{PDOC00139} {PS00154; ATPASE_E1_E2} {BEGIN} *************************************** * P-type ATPases phosphorylation site * *************************************** P-type ATPases (also known as E1-E2) are cation transport ATPases which form an aspartyl phosphate intermediate in the course of ATP hydrolysis. ATPases which belong to this family are listed below [1,2,3]. - Fungal and plant plasma membrane (H+) ATPases (EC 3.6.3.6). - Vertebrate (Na+, K+) ATPases (sodium pump) (EC 3.6.3.9). - Gastric (K+, H+) ATPases (proton pump) (EC 3.6.3.10). - Calcium (Ca++) ATPases (calcium pump) (EC 3.6.3.8) from the sarcoplasmic reticulum (SR), the endoplasmic reticulum (ER) and the plasma membrane. - Copper (Cu++) ATPases (copper pump) (EC 3.6.3.4) which are involved in two human genetic disorders: Menkes syndrome and Wilson disease. - Bacterial cadmium efflux (Cd++) ATPases (EC 3.6.3.3). - Bacterial magnesium (Mg++) ATPases (EC 3.6.3.2). - Bacterial potassium (K+) ATPases (EC 3.6.3.12). - Bacterial zinc (Zn+) ATPases (EC 3.6.3.5). - Fungal ENA sodium ATPases (EC 3.6.3.7). - fixI, a probable cation ATPase from Rhizobacea, involved in nitrogen fixation. The region around the phosphorylated aspartate residue is perfectly conserved in all these ATPases and can be used as a signature pattern. -Consensus pattern: D-K-T-G-T-[LIVM]-[TI] [D is phosphorylated] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: 1. -Last update: November 2002 / Text revised. -Expert(s) to contact by email: Axelsen K.B.; kristian.axelsen@sib.swiss [ 1] Fagan M.J., Saier M.H. Jr. "P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees." J. Mol. Evol. 38:57-99(1994). PubMed=8151716 [ 2] Palmgren M.G., Axelsen K.B. "Evolution of P-type ATPases." Biochim. Biophys. Acta 1365:37-45(1998). PubMed=9693719 [ 3] Axelsen K.B., Palmgren M.G. "Evolution of substrate specificities in the P-type ATPase superfamily." J. Mol. Evol. 46:84-101(1998). PubMed=9419228 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}