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0ATP5I_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameATP5I
DescriptionAtp synthase e chain, mitochondrial (ec 3.6.3.14).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.F-ATPases (also known as F1F0-ATPase.r H(+)-transporting two-sector ATPase) () are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha.eta.amma.elta.psilon).hile the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C).ine in mitochondria (A-G.6.8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex.he central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits.hile in the F0 complex.he ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions.ut the F0 rotor is usually stronger.sing the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis . These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.This entry represents subunit E found in the F0 complex of F-ATPases. Mitochondrial F-ATPases can associate together to form dimeric or oligomeric complexes.uch interactions involving the physical association of membrane-embedded F0 complexes. In yeast.he F0 complex E subunit appears to play an important role in supporting F-ATPase dimerisation. This subunit is anchored to the inner mitochondrial membrane via its N-terminal region.hich is involved in stabilizing subunits G and K of the F0 complex. The C-terminal region of subunit E is hydrophilic.rotruding into the intermembrane space where it can also help stabilize the F-ATPase dimer complex .More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR008386:ATPase, F0 complex, subunit E, mitochondrial
IPR008386:ATP-synt_E 
Evalue:-25.5228786468506 
Location:1-68
SequencesProtein: ATP5I_HUMAN (68 aa)
mRNA: NM_007100
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 28 residues, 656225-656308Exon2: 35 residues, 657091-657190Exon3: 20 residues, 657700-657755Exon4: 42 residues, 658000-658122Exon5: 2 residues, -Jump to ATP5I_HUMAN  
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Loci Cluster (Details)Loci: 4658 656225-658122 ~-2K 27158(ATP5I)(-)Loci: 4659 768745-809945 ~-41K 27171(CPLX1)(-)Loci: 4660 833065-915975 ~-83K 27175(GAK)(-)Loci: 3397 609394-654542 ~-45K 27157(PDE6B)(+)Link out to UCSC