ATP synthase subunit alpha, mitochondrial precursor - Atp5a1

Preferred order of sections

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

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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. HAMAP-Rule MF_01346
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. Interacts with BCL2L1 isoform BCL-X(L);the interaction mediates the association of BCL2L1 isoform BCL-X(L)with the mitochondrial membrane F₁F₀ ATP synthase and enhances neurons metabolic efficency 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. HAMAP-Rule MF_01346
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. HAMAP-Rule MF_01346 Acetylated on lysine residues. BLOC1S1 is required for acetylation By similarity. HAMAP-Rule MF_01346
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	Cell membrane CF(1) 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 lipid metabolic process Inferred from mutant phenotype PubMed 17612527. Source: MGI negative regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Ensembl
Cellular_component	COP9 signalosome Inferred from electronic annotation. Source: Ensembl mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial proton-transporting ATP synthase complex Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from direct assay PubMed 14651853 PubMed 18614015. Source: MGI 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
Molecular_function	ATP binding Inferred from mutant phenotype Ref.1. Source: MGI 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 HAMAP-Rule MF_01346

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

123

1

N6-acetyllysine Ref.7

Modified residue

126

1

N6-acetyllysine Ref.7

Modified residue

132

1

N6-acetyllysine Ref.7

Modified residue

161

1

N6-acetyllysine; alternate Ref.7

Modified residue

161

1

N6-succinyllysine; alternate Ref.6

Modified residue

166

1

Phosphoserine By similarity

Modified residue

167

1

N6-acetyllysine; alternate Ref.7

Modified residue

167

1

N6-succinyllysine; alternate Ref.6

Modified residue

230

1

N6-acetyllysine; alternate Ref.7

Modified residue

230

1

N6-succinyllysine; alternate Ref.6

Modified residue

239

1

N6-acetyllysine; alternate Ref.7

Modified residue

239

1

N6-succinyllysine; alternate Ref.6

Modified residue

240

1

N6-acetyllysine Ref.7

Modified residue

261

1

N6-acetyllysine; alternate Ref.7

Modified residue

261

1

N6-succinyllysine; alternate Ref.6

Modified residue

305

1

N6-acetyllysine; alternate Ref.7

Modified residue

305

1

N6-succinyllysine; alternate Ref.6

Modified residue

427

1

N6-acetyllysine; alternate Ref.7

Modified residue

427

1

N6-succinyllysine; alternate Ref.6

Modified residue

434

1

N6-acetyllysine Ref.7

Modified residue

498

1

N6-acetyllysine; alternate Ref.6 Ref.7

Modified residue

498

1

N6-succinyllysine; alternate Ref.6

Modified residue

506

1

N6-acetyllysine; alternate Ref.7

Modified residue

506

1

N6-succinyllysine; alternate Ref.6

Modified residue

531

1

N6-acetyllysine; alternate Ref.6 Ref.7

Modified residue

531

1

N6-succinyllysine; alternate Ref.6

Modified residue

539

1

N6-acetyllysine; alternate Ref.6 Ref.7

Modified residue

539

1

N6-succinyllysine; alternate Ref.6

Modified residue

541

1

N6-acetyllysine Ref.7

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)

Tools

Q03265 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: CF35B4FBA7ED431D
Show »

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

« Hide

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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic fibroblast and Liver.
[7]	"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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.
CCDS	CCDS29358.1.
PIR	JC1473.
RefSeq	NP_031531.1. NM_007505.2.
UniGene	Mm.276137.
3D structure databases
ProteinModelPortal	Q03265.
SMR	Q03265. Positions 56-552.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	198253. 13 interactions.
IntAct	Q03265. 18 interactions.
MINT	MINT-1859704.
PTM databases
PhosphoSite	Q03265.
2D gel databases
REPRODUCTION-2DPAGE	IPI00130280. Q03265.
SWISS-2DPAGE	Q03265.
UCD-2DPAGE	Q03265.
Proteomic databases
MaxQB	Q03265.
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	TPYPVED.
OrthoDB	EOG773XFP.
PhylomeDB	Q03265.
TreeFam	TF300321.
Gene expression databases
Bgee	Q03265.
Genevestigator	Q03265.
Family and domain databases
Gene3D	2.40.30.20. 1 hit. 3.40.50.300. 1 hit.
HAMAP	MF_01346. ATP_synth_alpha_bact.
InterPro	IPR020003. ATPase_a/bsu_AS. IPR023366. ATPase_asu-like. IPR005294. ATPase_F1-cplx_asu. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR004100. ATPase_F1_a/bsu_N. IPR027417. P-loop_NTPase. [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. SSF47917. 1 hit. SSF50615. SSF50615. 1 hit. SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5A1. mouse.
NextBio	280057.
PRO	Q03265.
SOURCE	Search...

Entry information

Entry name

ATPA_MOUSE

Accession

Primary (citable) accession number: Q03265
Secondary accession number(s): Q3TFN0

Q543Y6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents