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Protein

ATP synthase subunit alpha, mitochondrial

Gene

Atp5f1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

  • angiostatin binding Source: MGI
  • ATP binding Source: MGI
  • MHC class I protein binding Source: MGI
  • proton-transporting ATP synthase activity, rotational mechanism Source: MGI

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-163210 Formation of ATP by chemiosmotic coupling
R-MMU-8949613 Cristae formation

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrialCurated
Alternative name(s):
ATP synthase F1 subunit alphaBy similarity
Gene namesi
Name:Atp5f1aBy similarity
Synonyms:Atp5a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:88115 Atp5a1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 43MitochondrionBy similarityAdd BLAST43
ChainiPRO_000000242544 – 553ATP synthase subunit alpha, mitochondrialAdd BLAST510

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53PhosphoserineCombined sources1
Modified residuei65PhosphoserineBy similarity1
Modified residuei76Phosphoserine; alternateCombined sources1
Glycosylationi76O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei106PhosphoserineCombined sources1
Modified residuei123N6-acetyllysineCombined sources1
Modified residuei126N6-acetyllysineCombined sources1
Modified residuei132N6-acetyllysineCombined sources1
Modified residuei134PhosphothreonineBy similarity1
Modified residuei161N6-acetyllysine; alternateCombined sources1
Modified residuei161N6-succinyllysine; alternateCombined sources1
Modified residuei166PhosphoserineBy similarity1
Modified residuei167N6-acetyllysine; alternateCombined sources1
Modified residuei167N6-succinyllysine; alternateCombined sources1
Modified residuei184PhosphoserineBy similarity1
Modified residuei204Omega-N-methylarginineCombined sources1
Modified residuei230N6-acetyllysine; alternateCombined sources1
Modified residuei230N6-succinyllysine; alternateCombined sources1
Modified residuei239N6-acetyllysine; alternateCombined sources1
Modified residuei239N6-succinyllysine; alternateCombined sources1
Modified residuei240N6-acetyllysineCombined sources1
Modified residuei261N6-acetyllysine; alternateCombined sources1
Modified residuei261N6-succinyllysine; alternateCombined sources1
Modified residuei305N6-acetyllysine; alternateCombined sources1
Modified residuei305N6-succinyllysine; alternateCombined sources1
Modified residuei427N6-acetyllysine; alternateCombined sources1
Modified residuei427N6-succinyllysine; alternateCombined sources1
Modified residuei434N6-acetyllysineCombined sources1
Modified residuei498N6-acetyllysine; alternateCombined sources1
Modified residuei498N6-succinyllysine; alternateCombined sources1
Modified residuei506N6-acetyllysine; alternateCombined sources1
Modified residuei506N6-succinyllysine; alternateCombined sources1
Modified residuei521PhosphoserineCombined sources1
Modified residuei531N6-acetyllysine; alternateCombined sources1
Modified residuei531N6-succinyllysine; alternateCombined sources1
Modified residuei539N6-acetyllysine; alternateCombined sources1
Modified residuei539N6-succinyllysine; alternateCombined sources1
Modified residuei541N6-acetyllysineCombined sources1

Post-translational modificationi

Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.
Acetylated on lysine residues. BLOC1S1 is required for acetylation (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

EPDiQ03265
MaxQBiQ03265
PaxDbiQ03265
PeptideAtlasiQ03265
PRIDEiQ03265

2D gel databases

REPRODUCTION-2DPAGEiIPI00130280
Q03265
SWISS-2DPAGEiQ03265
UCD-2DPAGEiQ03265

PTM databases

CarbonylDBiQ03265
iPTMnetiQ03265
PhosphoSitePlusiQ03265
SwissPalmiQ03265

Expressioni

Gene expression databases

BgeeiENSMUSG00000025428
ExpressionAtlasiQ03265 baseline and differential
GenevisibleiQ03265 MM

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, ATP5MC1, ATP5F1E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, 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). Interacts with CLN5 and PPT1 (PubMed:19941651).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198253, 25 interactors
IntActiQ03265, 34 interactors
MINTiQ03265
STRINGi10090.ENSMUSP00000026495

Structurei

3D structure databases

ProteinModelPortaliQ03265
SMRiQ03265
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1353 Eukaryota
COG0056 LUCA
GeneTreeiENSGT00550000074846
HOVERGENiHBG001536
InParanoidiQ03265
KOiK02132
OMAiQDKCDSS
OrthoDBiEOG091G0D1M
PhylomeDBiQ03265
TreeFamiTF300321

Family and domain databases

CDDicd01132 F1_ATPase_alpha, 1 hit
Gene3Di1.20.150.20, 1 hit
2.40.30.20, 1 hit
HAMAPiMF_01346 ATP_synth_alpha_bact, 1 hit
InterProiView protein in InterPro
IPR023366 ATP_synth_asu-like_sf
IPR000793 ATP_synth_asu_C
IPR038376 ATP_synth_asu_C_sf
IPR033732 ATP_synth_F1_a
IPR005294 ATP_synth_F1_asu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF00306 ATP-synt_ab_C, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
PIRSFiPIRSF039088 F_ATPase_subunit_alpha, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00962 atpA, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q03265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE
60 70 80 90 100
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS
110 120 130 140 150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDV VKRTGAIVDV PVGEELLGRV
160 170 180 190 200
VDALGNAIDG KGPIGSKTRR 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
PSKITKFENA FLSHVISQHQ SLLGNIRSDG KISEQSDAKL KEIVTNFLAG

FEP
Length:553
Mass (Da):59,753
Last modified:October 1, 1993 - v1
Checksum:iCF35B4FBA7ED431D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3S → T in BAE37632 (PubMed:16141072).Curated1
Sequence conflicti63D → Y in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti119F → L in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti126K → N in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti315S → Y in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti321Y → C in BAE40868 (PubMed:16141072).Curated1
Sequence conflicti422 – 456Missing in BAE27439 (PubMed:16141072).CuratedAdd BLAST35
Sequence conflicti486A → T in BAE40158 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS29358.1
PIRiJC1473
RefSeqiNP_031531.1, NM_007505.2
UniGeneiMm.276137

Genome annotation databases

EnsembliENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428
GeneIDi11946
KEGGimmu:11946
UCSCiuc008fru.1 mouse

Similar proteinsi

Entry informationi

Entry nameiATPA_MOUSE
AccessioniPrimary (citable) accession number: Q03265
Secondary accession number(s): Q3TFN0
, Q3THN8, Q3TPR0, Q3TPV3, Q3TZU3, Q3UIR7, Q543Y6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 25, 2018
This is version 185 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health