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Protein

ATP synthase subunit alpha, mitochondrial

Gene

Atp5a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei413 – 4131Required for activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi212 – 2198ATPBy similarity

GO - Molecular functioni

  • ADP binding Source: RGD
  • ATPase activity Source: RGD
  • ATP binding Source: RGD
  • proton-transporting ATPase activity, rotational mechanism Source: InterPro
  • proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrial
Gene namesi
Name:Atp5a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619993. Atp5a1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: RGD
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
  • mitochondrion Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2176795.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionAdd
BLAST
Chaini44 – 553510ATP synthase subunit alpha, mitochondrialPRO_0000002427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Pyrrolidone carboxylic acidBy similarity
Modified residuei53 – 531PhosphoserineBy similarity
Modified residuei76 – 761Phosphoserine; alternateBy similarity
Glycosylationi76 – 761O-linked (GlcNAc); alternate1 Publication
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei132 – 1321N6-acetyllysineBy similarity
Modified residuei134 – 1341PhosphothreonineCombined sources
Modified residuei161 – 1611N6-acetyllysine; alternateBy similarity
Modified residuei161 – 1611N6-succinyllysine; alternateBy similarity
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
Modified residuei230 – 2301N6-acetyllysine; alternateBy similarity
Modified residuei230 – 2301N6-succinyllysine; alternateBy similarity
Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
Modified residuei240 – 2401N6-acetyllysineBy similarity
Modified residuei261 – 2611N6-acetyllysine; alternateBy similarity
Modified residuei261 – 2611N6-succinyllysine; alternateBy similarity
Modified residuei305 – 3051N6-acetyllysine; alternateBy similarity
Modified residuei305 – 3051N6-succinyllysine; alternateBy similarity
Modified residuei427 – 4271N6-acetyllysine; alternateBy similarity
Modified residuei427 – 4271N6-succinyllysine; alternateBy similarity
Modified residuei434 – 4341N6-acetyllysineBy similarity
Modified residuei498 – 4981N6-acetyllysine; alternateBy similarity
Modified residuei498 – 4981N6-succinyllysine; alternateBy similarity
Modified residuei506 – 5061N6-acetyllysine; alternateBy similarity
Modified residuei506 – 5061N6-succinyllysine; alternateBy similarity
Modified residuei531 – 5311N6-acetyllysine; alternateBy similarity
Modified residuei531 – 5311N6-succinyllysine; alternateBy similarity
Modified residuei539 – 5391N6-acetyllysine; alternateBy similarity
Modified residuei539 – 5391N6-succinyllysine; alternateBy similarity
Modified residuei541 – 5411N6-acetyllysineBy similarity

Post-translational modificationi

Acetylated on lysine residues. BLOC1S1 is required for acetylation (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP15999.
PRIDEiP15999.

2D gel databases

World-2DPAGE0004:P15999.

PTM databases

iPTMnetiP15999.
PhosphoSiteiP15999.

Miscellaneous databases

PMAP-CutDBP15999.

Expressioni

Tissue specificityi

Expressed in flagella of epididymal sperm.1 Publication

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi249327. 3 interactions.
IntActiP15999. 7 interactions.
MINTiMINT-4588311.
STRINGi10116.ENSRNOP00000022892.

