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P19483 (ATPA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 142. 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
Synonyms:ATP5A2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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). 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. Ref.6

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

Tissue specificity

Heart and liver.

Post-translational modification

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion Ref.5
Chain44 – 553510ATP synthase subunit alpha, mitochondrial HAMAP-Rule MF_01346
PRO_0000002423

Regions

Nucleotide binding212 – 2198ATP By similarity

Sites

Site4131Required for activity By similarity

Amino acid modifications

Modified residue441Pyrrolidone carboxylic acid HAMAP-Rule MF_01346
Modified residue761Phosphoserine By similarity
Modified residue1231N6-acetyllysine By similarity
Modified residue1261N6-acetyllysine By similarity
Modified residue1321N6-acetyllysine By similarity
Modified residue1611N6-acetyllysine; alternate By similarity
Modified residue1611N6-succinyllysine; alternate By similarity
Modified residue1661Phosphoserine By similarity
Modified residue1671N6-acetyllysine; alternate By similarity
Modified residue1671N6-succinyllysine; alternate By similarity
Modified residue2301N6-acetyllysine; alternate By similarity
Modified residue2301N6-succinyllysine; alternate By similarity
Modified residue2391N6-acetyllysine; alternate By similarity
Modified residue2391N6-succinyllysine; alternate By similarity
Modified residue2401N6-acetyllysine By similarity
Modified residue2611N6-acetyllysine; alternate By similarity
Modified residue2611N6-succinyllysine; alternate By similarity
Modified residue3051N6-acetyllysine; alternate By similarity
Modified residue3051N6-succinyllysine; alternate By similarity
Modified residue4271N6-acetyllysine; alternate By similarity
Modified residue4271N6-succinyllysine; alternate By similarity
Modified residue4341N6-acetyllysine By similarity
Modified residue4981N6-acetyllysine; alternate By similarity
Modified residue4981N6-succinyllysine; alternate By similarity
Modified residue5061N6-acetyllysine; alternate By similarity
Modified residue5061N6-succinyllysine; alternate By similarity
Modified residue5311N6-acetyllysine; alternate By similarity
Modified residue5311N6-succinyllysine; alternate By similarity
Modified residue5391N6-acetyllysine; alternate By similarity
Modified residue5391N6-succinyllysine; alternate By similarity
Modified residue5411N6-acetyllysine By similarity

Experimental info

Sequence conflict41V → M in AAI16060. Ref.3
Sequence conflict61V → I in AAA30399. Ref.4
Sequence conflict31 – 333IAA → VGT in AAA30399. Ref.4
Sequence conflict411S → T in AAA30399. Ref.4
Sequence conflict511V → M in AAA30399. Ref.4
Sequence conflict1441E → D in AAA30399. Ref.4
Sequence conflict1641I → V in AAA30399. Ref.4
Sequence conflict1681A → I in AAA30399. Ref.4
Sequence conflict3581A → S in AAA30399. Ref.4
Sequence conflict5241S → G in AAI16060. Ref.3
Sequence conflict5241S → G AA sequence Ref.5

Secondary structure

................................................................................................. 553
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19483 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 188E9531B3B815E0

FASTA55359,720
        10         20         30         40         50         60 
MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE VSSILEERIL 

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

       130        140        150        160        170        180 
NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKARR 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 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 FLSHVISQHQ ALLSKIRTDG KISEESDAKL 

       550 
KEIVTNFLAG FEA 

« Hide

References

« Hide 'large scale' references
[1]"ATP synthase from bovine mitochondria: complementary DNA sequence of the import precursor of a heart isoform of the alpha subunit."
Walker J.E., Powell S.J., Vinas O., Runswick M.J.
Biochemistry 28:4702-4708(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Structural organization of a nuclear gene for the alpha-subunit of the bovine mitochondrial ATP synthase complex."
Pierce D.J., Jordan E.M., Breen G.A.M.
Biochim. Biophys. Acta 1132:265-275(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Ascending colon.
[4]"Bovine liver cDNA clones encoding a precursor of the alpha-subunit of the mitochondrial ATP synthase complex."
Breen G.A.M.
Biochem. Biophys. Res. Commun. 152:264-269(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-359.
Tissue: Liver.
[5]"Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria."
Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.
J. Mol. Biol. 184:677-701(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 44-552.
Tissue: Heart.
[6]"Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
[7]"Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria."
Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.
Nature 370:621-628(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[8]"The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin."
Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G., Walker J.E.
Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
[9]"Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism."
Orriss G.L., Leslie A.G., Braig K., Walker J.E.
Structure 6:831-837(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[10]"The structure of bovine F1-ATPase in complex with its regulatory protein IF1."
Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.
Nat. Struct. Biol. 10:744-750(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-553 IN COMPLEX WITH ATPIF1; ATP5B AND ATP5C1.
[11]"How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria."
Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.
Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 45-553 IN COMPLEX WITH ATPIF1; ATP5B; ATP5C1; ATP5D AND ATP5E.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22465 mRNA. Translation: AAB59266.1.
X64565 Genomic DNA. Translation: CAA45865.1.
BC116059 mRNA. Translation: AAI16060.1.
M19680 mRNA. Translation: AAA30399.1.
PIRA27693.
PWBOA. S27201.
RefSeqNP_777109.1. NM_174684.2.
UniGeneBt.7194.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMFX-ray2.85A/B/C44-553[»]
1COWX-ray3.10A/B/C45-553[»]
1E1QX-ray2.61A/B/C44-553[»]
1E1RX-ray2.50A/B/C44-553[»]
1E79X-ray2.40A/B/C44-553[»]
1EFRX-ray3.10A/B/C45-553[»]
1H8EX-ray2.00A/B/C44-553[»]
1H8HX-ray2.90A/B/C44-553[»]
1NBMX-ray3.00A/B/C44-553[»]
1OHHX-ray2.80A/B/C44-553[»]
1QO1X-ray3.90A/B/C44-553[»]
1W0JX-ray2.20A/B/C44-553[»]
1W0KX-ray2.85A/B/C44-553[»]
2CK3X-ray1.90A/B/C44-553[»]
2JDIX-ray1.90A/B/C44-553[»]
2JIZX-ray2.30A/B/C/H/I/J45-553[»]
2JJ1X-ray2.70A/B/C/H/I/J45-553[»]
2JJ2X-ray2.40A/B/C/H/I/J45-553[»]
2JMXNMR-B44-68[»]
2V7QX-ray2.10A/B/C45-553[»]
2W6EX-ray6.50A/B/C1-553[»]
2W6FX-ray6.00A/B/C1-553[»]
2W6GX-ray6.00A/B/C1-553[»]
2W6HX-ray5.00A/B/C1-553[»]
2W6IX-ray4.00A/B/C1-553[»]
2W6JX-ray3.84A/B/C1-553[»]
2WSSX-ray3.20A/B/C/J/K/L44-553[»]
2XNDX-ray3.50A/B/C62-553[»]
4ASUX-ray2.60A/B/C44-553[»]
ProteinModelPortalP19483.
SMRP19483. Positions 59-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35479N.
IntActP19483. 4 interactions.
MINTMINT-5006839.
STRING9913.ENSBTAP00000003259.

2D gel databases

UCD-2DPAGEP19483.

Proteomic databases

PaxDbP19483.
PRIDEP19483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282578.
KEGGbta:282578.

Organism-specific databases

CTD498.

Phylogenomic databases

eggNOGCOG0056.
HOGENOMHOG000130111.
InParanoidP19482.
KOK02132.

Family and domain databases

Gene3D2.40.30.20. 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

EvolutionaryTraceP19483.
NextBio20806299.

Entry information

Entry nameATPA_BOVIN
AccessionPrimary (citable) accession number: P19483
Secondary accession number(s): P05629, P19482, Q1JQC4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: March 19, 2014
This is version 142 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references