P-type ATPase
From Wikipedia, the free encyclopedia
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| Calcium ATPase, E2-Pi state | ||
| Identifiers | ||
|---|---|---|
| Symbol | E1-E2_ATPase | |
| Pfam | PF00122 | |
| InterPro | IPR008250 | |
| PROSITE | PDOC00139 | |
| SCOP | 1eul | |
| OPM family | 22 | |
| OPM protein | 1wpg | |
| Available PDB structures:
2b8eC:407-414 1vfpA:93-341 1wpgC:93-341 1t5sA:93-341 1iwoB:93-341 1t5tA:93-341 1xp5A:93-341 1su4A:93-341 1kjuA:93-341 1wpeA:93-341 2agvA:93-341 1fquA:93-341 1u5nA:99-348 1mhsB:146-368 |
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P-type (or E1-E2-type) ATPases constitute a superfamily of cation transport enzymes, present both in prokaryota and eukaryota, whose members mediate membrane flux of all common biologically relevant cations[1]. The ATPases, that form an aspartyl phosphate intermediate in the course of ATP hydrolysis, can be divided into 4 major groups[2]:
- (1) Ca2+-transporting ATPases;
- (2) Na+/K+- and gastric H+/K+-transporting ATPases;
- (3) Plasma membrane H+-transporting ATPases (proton pumps) of plants, fungi and lower eukaryotes; and
- (4) all bacterial P-type ATPases, except the Mg2+-ATPase of Salmonella typhimurium, which is more similar to the eukaryotic sequences.
[edit] Human proteins containing this domain
- Na+/K+ transporting: ATP1A1, ATP1A2, ATP1A3, ATP1A4, ATP1B1, ATP1B2, ATP1B3, ATP1B4
- Ca++ transporting: ATP2A1, ATP2A2, ATP2A3, ATP2B1, ATP2B2, ATP2B3, ATP2B4, ATP2C1
- Cu++ transporting: ATP7A (see also ATP7A), ATP7B (see also ATP7B)
- Class I, type 8: ATP8A1, ATP8B1, ATP8B2, ATP8B3, ATP8B4
- Class II, type 9: ATP9A, ATP9B
- Class V, type 10: ATP10A, ATP10B, ATP10D
- Class VI, type 11: ATP11A, ATP11B, ATP11C
- H+/K+ transporting, nongastric: ATP12A
- type 13: ATP13A1, ATP13A2, ATP13A3, ATP13A4, ATP13A5
- ATP2C2;
- ATP4A;
- KIAA0195
[edit] See also
[edit] References
- ^ Maguire ME, Smith DL, Tao T (1993). "Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium". J. Biol. Chem. 268 (30): 22469-22479. PMID 8226755.
- ^ Fagan MJ, Saier Jr MH (1994). "P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees". J. Mol. Evol. 38 (1): 57-99. PMID 8151716.