Structurei

Secondary structure

1
553
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 583Combined sources
Beta strandi62 – 643Combined sources
Turni68 – 703Combined sources
Beta strandi71 – 744Combined sources
Beta strandi78 – 803Combined sources
Beta strandi81 – 844Combined sources
Beta strandi94 – 974Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi136 – 1449Combined sources
Turni145 – 1484Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi167 – 1726Combined sources
Turni179 – 1813Combined sources
Helixi194 – 1974Combined sources
Beta strandi209 – 2179Combined sources
Helixi218 – 22710Combined sources
Helixi228 – 2303Combined sources
Turni231 – 2344Combined sources
Beta strandi243 – 2508Combined sources
Helixi255 – 26511Combined sources
Helixi268 – 2714Combined sources
Beta strandi272 – 2787Combined sources
Helixi285 – 2884Combined sources
Helixi290 – 30011Combined sources
Beta strandi307 – 3126Combined sources
Helixi314 – 32714Combined sources
Helixi342 – 3454Combined sources
Helixi349 – 3513Combined sources
Turni357 – 3593Combined sources
Beta strandi365 – 3739Combined sources
Helixi382 – 3865Combined sources
Beta strandi392 – 3954Combined sources
Helixi397 – 4004Combined sources
Helixi418 – 4203Combined sources
Turni424 – 4296Combined sources
Helixi430 – 44314Combined sources
Turni444 – 4463Combined sources
Helixi447 – 4493Combined sources
Beta strandi451 – 4533Combined sources
Helixi455 – 4573Combined sources
Helixi458 – 47114Combined sources
Helixi481 – 49212Combined sources
Helixi504 – 51815Combined sources
Helixi520 – 5267Combined sources
Turni527 – 5293Combined sources
Helixi534 – 54815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80A44-553[»]
2F43X-ray3.00A44-553[»]
ProteinModelPortaliP15999.
SMRiP15999. Positions 66-545.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15999.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
HOGENOMiHOG000130111.
HOVERGENiHBG001536.
InParanoidiP15999.
KOiK02132.
PhylomeDBiP15999.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. 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]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSVRIAAAV ARALPRRAGL VSKNALGSSF VGTRNLHASN TRLQKTGTAE
60 70 80 90 100
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS
110 120 130 140 150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGDELLGRV
160 170 180 190 200
VDALGNAIDG KGPVGSKIRR RVGLKAPGII PRISVREPMQ TGIKAVDSLV
210 220 230 240 250
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG
260 270 280 290 300
QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
310 320 330 340 350
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
360 370 380 390 400
RAAKMNDSFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF
410 420 430 440 450
YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG
460 470 480 490 500
SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE
510 520 530 540 550
PSKITKFESA FLSHVVSQHQ SLLGNIRSDG KISEQSDAKL KEIVTNFLAG

FEP
Length:553
Mass (Da):59,754
Last modified:December 6, 2005 - v2
Checksum:iD48886ED1245302C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → R in AAA40784 (PubMed:2137825).Curated
Sequence conflicti321 – 3211Y → D in CAA39599 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061830 mRNA. Translation: AAH61830.1.
J05266 mRNA. Translation: AAA40784.1.
X56133 mRNA. Translation: CAA39599.1.
PIRiA35730.
RefSeqiNP_075581.1. NM_023093.1.
UniGeneiRn.40255.

Genome annotation databases

GeneIDi65262.
KEGGirno:65262.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061830 mRNA. Translation: AAH61830.1.
J05266 mRNA. Translation: AAA40784.1.
X56133 mRNA. Translation: CAA39599.1.
PIRiA35730.
RefSeqiNP_075581.1. NM_023093.1.
UniGeneiRn.40255.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80A44-553[»]
2F43X-ray3.00A44-553[»]
ProteinModelPortaliP15999.
SMRiP15999. Positions 66-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249327. 3 interactions.
IntActiP15999. 7 interactions.
MINTiMINT-4588311.
STRINGi10116.ENSRNOP00000022892.

Chemistry

ChEMBLiCHEMBL2176795.

PTM databases

iPTMnetiP15999.
PhosphoSiteiP15999.

2D gel databases

World-2DPAGE0004:P15999.

Proteomic databases

PaxDbiP15999.
PRIDEiP15999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi65262.
KEGGirno:65262.

Organism-specific databases

CTDi498.
RGDi619993. Atp5a1.

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
HOGENOMiHOG000130111.
HOVERGENiHBG001536.
InParanoidiP15999.
KOiK02132.
PhylomeDBiP15999.

Miscellaneous databases

EvolutionaryTraceiP15999.
NextBioi614213.
PMAP-CutDBP15999.
PROiP15999.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. 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]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Prostate.
  2. "Mitochondrial ATP synthase. cDNA cloning, amino acid sequence, overexpression, and properties of the rat liver alpha subunit."
    Lee J.H., Garboczi D.N., Thomas P.J., Pedersen P.L.
    J. Biol. Chem. 265:4664-4669(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-553.
    Tissue: Liver.
  3. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-58; 104-123; 134-161; 195-204; 335-347; 403-416; 435-463; 467-493; 507-527 AND 540-553, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  4. Frey B.A.J., Weber F.E., Fett R., Pette D.
    Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 319-553.
    Tissue: Muscle.
  5. "Identification of two proteins associated with mammalian ATP synthase."
    Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.
    Mol. Cell. Proteomics 6:1690-1699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
  6. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
    Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
    Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  7. Cited for: INTERACTION WITH BCL2L1.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
    Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
    PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-76.
  10. "The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis."
    Bianchet M.A., Hullihen J., Pedersen P.L., Amzel L.M.
    Proc. Natl. Acad. Sci. U.S.A. 95:11065-11070(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-553.

Entry informationi

Entry nameiATPA_RAT
AccessioniPrimary (citable) accession number: P15999
Secondary accession number(s): Q6P753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 6, 2005
Last modified: January 20, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.