; BAE35125.1; BAE35349.1; BAE35585.1; BAE37632.1; BAE37675.1; BAE38962.1; BAE39039.1; BAE39300.1; BAE39881.1; BAE40158.1; BAE40482.1; BAE40697.1; BAE40707.1; BAE40744.1; BAE40864.1; BAE40868.1; BAE40887.1; BAE40921.1; BAE41056.1; BAE41063.1; BAE41160.1; AAH14854.1 

Protein Name

 ATP synthase subunit alpha, mitochondrial 

Protein Synonyms/Alias

  

Gene Name

 Atp5a1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
45	ASNTRLQKTGTAEMS	ubiquitination	[1]
123	VVVFGNDKLIKEGDV	ubiquitination	[1]
126	FGNDKLIKEGDVVKR	acetylation	[2]
132	IKEGDVVKRTGAIVD	acetylation	[2, 3]
161	LGNAIDGKGPIGSKT	acetylation	[2]
161	LGNAIDGKGPIGSKT	ubiquitination	[1]
167	GKGPIGSKTRRRVGL	acetylation	[2]
167	GKGPIGSKTRRRVGL	ubiquitination	[1]
175	TRRRVGLKAPGIIPR	ubiquitination	[1]
194	EPMQTGIKAVDSLVP	ubiquitination	[1]
218	IGDRQTGKTSIAIDT	ubiquitination	[1]
230	IDTIINQKRFNDGTD	acetylation	[2, 3]
230	IDTIINQKRFNDGTD	ubiquitination	[1]
239	FNDGTDEKKKLYCIY	acetylation	[2, 3]
240	NDGTDEKKKLYCIYV	acetylation	[2]
261	STVAQLVKRLTDADA	acetylation	[2, 3]
261	STVAQLVKRLTDADA	ubiquitination	[1]
305	EYFRDNGKHALIIYD	acetylation	[2, 3]
305	EYFRDNGKHALIIYD	ubiquitination	[1]
316	IIYDDLSKQAVAYRQ	acetylation	[2]
427	AAQTRAMKQVAGTMK	acetylation	[2, 3]
427	AAQTRAMKQVAGTMK	ubiquitination	[1]
434	KQVAGTMKLELAQYR	acetylation	[2]
434	KQVAGTMKLELAQYR	ubiquitination	[1]
498	GVRGYLDKLEPSKIT	acetylation	[2, 3]
498	GVRGYLDKLEPSKIT	ubiquitination	[1]
503	LDKLEPSKITKFENA	acetylation	[2]
503	LDKLEPSKITKFENA	ubiquitination	[1]
506	LEPSKITKFENAFLS	acetylation	[2]
531	GNIRSDGKISEQSDA	acetylation	[2, 3]
539	ISEQSDAKLKEIVTN	acetylation	[2, 3]
539	ISEQSDAKLKEIVTN	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647] 

Functional Description

 Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). 

Sequence Annotation

 NP_BIND 212 219 ATP (By similarity).
 MOD_RES 44 44 Pyrrolidone carboxylic acid (By
 MOD_RES 76 76 Phosphoserine.
 MOD_RES 132 132 N6-acetyllysine.
 MOD_RES 161 161 N6-acetyllysine (By similarity).
 MOD_RES 166 166 Phosphoserine (By similarity).
 MOD_RES 230 230 N6-acetyllysine.
 MOD_RES 239 239 N6-acetyllysine.
 MOD_RES 261 261 N6-acetyllysine.
 MOD_RES 305 305 N6-acetyllysine.
 MOD_RES 427 427 N6-acetyllysine.
 MOD_RES 434 434 N6-acetyllysine (By similarity).
 MOD_RES 498 498 N6-acetyllysine.
 MOD_RES 506 506 N6-acetyllysine (By similarity).
 MOD_RES 531 531 N6-acetyllysine.
 MOD_RES 539 539 N6-acetyllysine.  

Keyword

 Acetylation; ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Transit peptide; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 553 AA 

Protein Sequence

Gene Ontology

 GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0005524; F:ATP binding; IMP:MGI.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:MGI.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
 GO:0009790; P:embryo development; IMP:MGI.
 GO:0006629; P:lipid metabolic process; IMP:MGI.
 GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Compara. 

Interpro

 IPR020003; ATPase_a/bsu_AS.
 IPR004100; ATPase_a/bsu_N.
 IPR005294; ATPase_F1-cplx_asu.
 IPR023366; ATPase_F1/A1-cplx_a_su_N.
 IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
 IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
 IPR027417; P-loop_NTPase. 

Pfam

 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N 

SMART

  

PROSITE

 PS00152; ATPASE_ALPHA_BETA 

PRINTS