Detail Information for IndEnz0002019199
IED ID IndEnz0002019199
Enzyme Type ID protease019199
Protein Name ATP synthase subunit e, mitochondrial
ATPase subunit e
ATP synthase membrane subunit e

Cleaved into: ATP synthase subunit e, mitochondrial, N-terminally processed
Gene Name ATP5ME ATP5I ATP5K
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MVPPVQVSPLIKLGRYSALFLGVAYGATRYNYLKPRAEEERRIAAEEKKKQDELKRIARELAEDDSILK
Enzyme Length 69
Uniprot Accession Number P56385
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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (2); Initiator methionine (1); Modified residue (2)
Keywords ATP synthesis;Acetylation;CF(0);Direct protein sequencing;Hydrogen ion transport;Ion transport;Membrane;Mitochondrion;Mitochondrion inner membrane;Phosphoprotein;Reference proteome;Transport
Interact With Q9UHD4; Q9NZD8
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
Modified Residue MOD_RES 34; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q06185; MOD_RES 66; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P29419
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11939412; 16682002; 17121862; 18060860; 18323778; 19167051; 19688755; 20195357; 20833715; 20877624; 21836051; 21874239; 22623428; 22864911; 24098383; 24344204; 25285856; 25561175; 25852190; 26496610; 4517936;
Motif
Gene Encoded By
Mass 7,933
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda