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Q03265 (ATPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit alpha, mitochondrial
Gene names
Name:Atp5a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCell membrane
CF(1)
Membrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP 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_componentCOP9 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 14651853PubMed 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_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion By similarity
Chain44 – 553510ATP synthase subunit alpha, mitochondrial HAMAP-Rule MF_01346
PRO_0000002425

Regions

Nucleotide binding212 – 2198ATP By similarity

Sites

Site4131Required for activity By similarity

Amino acid modifications

Modified residue441Pyrrolidone carboxylic acid By similarity
Modified residue761Phosphoserine Ref.5
Modified residue1231N6-acetyllysine Ref.7
Modified residue1261N6-acetyllysine Ref.7
Modified residue1321N6-acetyllysine Ref.7
Modified residue1611N6-acetyllysine; alternate Ref.7
Modified residue1611N6-succinyllysine; alternate Ref.6
Modified residue1661Phosphoserine By similarity
Modified residue1671N6-acetyllysine; alternate Ref.7
Modified residue1671N6-succinyllysine; alternate Ref.6
Modified residue2301N6-acetyllysine; alternate Ref.7
Modified residue2301N6-succinyllysine; alternate Ref.6
Modified residue2391N6-acetyllysine; alternate Ref.7
Modified residue2391N6-succinyllysine; alternate Ref.6
Modified residue2401N6-acetyllysine Ref.7
Modified residue2611N6-acetyllysine; alternate Ref.7
Modified residue2611N6-succinyllysine; alternate Ref.6
Modified residue3051N6-acetyllysine; alternate Ref.7
Modified residue3051N6-succinyllysine; alternate Ref.6
Modified residue4271N6-acetyllysine; alternate Ref.7
Modified residue4271N6-succinyllysine; alternate Ref.6
Modified residue4341N6-acetyllysine Ref.7
Modified residue4981N6-acetyllysine; alternate Ref.6 Ref.7
Modified residue4981N6-succinyllysine; alternate Ref.6
Modified residue5061N6-acetyllysine; alternate Ref.7
Modified residue5061N6-succinyllysine; alternate Ref.6
Modified residue5311N6-acetyllysine; alternate Ref.6 Ref.7
Modified residue5311N6-succinyllysine; alternate Ref.6
Modified residue5391N6-acetyllysine; alternate Ref.6 Ref.7
Modified residue5391N6-succinyllysine; alternate Ref.6
Modified residue5411N6-acetyllysine Ref.7

Experimental info

Sequence conflict31S → T in BAE37632. Ref.2
Sequence conflict631D → Y in BAE34114. Ref.2
Sequence conflict1191F → L in BAE34114. Ref.2
Sequence conflict1261K → N in BAE34114. Ref.2
Sequence conflict3151S → Y in BAE34114. Ref.2
Sequence conflict3211Y → C in BAE40868. Ref.2
Sequence conflict422 – 45635Missing in BAE27439. Ref.2
Sequence conflict4861A → T in BAE40158. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q03265 [UniParc].

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

FASTA55359,753
        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' 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. expand/collapse author list , 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, 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.
CCDSCCDS29358.1.
PIRJC1473.
RefSeqNP_031531.1. NM_007505.2.
UniGeneMm.276137.

3D structure databases

ProteinModelPortalQ03265.
SMRQ03265. Positions 56-552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198253. 13 interactions.
IntActQ03265. 18 interactions.
MINTMINT-1859704.

PTM databases

PhosphoSiteQ03265.

2D gel databases

REPRODUCTION-2DPAGEIPI00130280.
Q03265.
SWISS-2DPAGEQ03265.
UCD-2DPAGEQ03265.

Proteomic databases

MaxQBQ03265.
PaxDbQ03265.
PRIDEQ03265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
GeneID11946.
KEGGmmu:11946.
UCSCuc008fru.1. mouse.

Organism-specific databases

CTD498.
MGIMGI:88115. Atp5a1.

Phylogenomic databases

eggNOGCOG0056.
GeneTreeENSGT00550000074846.
HOVERGENHBG001536.
InParanoidQ03265.
KOK02132.
OMATPYPVED.
OrthoDBEOG773XFP.
PhylomeDBQ03265.
TreeFamTF300321.

Gene expression databases

BgeeQ03265.
GenevestigatorQ03265.

Family and domain databases

Gene3D2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01346. ATP_synth_alpha_bact.
InterProIPR020003. 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]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00962. atpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5A1. mouse.
NextBio280057.
PROQ03265.
SOURCESearch...

Entry information

Entry nameATPA_MOUSE
AccessionPrimary (citable) accession number: Q03265
Secondary accession number(s): Q3TFN0 expand/collapse secondary AC list , Q3THN8, Q3TPR0, Q3TPV3, Q3TZU3, Q3UIR7, 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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