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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)DescriptionActionsGraphical viewLength
Sitei413Required for activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi212 – 219ATPBy similarity8

GO - Molecular functioni

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

GO - Biological processi

  • ATP metabolic process Source: RGD
  • ATP synthesis coupled proton transport Source: InterPro
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 databases

ChEMBLiCHEMBL2176795.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 43MitochondrionAdd BLAST43
ChainiPRO_000000242744 – 553ATP synthase subunit alpha, mitochondrialAdd BLAST510

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44Pyrrolidone carboxylic acidBy similarity1
Modified residuei53PhosphoserineBy similarity1
Modified residuei65PhosphoserineBy similarity1
Modified residuei76Phosphoserine; alternateBy similarity1
Glycosylationi76O-linked (GlcNAc); alternate1 Publication1
Modified residuei106PhosphoserineBy similarity1
Modified residuei123N6-acetyllysineBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei132N6-acetyllysineBy similarity1
Modified residuei134PhosphothreonineCombined sources1
Modified residuei161N6-acetyllysine; alternateBy similarity1
Modified residuei161N6-succinyllysine; alternateBy similarity1
Modified residuei166PhosphoserineBy similarity1
Modified residuei167N6-acetyllysine; alternateBy similarity1
Modified residuei167N6-succinyllysine; alternateBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei204Omega-N-methylarginineBy similarity1
Modified residuei230N6-acetyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysine; alternateBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
Modified residuei239N6-succinyllysine; alternateBy similarity1
Modified residuei240N6-acetyllysineBy similarity1
Modified residuei261N6-acetyllysine; alternateBy similarity1
Modified residuei261N6-succinyllysine; alternateBy similarity1
Modified residuei305N6-acetyllysine; alternateBy similarity1
Modified residuei305N6-succinyllysine; alternateBy similarity1
Modified residuei427N6-acetyllysine; alternateBy similarity1
Modified residuei427N6-succinyllysine; alternateBy similarity1
Modified residuei434N6-acetyllysineBy similarity1
Modified residuei498N6-acetyllysine; alternateBy similarity1
Modified residuei498N6-succinyllysine; alternateBy similarity1
Modified residuei506N6-acetyllysine; alternateBy similarity1
Modified residuei506N6-succinyllysine; alternateBy similarity1
Modified residuei531N6-acetyllysine; alternateBy similarity1
Modified residuei531N6-succinyllysine; alternateBy similarity1
Modified residuei539N6-acetyllysine; alternateBy similarity1
Modified residuei539N6-succinyllysine; alternateBy similarity1
Modified residuei541N6-acetyllysineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP15999.
PRIDEiP15999.

2D gel databases

World-2DPAGE0004:P15999.

PTM databases

iPTMnetiP15999.
PhosphoSitePlusiP15999.

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. Interacts with CLN5 and PPT1 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi249327. 3 interactors.
IntActiP15999. 8 interactors.
MINTiMINT-4588311.
STRINGi10116.ENSRNOP00000022892.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 58Combined sources3
Beta strandi62 – 64Combined sources3
Turni68 – 70Combined sources3
Beta strandi71 – 74Combined sources4
Beta strandi78 – 80Combined sources3
Beta strandi81 – 84Combined sources4
Beta strandi94 – 97Combined sources4
Beta strandi103 – 106Combined sources4
Beta strandi116 – 120Combined sources5
Beta strandi130 – 132Combined sources3
Beta strandi136 – 144Combined sources9
Turni145 – 148Combined sources4
Beta strandi149 – 151Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi167 – 172Combined sources6
Turni179 – 181Combined sources3
Helixi194 – 197Combined sources4
Beta strandi209 – 217Combined sources9
Helixi218 – 227Combined sources10
Helixi228 – 230Combined sources3
Turni231 – 234Combined sources4
Beta strandi243 – 250Combined sources8
Helixi255 – 265Combined sources11
Helixi268 – 271Combined sources4
Beta strandi272 – 278Combined sources7
Helixi285 – 288Combined sources4
Helixi290 – 300Combined sources11
Beta strandi307 – 312Combined sources6
Helixi314 – 327Combined sources14
Helixi342 – 345Combined sources4
Helixi349 – 351Combined sources3
Turni357 – 359Combined sources3
Beta strandi365 – 373Combined sources9
Helixi382 – 386Combined sources5
Beta strandi392 – 395Combined sources4
Helixi397 – 400Combined sources4
Helixi418 – 420Combined sources3
Turni424 – 429Combined sources6
Helixi430 – 443Combined sources14
Turni444 – 446Combined sources3
Helixi447 – 449Combined sources3
Beta strandi451 – 453Combined sources3
Helixi455 – 457Combined sources3
Helixi458 – 471Combined sources14
Helixi481 – 492Combined sources12
Helixi504 – 518Combined sources15
Helixi520 – 526Combined sources7
Turni527 – 529Combined sources3
Helixi534 – 548Combined sources15

3D structure databases

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

CDDicd01132. F1_ATPase_alpha. 1 hit.
Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR000793. ATP_synth_asu_C.
IPR033732. ATP_synth_F1_a.
IPR005294. ATP_synth_F1_asu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
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.
SUPFAMiSSF50615. 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)DescriptionActionsGraphical viewLength
Sequence conflicti11A → R in AAA40784 (PubMed:2137825).Curated1
Sequence conflicti321Y → D in CAA39599 (Ref. 4) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80A44-553[»]
2F43X-ray3.00A44-553[»]
ProteinModelPortaliP15999.
SMRiP15999.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249327. 3 interactors.
IntActiP15999. 8 interactors.
MINTiMINT-4588311.
STRINGi10116.ENSRNOP00000022892.

Chemistry databases

ChEMBLiCHEMBL2176795.

PTM databases

iPTMnetiP15999.
PhosphoSitePlusiP15999.

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.
PMAP-CutDBP15999.
PROiP15999.

Family and domain databases

CDDicd01132. F1_ATPase_alpha. 1 hit.
Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR000793. ATP_synth_asu_C.
IPR033732. ATP_synth_F1_a.
IPR005294. ATP_synth_F1_asu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
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.
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 164 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.