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Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP5A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.14. 908.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrial
Gene namesi
Name:ATP5A1
Synonyms:ATP5A2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 43Mitochondrion1 PublicationAdd BLAST43
ChainiPRO_000000242344 – 553ATP synthase subunit alpha, mitochondrialAdd BLAST510

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44Pyrrolidone carboxylic acid1
Modified residuei53PhosphoserineBy similarity1
Modified residuei65PhosphoserineBy similarity1
Modified residuei76Phosphoserine; alternateBy similarity1
Glycosylationi76O-linked (GlcNAc); alternateBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei123N6-acetyllysineBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei132N6-acetyllysineBy similarity1
Modified residuei134PhosphothreonineBy similarity1
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

PaxDbiP19483.
PeptideAtlasiP19483.
PRIDEiP19483.

2D gel databases

UCD-2DPAGEP19483.

Expressioni

Tissue specificityi

Heart and liver.

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). 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 similarity3 Publications

Protein-protein interaction databases

DIPiDIP-35479N.
IntActiP19483. 4 interactors.
MINTiMINT-5006839.
STRINGi9913.ENSBTAP00000003259.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi53 – 60Combined sources8
Turni68 – 70Combined sources3
Beta strandi71 – 78Combined sources8
Beta strandi81 – 86Combined sources6
Beta strandi95 – 98Combined sources4
Beta strandi103 – 109Combined sources7
Beta strandi114 – 120Combined sources7
Helixi122 – 124Combined sources3
Beta strandi130 – 132Combined sources3
Beta strandi139 – 143Combined sources5
Helixi144 – 146Combined sources3
Beta strandi150 – 152Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi167 – 173Combined sources7
Beta strandi179 – 182Combined sources4
Beta strandi187 – 189Combined sources3
Helixi194 – 199Combined sources6
Beta strandi209 – 213Combined sources5
Helixi218 – 228Combined sources11
Helixi230 – 233Combined sources4
Beta strandi234 – 236Combined sources3
Turni238 – 240Combined sources3
Beta strandi243 – 250Combined sources8
Helixi253 – 265Combined sources13
Helixi269 – 271Combined sources3
Beta strandi272 – 277Combined sources6
Helixi283 – 302Combined sources20
Beta strandi306 – 312Combined sources7
Helixi314 – 327Combined sources14
Helixi334 – 336Combined sources3
Helixi341 – 349Combined sources9
Beta strandi353 – 355Combined sources3
Helixi357 – 359Combined sources3
Beta strandi363 – 371Combined sources9
Beta strandi373 – 375Combined sources3
Helixi380 – 388Combined sources9
Beta strandi389 – 395Combined sources7
Helixi397 – 402Combined sources6
Turni410 – 412Combined sources3
Beta strandi414 – 417Combined sources4
Helixi418 – 421Combined sources4
Helixi424 – 441Combined sources18
Helixi444 – 446Combined sources3
Beta strandi447 – 449Combined sources3
Beta strandi451 – 453Combined sources3
Helixi455 – 470Combined sources16
Helixi481 – 492Combined sources12
Turni493 – 498Combined sources6
Helixi501 – 503Combined sources3
Helixi504 – 517Combined sources14
Helixi520 – 529Combined sources10
Helixi534 – 551Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/J44-553[»]
2JJ1X-ray2.70A/B/C/H/I/J44-553[»]
2JJ2X-ray2.40A/B/C/H/I/J44-553[»]
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[»]
4TSFX-ray3.20A/B/C44-553[»]
4TT3X-ray3.21A/B/C44-553[»]
4YXWX-ray3.10A/B/C44-553[»]
4Z1MX-ray3.30A/B/C44-553[»]
5ARAelectron microscopy6.70A/B/C44-553[»]
5AREelectron microscopy7.40A/B/C44-553[»]
5ARHelectron microscopy7.20A/B/C44-553[»]
5ARIelectron microscopy7.40A/B/C44-553[»]
5FIJelectron microscopy7.40A/B/C44-553[»]
5FIKelectron microscopy6.40A/B/C44-553[»]
5FILelectron microscopy7.10A/B/C44-553[»]
ProteinModelPortaliP19483.
SMRiP19483.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19483.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
HOGENOMiHOG000130111.
InParanoidiP19483.
KOiK02132.

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.

P19483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE
60 70 80 90 100
VSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS
110 120 130 140 150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV
160 170 180 190 200
VDALGNAIDG KGPIGSKARR 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
RAAKMNDAFG 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 ALLSKIRTDG KISEESDAKL KEIVTNFLAG

FEA
Length:553
Mass (Da):59,720
Last modified:February 1, 1991 - v1
Checksum:i188E9531B3B815E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4V → M in AAI16060 (Ref. 3) Curated1
Sequence conflicti6V → I in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti31 – 33IAA → VGT in AAA30399 (PubMed:2896000).Curated3
Sequence conflicti41S → T in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti51V → M in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti144E → D in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti164I → V in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti168A → I in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti358A → S in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti524S → G in AAI16060 (Ref. 3) Curated1
Sequence conflicti524S → G AA sequence (PubMed:2864455).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22465 mRNA. Translation: AAB59266.1.
X64565 Genomic DNA. Translation: CAA45865.1.
BC116059 mRNA. Translation: AAI16060.1.
M19680 mRNA. Translation: AAA30399.1.
PIRiA27693.
S27201. PWBOA.
RefSeqiNP_777109.1. NM_174684.2.
UniGeneiBt.7194.

Genome annotation databases

GeneIDi282578.
KEGGibta:282578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22465 mRNA. Translation: AAB59266.1.
X64565 Genomic DNA. Translation: CAA45865.1.
BC116059 mRNA. Translation: AAI16060.1.
M19680 mRNA. Translation: AAA30399.1.
PIRiA27693.
S27201. PWBOA.
RefSeqiNP_777109.1. NM_174684.2.
UniGeneiBt.7194.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/J44-553[»]
2JJ1X-ray2.70A/B/C/H/I/J44-553[»]
2JJ2X-ray2.40A/B/C/H/I/J44-553[»]
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[»]
4TSFX-ray3.20A/B/C44-553[»]
4TT3X-ray3.21A/B/C44-553[»]
4YXWX-ray3.10A/B/C44-553[»]
4Z1MX-ray3.30A/B/C44-553[»]
5ARAelectron microscopy6.70A/B/C44-553[»]
5AREelectron microscopy7.40A/B/C44-553[»]
5ARHelectron microscopy7.20A/B/C44-553[»]
5ARIelectron microscopy7.40A/B/C44-553[»]
5FIJelectron microscopy7.40A/B/C44-553[»]
5FIKelectron microscopy6.40A/B/C44-553[»]
5FILelectron microscopy7.10A/B/C44-553[»]
ProteinModelPortaliP19483.
SMRiP19483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35479N.
IntActiP19483. 4 interactors.
MINTiMINT-5006839.
STRINGi9913.ENSBTAP00000003259.

2D gel databases

UCD-2DPAGEP19483.

Proteomic databases

PaxDbiP19483.
PeptideAtlasiP19483.
PRIDEiP19483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282578.
KEGGibta:282578.

Organism-specific databases

CTDi498.

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
HOGENOMiHOG000130111.
InParanoidiP19483.
KOiK02132.

Enzyme and pathway databases

BRENDAi3.6.3.14. 908.

Miscellaneous databases

EvolutionaryTraceiP19483.

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_BOVIN
AccessioniPrimary (citable) accession number: P19483
Secondary accession number(s): P05629, P19482, Q1JQC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 163 of the entry and version 1 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.