V-ATPase

V-ATPase
V-ATPase schematic
Identifiers
SymbolV-ATPase
TCDB3.A.2
OPM superfamily5
OPM protein2bl2
Membranome226
V-ATPase, subunit c (Vo)
Membrane-spanning region of the V-type sodium ATPase from Enterococcus hirae. Calculated hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots
Identifiers
SymbolATP-synt_C
PfamPF00137
InterProIPR002379
PROSITEPDOC00526
SCOP21aty / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
V-ATPase, subunit C (V1)
crystal structure of subunit C (vma5p) of the yeast v-atpase
Identifiers
SymbolV-ATPase_C
PfamPF03223
InterProIPR004907
SCOP21u7l / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
V-ATPase, subunit I/a
Identifiers
SymbolV_ATPase_I
PfamPF01496
InterProIPR002490
SCOP23rrk / SCOPe / SUPFAM
TCDB3.A.2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
V-ATPase, subunit E
Identifiers
SymbolvATP-synt_E
PfamPF01991
Pfam clanCL0255
InterProIPR002842
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
V-ATPase, subunit d/d2
crystal structure of subunit C (yeast subunit d) of v-atpase
Identifiers
SymbolvATP-synt_AC39
PfamPF01992
InterProIPR002843
SCOP21r5z / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
V-ATPase, subunit H, N-terminal
crystal structure of the regulatory subunit H of the v-type atpase of saccharomyces cerevisiae
Identifiers
SymbolV-ATPase_H_N
PfamPF03224
Pfam clanCL0020
InterProIPR004908
SCOP21ho8 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
V-ATPase, subunit G
Identifiers
SymbolV-ATPase_G
PfamPF03179
Pfam clanCL0255
InterProIPR005124
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms.[1] V-ATPases acidify a wide array of intracellular organelles and pumps protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.

The Archaea-type ATPase (A-ATPase) is a related group of ATPases found in archaea that often work as an ATP synthase. It forms a clade V/A-ATPase with V-ATPase. Most members of either group shuttle protons (H+
), but a few members have evolved to use sodium ions (Na+
) instead.

  1. ^ Nelson N, Perzov N, Cohen A, Hagai K, Padler V, Nelson H (January 2000). "The cellular biology of proton-motive force generation by V-ATPases". The Journal of Experimental Biology. 203 (Pt 1): 89–95. doi:10.1242/jeb.203.1.89. PMID 10600677.