Q03265 (ATPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit alpha, mitochondrial

Gene names

Name:

Atp5a1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 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.
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. Interacts with BLOC1S1 By similarity.
Subcellular location	Mitochondrion inner membrane By similarity. Cell membrane; Peripheral membrane protein; Extracellular side By similarity. Note: Colocalizes with HRG on the cell surface of T-cells By similarity.
Post-translational modification	Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice. Acetylated on lysine residues. BLOC1S1 is required for acetylation By similarity.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell membrane Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro embryo development Inferred from mutant phenotype PubMed 17387143. Source: MGI lipid metabolic process Inferred from mutant phenotype PubMed 17612527. Source: MGI negative regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial proton-transporting ATP synthase complex Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW signalosome Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from mutant phenotype Ref.1. Source: MGI eukaryotic cell surface binding Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase activity, rotational mechanism Inferred from mutant phenotype PubMed 17612527. Source: MGI proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Mitochondrion By similarity
	Chain	44 – 553	510	ATP synthase subunit alpha, mitochondrial		PRO_0000002425
Regions
	Nucleotide binding	212 – 219	8	ATP By similarity
Sites
	Site	413	1	Required for activity By similarity
Amino acid modifications
	Modified residue	44	1	Pyrrolidone carboxylic acid By similarity
	Modified residue	76	1	Phosphoserine Ref.5
	Modified residue	132	1	N6-acetyllysine Ref.6
	Modified residue	161	1	N6-acetyllysine By similarity
	Modified residue	166	1	Phosphoserine By similarity
	Modified residue	230	1	N6-acetyllysine Ref.6
	Modified residue	239	1	N6-acetyllysine Ref.6
	Modified residue	261	1	N6-acetyllysine Ref.6
	Modified residue	305	1	N6-acetyllysine Ref.6
	Modified residue	427	1	N6-acetyllysine Ref.6
	Modified residue	434	1	N6-acetyllysine By similarity
	Modified residue	498	1	N6-acetyllysine Ref.6
	Modified residue	506	1	N6-acetyllysine By similarity
	Modified residue	531	1	N6-acetyllysine Ref.6
	Modified residue	539	1	N6-acetyllysine Ref.6
Experimental info
	Sequence conflict	3	1	S → T in BAE37632. Ref.2
	Sequence conflict	63	1	D → Y in BAE34114. Ref.2
	Sequence conflict	119	1	F → L in BAE34114. Ref.2
	Sequence conflict	126	1	K → N in BAE34114. Ref.2
	Sequence conflict	315	1	S → Y in BAE34114. Ref.2
	Sequence conflict	321	1	Y → C in BAE40868. Ref.2
	Sequence conflict	422 – 456	35	Missing in BAE27439. Ref.2
	Sequence conflict	486	1	A → T in BAE40158. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q03265 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: CF35B4FBA7ED431D	FASTA	553	59,753
	10 20 30 40 50 60 MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE MSSILEERIL 70 80 90 100 110 120 GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG 130 140 150 160 170 180 NDKLIKEGDV VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII 190 200 210 220 230 240 PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK 250 260 270 280 290 300 KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 310 320 330 340 350 360 RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDSFG 370 380 390 400 410 420 GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA 430 440 450 460 470 480 AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA 490 500 510 520 530 540 IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVISQHQ SLLGNIRSDG KISEQSDAKL 550 KEIVTNFLAG FEP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional expression analysis of the alpha subunit of mouse ATP synthase." Yotov W.V., St Arnaud R. Biochem. Biophys. Res. Commun. 191:142-148(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c, C57BL/6J and NOD. Tissue: Heart, Hippocampus, Liver, Spinal cord and Spleen.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[4]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 24-42; 46-83; 89-123; 133-161; 176-182; 195-204; 208-214; 219-230; 241-252; 254-261; 263-270; 306-316; 323-329; 335-347; 403-416; 435-463; 467-503; 507-527 AND 540-553. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[5]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-531 AND LYS-539, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L01062 mRNA. Translation: AAA37271.1. AK043976 mRNA. Translation: BAC31722.1. AK076572 mRNA. Translation: BAC36399.1. AK146797 mRNA. Translation: BAE27439.1. AK150426 mRNA. Translation: BAE29549.1. AK150843 mRNA. Translation: BAE29901.1. AK151004 mRNA. Translation: BAE30027.1. AK151128 mRNA. Translation: BAE30136.1. AK151224 mRNA. Translation: BAE30216.1. AK151920 mRNA. Translation: BAE30798.1. AK152054 mRNA. Translation: BAE30910.1. AK152890 mRNA. Translation: BAE31573.1. AK157529 mRNA. Translation: BAE34114.1. AK159540 mRNA. Translation: BAE35167.1. AK159491 mRNA. Translation: BAE35125.1. AK159758 mRNA. Translation: BAE35349.1. AK160043 mRNA. Translation: BAE35585.1. AK164110 mRNA. Translation: BAE37632.1. AK164193 mRNA. Translation: BAE37675.1. AK166709 mRNA. Translation: BAE38962.1. AK166812 mRNA. Translation: BAE39039.1. AK167159 mRNA. Translation: BAE39300.1. AK167863 mRNA. Translation: BAE39881.1. AK168198 mRNA. Translation: BAE40158.1. AK168617 mRNA. Translation: BAE40482.1. AK168879 mRNA. Translation: BAE40697.1. AK168890 mRNA. Translation: BAE40707.1. AK168932 mRNA. Translation: BAE40744.1. AK169080 mRNA. Translation: BAE40864.1. AK169084 mRNA. Translation: BAE40868.1. AK169105 mRNA. Translation: BAE40887.1. AK169142 mRNA. Translation: BAE40921.1. AK169300 mRNA. Translation: BAE41056.1. AK169308 mRNA. Translation: BAE41063.1. AK169414 mRNA. Translation: BAE41160.1. BC014854 mRNA. Translation: AAH14854.1.
IPI	IPI00130280.
PIR	JC1473.
RefSeq	NP_031531.1. NM_007505.2.
UniGene	Mm.276137.
3D structure databases
ProteinModelPortal	Q03265.
SMR	Q03265. Positions 56-552.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q03265. 9 interactions.
PTM databases
PhosphoSite	Q03265.
2D gel databases
REPRODUCTION-2DPAGE	IPI00130280. Q03265.
SWISS-2DPAGE	Q03265.
UCD-2DPAGE	Q03265.
Proteomic databases
PaxDb	Q03265.
PRIDE	Q03265.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
GeneID	11946.
KEGG	mmu:11946.
UCSC	uc008fru.1. mouse.
Organism-specific databases
CTD	498.
MGI	MGI:88115. Atp5a1.
Phylogenomic databases
eggNOG	COG0056.
GeneTree	ENSGT00550000074846.
HOVERGEN	HBG001536.
InParanoid	Q03265.
KO	K02132.
OMA	HDHLKTK.
OrthoDB	EOG4ZCT48.
Gene expression databases
ArrayExpress	Q03265.
Bgee	Q03265.
Genevestigator	Q03265.
GermOnline	ENSMUSG00000025428. Mus musculus.
Family and domain databases
Gene3D	2.40.30.20. 1 hit.
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. [Graphical view]
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5A1. mouse.
NextBio	280057.
SOURCE	Search...

Entry information

Entry name

ATPA_MOUSE

Accession

Primary (citable) accession number: Q03265
Secondary accession number(s): Q3TFN0 , Q3THN8, Q3TPR0, Q3TPV3, Q3TZU3, Q3UIR7, Q543Y6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program