SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0AT5G1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameATP5G1
DescriptionAtp synthase lipid-binding protein, mitochondrial precursor (ec 3.6.3.14) (atp synthase proteolipid p1) (atpase protein 9) (atpase subunit c).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005753 proton-transporting ATP synthase complex (s... (TAS)
0005215 transporter activity (NAS)

Warning: fopen(/home/kongl/syndb/www/temp/1032084531.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
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 C (also called subunit 9.r proteolipid) found in the F0 complex of F-ATPases. Ten C subunits form an oligomeric ring that makes up the F0 rotor. The flux of protons through the ATPase channel drives the rotation of the C subunit ring.hich in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the C subunit ring of F0. The sequential protonation and deprotonation of Asp61 of subunit C is coupled to the stepwise movement of the rotor . More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR000454:ATPase, F0 complex, subunit C
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.The F-ATPases (or F1F0-ATPases) and V-ATPases (or V1V0-ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP.nd the F0 or V0 complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors.ne that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis . This entry represents subunit C (also called subunit 9.r proteolipid in F-ATPases.r the 16 kDa proteolipid in V-ATPases) found in the F0 or V0 complex of F- and V-ATPases.espectively. In F-ATPases.en C subunits form an oligomeric ring that makes up the F0 rotor. The flux of protons through the ATPase channel drives the rotation of the C subunit ring.hich in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the C subunit ring of F0. The sequential protonation and deprotonation of Asp61 of subunit C is coupled to the stepwise movement of the rotor . In V-ATPases.here are three proteolipid subunits (c. and c) that form part of the proton-conducting pore.ach containing a buried glutamic acid residue that is essential for proton transport.nd together they form a hexameric ring spanning the membrane . More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR002379:ATPase, F0/V0 complex, subunit C
IPR002379:ATP-synt_C 
Evalue:-29.1938209533691 
Location:67-135
SequencesProtein: AT5G1_HUMAN (136 aa)
mRNA: NM_005175
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: 42 residues, 44325146-44325271Exon2: 18 residues, 44325769-44325817Exon3: 28 residues, 44326732-44326810Exon4: 61 residues, 44327516-44327695Exon5: 73 residues, 44328015-44328229Exon6: 2 residues, -Jump to AT5G1_HUMAN  
Tune and view alternative isoforms