UniProtKB - P19483 (ATPA_BOVIN)
ATP synthase subunit alpha, mitochondrial
ATP5F1A
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. Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).
By similarity2 PublicationsMiscellaneous
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 413 | Required for activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 213 – 220 | ATPCombined sources4 Publications | 8 | |
Nucleotide bindingi | 473 – 475 | ATPCombined sources4 Publications | 3 |
GO - Molecular functioni
- ADP binding Source: GO_Central
- ATP binding Source: GO_Central
- proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
GO - Biological processi
- ATP synthesis coupled proton transport Source: GO_Central
Keywordsi
Biological process | ATP synthesis, Hydrogen ion transport, Ion transport, Transport |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 7.1.2.2, 908 |
Names & Taxonomyi
Protein namesi | Recommended name: ATP synthase subunit alpha, mitochondrialCuratedAlternative name(s): ATP synthase F1 subunit alphaBy similarity |
Gene namesi | Name:ATP5F1ABy similarity Synonyms:ATP5A1, ATP5A2 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Mitochondrion
- Mitochondrion inner membrane 4 Publications; Peripheral membrane protein 4 Publications; Matrix side 2 Publications
Plasma membrane
- Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
Note: Colocalizes with HRG on the cell surface of T-cells.By similarity
Mitochondrion
- mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
- mitochondrial proton-transporting ATP synthase, catalytic core Source: GO_Central
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- proton-transporting ATP synthase complex, catalytic core F(1) Source: GO_Central
Keywords - Cellular componenti
Cell membrane, CF(1), Membrane, Mitochondrion, Mitochondrion inner membranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 43 | Mitochondrion1 PublicationAdd BLAST | 43 | |
ChainiPRO_0000002423 | 44 – 553 | ATP synthase subunit alpha, mitochondrialAdd BLAST | 510 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 44 | Pyrrolidone carboxylic acid1 Publication | 1 | |
Modified residuei | 53 | PhosphoserineBy similarity | 1 | |
Modified residuei | 65 | PhosphoserineBy similarity | 1 | |
Modified residuei | 76 | Phosphoserine; alternateBy similarity | 1 | |
Glycosylationi | 76 | O-linked (GlcNAc) serine; alternateBy similarity | 1 | |
Modified residuei | 106 | PhosphoserineBy similarity | 1 | |
Modified residuei | 123 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 126 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 132 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 134 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 161 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 161 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 166 | PhosphoserineBy similarity | 1 | |
Modified residuei | 167 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 167 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 184 | PhosphoserineBy similarity | 1 | |
Modified residuei | 204 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 230 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 230 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 239 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 239 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 240 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 261 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 261 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 305 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 305 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 427 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 427 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 434 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 498 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 498 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 506 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 506 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 531 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 531 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 539 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 539 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 541 | N6-acetyllysineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Glycoprotein, Methylation, Phosphoprotein, Pyrrolidone carboxylic acidProteomic databases
PaxDbi | P19483 |
PeptideAtlasi | P19483 |
PRIDEi | P19483 |
2D gel databases
UCD-2DPAGEi | P19483 |
Expressioni
Tissue specificityi
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 (PubMed:2864455, PubMed:17570365, PubMed:23407638). CF0 has three main subunits: a, b and c (PubMed:2864455, PubMed:17570365, PubMed:23407638).
Interacts with ATPAF2 (By similarity).
Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro) (By similarity).
Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (PubMed:2864455, PubMed:17570365, PubMed:23407638, PubMed:25851905).
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 efficiency.
Interacts with CLN5 and PPT1 (By similarity).
Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity).
Interacts with ABCB7; this interaction allows the regulation of cellular iron homeostasis and cellular reactive oxygen species (ROS) levels in cardiomyocytes (By similarity).
By similarity6 PublicationsProtein-protein interaction databases
CORUMi | P19483 |
DIPi | DIP-35479N |
IntActi | P19483, 9 interactors |
MINTi | P19483 |
STRINGi | 9913.ENSBTAP00000003259 |
Structurei
Secondary structure
3D structure databases
BMRBi | P19483 |
SMRi | P19483 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P19483 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG1353, Eukaryota |
InParanoidi | P19483 |
OrthoDBi | 470054at2759 |
Family and domain databases
CDDi | cd18113, ATP-synt_F1_alpha_C, 1 hit cd01132, F1_ATPase_alpha, 1 hit |
Gene3Di | 1.20.150.20, 1 hit 2.40.30.20, 1 hit 3.40.50.300, 1 hit |
HAMAPi | MF_01346, ATP_synth_alpha_bact, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF00006, ATP-synt_ab, 1 hit PF00306, ATP-synt_ab_C, 1 hit PF02874, ATP-synt_ab_N, 1 hit |
PIRSFi | PIRSF039088, F_ATPase_subunit_alpha, 1 hit |
SUPFAMi | SSF50615, SSF50615, 1 hit SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR00962, atpA, 1 hit |
PROSITEi | View protein in PROSITE PS00152, ATPASE_ALPHA_BETA, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 4 | V → M in AAI16060 (Ref. 3) Curated | 1 | |
Sequence conflicti | 6 | V → I in AAA30399 (PubMed:2896000).Curated | 1 | |
Sequence conflicti | 31 – 33 | IAA → VGT in AAA30399 (PubMed:2896000).Curated | 3 | |
Sequence conflicti | 41 | S → T in AAA30399 (PubMed:2896000).Curated | 1 | |
Sequence conflicti | 51 | V → M in AAA30399 (PubMed:2896000).Curated | 1 | |
Sequence conflicti | 144 | E → D in AAA30399 (PubMed:2896000).Curated | 1 | |
Sequence conflicti | 164 | I → V in AAA30399 (PubMed:2896000).Curated | 1 | |
Sequence conflicti | 168 | A → I in AAA30399 (PubMed:2896000).Curated | 1 | |
Sequence conflicti | 358 | A → S in AAA30399 (PubMed:2896000).Curated | 1 | |
Sequence conflicti | 524 | S → G in AAI16060 (Ref. 3) Curated | 1 | |
Sequence conflicti | 524 | S → G AA sequence (PubMed:2864455).Curated | 1 |
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 |
PIRi | A27693 S27201, PWBOA |
RefSeqi | NP_777109.1, NM_174684.2 |
Genome annotation databases
GeneIDi | 282578 |
KEGGi | bta:282578 |
Similar proteinsi
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 |
PIRi | A27693 S27201, PWBOA |
RefSeqi | NP_777109.1, NM_174684.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BMF | X-ray | 2.85 | A/B/C | 44-553 | [»] | |
1COW | X-ray | 3.10 | A/B/C | 45-553 | [»] | |
1E1Q | X-ray | 2.61 | A/B/C | 44-553 | [»] | |
1E1R | X-ray | 2.50 | A/B/C | 44-553 | [»] | |
1E79 | X-ray | 2.40 | A/B/C | 44-553 | [»] | |
1EFR | X-ray | 3.10 | A/B/C | 45-553 | [»] | |
1H8E | X-ray | 2.00 | A/B/C | 44-553 | [»] | |
1H8H | X-ray | 2.90 | A/B/C | 44-553 | [»] | |
1NBM | X-ray | 3.00 | A/B/C | 44-553 | [»] | |
1OHH | X-ray | 2.80 | A/B/C | 44-553 | [»] | |
1QO1 | X-ray | 3.90 | A/B/C | 44-553 | [»] | |
1W0J | X-ray | 2.20 | A/B/C | 44-553 | [»] | |
1W0K | X-ray | 2.85 | A/B/C | 44-553 | [»] | |
2CK3 | X-ray | 1.90 | A/B/C | 44-553 | [»] | |
2JDI | X-ray | 1.90 | A/B/C | 44-553 | [»] | |
2JIZ | X-ray | 2.30 | A/B/C/H/I/J | 44-553 | [»] | |
2JJ1 | X-ray | 2.70 | A/B/C/H/I/J | 44-553 | [»] | |
2JJ2 | X-ray | 2.40 | A/B/C/H/I/J | 44-553 | [»] | |
2JMX | NMR | - | B | 44-68 | [»] | |
2V7Q | X-ray | 2.10 | A/B/C | 45-553 | [»] | |
2W6E | X-ray | 6.50 | A/B/C | 1-553 | [»] | |
2W6F | X-ray | 6.00 | A/B/C | 1-553 | [»] | |
2W6G | X-ray | 6.00 | A/B/C | 1-553 | [»] | |
2W6H | X-ray | 5.00 | A/B/C | 1-553 | [»] | |
2W6I | X-ray | 4.00 | A/B/C | 1-553 | [»] | |
2W6J | X-ray | 3.84 | A/B/C | 1-553 | [»] | |
2WSS | X-ray | 3.20 | A/B/C/J/K/L | 44-553 | [»] | |
2XND | X-ray | 3.50 | A/B/C | 62-553 | [»] | |
4ASU | X-ray | 2.60 | A/B/C | 44-553 | [»] | |
4TSF | X-ray | 3.20 | A/B/C | 44-553 | [»] | |
4TT3 | X-ray | 3.21 | A/B/C | 44-553 | [»] | |
4YXW | X-ray | 3.10 | A/B/C | 44-553 | [»] | |
4Z1M | X-ray | 3.30 | A/B/C | 44-553 | [»] | |
5ARA | electron microscopy | 6.70 | A/B/C | 44-553 | [»] | |
5ARE | electron microscopy | 7.40 | A/B/C | 44-553 | [»] | |
5ARH | electron microscopy | 7.20 | A/B/C | 44-553 | [»] | |
5ARI | electron microscopy | 7.40 | A/B/C | 44-553 | [»] | |
5FIJ | electron microscopy | 7.40 | A/B/C | 44-553 | [»] | |
5FIK | electron microscopy | 6.40 | A/B/C | 44-553 | [»] | |
5FIL | electron microscopy | 7.10 | A/B/C | 44-553 | [»] | |
6YY0 | electron microscopy | 3.23 | A/B/C | 44-553 | [»] | |
6Z1R | electron microscopy | 3.29 | A/B/C | 44-553 | [»] | |
6Z1U | electron microscopy | 3.47 | A/B/C | 44-553 | [»] | |
6ZIQ | electron microscopy | 4.33 | C | 44-553 | [»] | |
6ZIT | electron microscopy | 3.49 | C | 44-553 | [»] | |
6ZIU | electron microscopy | 6.02 | C | 44-553 | [»] | |
6ZPO | electron microscopy | 4.00 | A/B/C | 44-553 | [»] | |
6ZQM | electron microscopy | 3.29 | A/B/C | 44-553 | [»] | |
6ZQN | electron microscopy | 4.00 | A/B/C | 44-553 | [»] | |
7AJB | electron microscopy | 9.20 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJC | electron microscopy | 11.90 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJD | electron microscopy | 9.00 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJE | electron microscopy | 9.40 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJF | electron microscopy | 8.45 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJG | electron microscopy | 10.70 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJH | electron microscopy | 9.70 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJI | electron microscopy | 11.40 | A/AA/AB/AC/B/C | 44-553 | [»] | |
7AJJ | electron microscopy | 13.10 | A/AA/AB/AC/B/C | 44-553 | [»] | |
BMRBi | P19483 | |||||
SMRi | P19483 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
CORUMi | P19483 |
DIPi | DIP-35479N |
IntActi | P19483, 9 interactors |
MINTi | P19483 |
STRINGi | 9913.ENSBTAP00000003259 |
2D gel databases
UCD-2DPAGEi | P19483 |
Proteomic databases
PaxDbi | P19483 |
PeptideAtlasi | P19483 |
PRIDEi | P19483 |
Genome annotation databases
GeneIDi | 282578 |
KEGGi | bta:282578 |
Organism-specific databases
CTDi | 498 |
Phylogenomic databases
eggNOGi | KOG1353, Eukaryota |
InParanoidi | P19483 |
OrthoDBi | 470054at2759 |
Enzyme and pathway databases
BRENDAi | 7.1.2.2, 908 |
Miscellaneous databases
EvolutionaryTracei | P19483 |
Family and domain databases
CDDi | cd18113, ATP-synt_F1_alpha_C, 1 hit cd01132, F1_ATPase_alpha, 1 hit |
Gene3Di | 1.20.150.20, 1 hit 2.40.30.20, 1 hit 3.40.50.300, 1 hit |
HAMAPi | MF_01346, ATP_synth_alpha_bact, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF00006, ATP-synt_ab, 1 hit PF00306, ATP-synt_ab_C, 1 hit PF02874, ATP-synt_ab_N, 1 hit |
PIRSFi | PIRSF039088, F_ATPase_subunit_alpha, 1 hit |
SUPFAMi | SSF50615, SSF50615, 1 hit SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR00962, atpA, 1 hit |
PROSITEi | View protein in PROSITE PS00152, ATPASE_ALPHA_BETA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ATPA_BOVIN | |
Accessioni | P19483Primary (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: | February 23, 2022 | |
This is version 194 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families