| IED ID | IndEnz0002006360 |
| Enzyme Type ID | protease006360 |
| Protein Name |
ATP synthase subunit alpha, mitochondrial ATP synthase F1 subunit alpha |
| Gene Name | Atp5f1a Atp5a1 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLSVRIAAAVARALPRRAGLVSKNALGSSFVGTRNLHASNTRLQKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP |
| Enzyme Length | 553 |
| Uniprot Accession Number | P15999 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) 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). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity). {ECO:0000250|UniProtKB:P19483, ECO:0000250|UniProtKB:P25705}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 213..220; /note=ATP; /evidence=ECO:0000250|UniProtKB:P19483; NP_BIND 473..475; /note=ATP; /evidence=ECO:0000250|UniProtKB:P19483 |
| Features | Beta strand (21); Chain (1); Glycosylation (1); Helix (21); Modified residue (36); Nucleotide binding (2); Sequence conflict (2); Site (1); Transit peptide (1); Turn (8) |
| Keywords | 3D-structure;ATP synthesis;ATP-binding;Acetylation;CF(1);Cell membrane;Direct protein sequencing;Glycoprotein;Hydrogen ion transport;Ion transport;Membrane;Methylation;Mitochondrion;Mitochondrion inner membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Transit peptide;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17575325}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side {ECO:0000250|UniProtKB:P19483}. Cell membrane {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein {ECO:0000250|UniProtKB:P25705}; Extracellular side {ECO:0000250|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell surface of T-cells. {ECO:0000250|UniProtKB:P25705}. |
| Modified Residue | MOD_RES 53; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 65; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 76; /note=Phosphoserine; alternate; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 106; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 123; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 126; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 132; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 134; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 161; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 161; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 166; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 167; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 167; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 184; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 204; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 230; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 230; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 239; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 239; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 240; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 261; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 261; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 305; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 305; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 427; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 427; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 434; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 498; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 498; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 506; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 506; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 531; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 531; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 539; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P25705; MOD_RES 539; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q03265; MOD_RES 541; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q03265 |
| Post Translational Modification | PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation. {ECO:0000250|UniProtKB:P25705}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1MAB; 2F43; |
| Mapped Pubmed ID | 10887193; 1429535; 14499952; 16187210; 16215688; 16396496; 16518874; 16531409; 1834656; 18457437; 19106112; 19119138; 19562802; 19935650; 20178748; 20483212; 20850499; 21396162; 22401655; 24388463; 24610369; 24687852; 25222487; 25561935; 25658244; 25689466; 25772430; 26633942; 26698593; 28526935; 2894844; 8075110; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,754 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |