ATP synthase subunit alpha, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P25705 (ATPA_HUMAN)

Last modified November 24, 2009. Version 120. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
ATP synthase subunit alpha, mitochondrial

Gene names

Name:	ATP5A1
Synonyms:	ATP5A, ATP5AL2, ATPM

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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. Ref.9
Subcellular location	Mitochondrion inner membrane. Note: Peripheral membrane protein.
Tissue specificity	Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. Ref.2
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

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Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	embryonic development Inferred from sequence or structural similarity. Source: UniProtKB lipid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial ATP synthesis coupled proton transport Inferred by curator. Source: UniProtKB negative regulation of endothelial cell proliferation Inferred from mutant phenotype. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from Experiment. Source: Reactome plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB MHC class I protein binding Inferred from direct assay. Source: UniProtKB eukaryotic cell surface binding Inferred from direct assay. Source: UniProtKB hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from sequence or structural similarity. Source: UniProtKB proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIRT3	Q9NTG7	1	EBI-351437,EBI-724621

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 43

Mitochondrion By similarity

Chain

44 – 553

510

ATP synthase subunit alpha, mitochondrial

PRO_0000002424

Regions

Nucleotide binding

212 – 219

ATP By similarity

Sites

Site

413

Required for activity By similarity

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid By similarity

Modified residue

Phosphoserine By similarity

Modified residue

132

N6-acetyllysine By similarity

Modified residue

161

N6-acetyllysine Ref.11

Modified residue

230

N6-acetyllysine By similarity

Modified residue

239

N6-acetyllysine By similarity

Modified residue

261

N6-acetyllysine Ref.11

Modified residue

305

N6-acetyllysine Ref.11

Modified residue

427

N6-acetyllysine By similarity

Modified residue

434

N6-acetyllysine Ref.11

Modified residue

498

N6-acetyllysine Ref.11

Modified residue

506

N6-acetyllysine Ref.11

Modified residue

531

N6-acetyllysine By similarity

Modified residue

539

N6-acetyllysine Ref.11

Natural variations

Natural variant

A → S: dbSNP rs2228437.

VAR_048369

Natural variant

223

I → V: dbSNP rs2228436.

VAR_048370

Experimental info

Sequence conflict

329

R → L in AAH39135. Ref.5

Sequence conflict

510

A → D in AAH11384. Ref.5

Sequence conflict

529

D → E in AAH11384. Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P25705-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: AA47BBB8EDA77EAC
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FASTA

553

59,751

        10         20         30         40         50         60 
MLSVRVAAAV VRALPRRAGL VSRNALGSSF IAARNFHASN THLQKTGTAE MSSILEERIL 

        70         80         90        100        110        120 
GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG 

       130        140        150        160        170        180 
NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII 

       190        200        210        220        230        240 
PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGSDEKK 

       250        260        270        280        290        300 
KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 

       310        320        330        340        350        360 
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG 

       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 FLSHVVSQHQ ALLGTIRADG KISEQSDAKL 

       550 
KEIVTNFLAG FEA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA for the alpha subunit of human mitochondrial ATP synthase." Kataoka H., Biswas C. Biochim. Biophys. Acta 1089:393-395(1991) [PubMed: 1830491] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung tumor.
[2]	"Amplification of the gene encoding the alpha-subunit of the mitochondrial ATP synthase complex in a human retinoblastoma cell line." Godbout R., Bisgrove D.A., Honore L.H., Day R.S. III Gene 123:195-201(1993) [PubMed: 8428659] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Retinoblastoma.
[3]	"Gene structure and cell type-specific expression of the human ATP synthase alpha subunit." Akiyama S., Endo H., Inohara N., Ohta S., Kagawa Y. Biochim. Biophys. Acta 1219:129-140(1994) [PubMed: 8086450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Colon tumor.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung, Retina and Uterus.
[6]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-83; 89-103; 134-161; 176-182; 219-230; 242-252; 306-316; 335-347; 403-416; 435-463 AND 507-527, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]	Bienvenut W.V. Submitted (MAR-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-73; 104-123; 134-161; 219-230; 232-239; 306-316; 335-347; 403-416; 442-463 AND 507-527, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"The major protein expression profile and two-dimensional protein database of human heart." Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K. Electrophoresis 16:1160-1169(1995) [PubMed: 7498159] [Abstract] Cited for: PROTEIN SEQUENCE OF 134-141 AND 335-339. Tissue: Heart.
[9]	"Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria." Wang Z.-G., White P.S., Ackerman S.H. J. Biol. Chem. 276:30773-30778(2001) [PubMed: 11410595] [Abstract] Cited for: INTERACTION WITH ATPAF2.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-261; LYS-305; LYS-434; LYS-498; LYS-506 AND LYS-539, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X59066 mRNA. Translation: CAA41789.1. X65460 mRNA. Translation: CAA46452.1. D14710 mRNA. Translation: BAA03531.1. D28126 Genomic DNA. Translation: BAA05672.1. BT007209 mRNA. Translation: AAP35873.1. BC003119 mRNA. Translation: AAH03119.1. BC007299 mRNA. Translation: AAH07299.1. BC008028 mRNA. Translation: AAH08028.2. BC011384 mRNA. Translation: AAH11384.1. BC016046 mRNA. Translation: AAH16046.1. BC019310 mRNA. Translation: AAH19310.1. BC039135 mRNA. Translation: AAH39135.2. BC064562 mRNA. Translation: AAH64562.1. BC067385 mRNA. Translation: AAH67385.1.
IPI	IPI00440493.
PIR	PWHUA. S17193.
RefSeq	NP_001001937.1. NP_004037.1.
UniGene	Hs.298280
3D structure databases
SMR	P25705. Positions 64-553.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25705. 14 interactions.
STRING	P25705.
PTM databases
PhosphoSite	P25705.
2-D gel databases
HSC-2DPAGE	P25705.
OGP	P25705.
REPRODUCTION-2DPAGE	P25705.
Proteomic databases
PRIDE	P25705.
Genome annotation databases
Ensembl	ENST00000282050; ENSP00000282050; ENSG00000152234; Homo sapiens. [Genome view] ENST00000398752; ENSP00000381736; ENSG00000152234; Homo sapiens. [Genome view]
GeneID	498.
KEGG	hsa:498.
UCSC	uc002lbr.1. human.
Organism-specific databases
CTD	498.
GeneCards	GC18M041918.
H-InvDB	HIX0014426.
HGNC	HGNC:823. ATP5A1.
HPA	CAB013067.
MIM	164360. gene.
PharmGKB	PA25115.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P25705.
HOVERGEN	P25705.
OMA	TKQTLNR
OrthoDB	EOG99S8SS
Enzyme and pathway databases
Reactome	REACT_1505. Integration of energy metabolism. REACT_15380. Diabetes pathways. REACT_1698. Metablism of nucleotides.
Gene expression databases
ArrayExpress	P25705.
Bgee	P25705.
CleanEx	HS_ATP5A1.
Genevestigator	P25705.
GermOnline	ENSG00000152234. Homo sapiens.
Family and domain databases
InterPro	IPR005294. ATPase_F1-cplx_asu. IPR018118. ATPase_F1/A1-cplx_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. 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]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	2089.
PMAP-CutDB	P25705.
SOURCE	Search...

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Entry information

Entry name

ATPA_HUMAN

Accession

Primary (citable) accession number: P25705
Secondary accession number(s): Q53XX6

Q9BTV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	November 24, 2009
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents