ATP5A1 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. Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions. Belongs to the ATPase alpha/beta chains family. Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.3.14; Energy Metabolism - oxidative phosphorylation; Hydrolase; Membrane protein, integral; Mitochondrial; Transporter
Chromosomal Location of human Ortholog: 18q21.1
Cellular Component:  cell surface; membrane; membrane raft; mitochondrial inner membrane; mitochondrial matrix; mitochondrial proton-transporting ATP synthase complex; mitochondrial proton-transporting ATP synthase, catalytic core; mitochondrion; plasma membrane; proton-transporting ATP synthase complex; proton-transporting ATP synthase complex, catalytic core F(1)
Molecular Function:  ADP binding; angiostatin binding; ATP binding; ATP hydrolysis activity; MHC class I protein binding; protease binding; protein binding; proton-transporting ATP synthase activity, rotational mechanism
Biological Process:  ATP biosynthetic process; cellular response to dexamethasone stimulus; cellular response to nitric oxide; lipid metabolic process; negative regulation of endothelial cell proliferation; positive regulation of blood vessel endothelial cell migration; proton motive force-driven ATP synthesis; proton motive force-driven mitochondrial ATP synthesis; proton transmembrane transport; response to ethanol; response to muscle activity
Disease: Combined Oxidative Phosphorylation Deficiency 22; Mitochondrial Complex V (atp Synthase) Deficiency, Nuclear Type 4; Mitochondrial Complex V (atp Synthase) Deficiency, Nuclear Type 4a
Reference #:  P25705 (UniProtKB)
Alt. Names/Synonyms: ATP synthase alpha chain, mitochondrial; ATP synthase F1 subunit alpha; ATP synthase subunit alpha, mitochondrial; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 1, cardiac muscle; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 2, non-cardiac muscle-like 2; ATP sythase (F1-ATPase) alpha subunit; ATP5A; ATP5A1; ATP5AL2; ATP5F1A; ATPA; ATPM; COXPD22; epididymis secretory sperm binding protein Li 123m; hATP1; HEL-S-123m; MC5DN4; mitochondrial ATP synthetase, oligomycin-resistant; MOM2; OMR; ORM
Gene Symbols: ATP5F1A
Molecular weight: 59,751 Da
Basal Isoelectric point: 9.16  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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ATP5A1

Protein Structure Not Found.


Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB  |  Ensembl Protein