ATP5O 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Belongs to the ATPase delta chain family. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.3.14; Energy Metabolism - oxidative phosphorylation; Hydrolase; Mitochondrial
Chromosomal Location of Human Ortholog: 21q22.11
Cellular Component:  mitochondrial inner membrane; mitochondrial proton-transporting ATP synthase complex; mitochondrion; plasma membrane
Molecular Function:  ATPase activity; drug binding; protein binding; proton-transporting ATP synthase activity, rotational mechanism; transmembrane transporter activity
Biological Process:  ATP biosynthetic process; ATP hydrolysis coupled cation transmembrane transport; cristae formation; mitochondrial ATP synthesis coupled proton transport; proton transmembrane transport
Reference #:  P48047 (UniProtKB)
Alt. Names/Synonyms: ATP synthase subunit O, mitochondrial; ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit; ATP5O; ATP5PO; ATPO; human ATP synthase OSCP subunit; mitochondrial ATP synthase, O subunit; Oligomycin sensitivity conferral protein; oligomycin sensitivity conferring protein; OSCP
Gene Symbols: ATP5PO
Molecular weight: 23,277 Da
Basal Isoelectric point: 9.97  Predict pI for various phosphorylation states
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ATP5O

Protein Structure Not Found.


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