P-type ATPase, A domain
IPR059000
Definition
This entry represents the actuator (A) domain, and some transmembrane helices found in P-type ATPases PMID:8226755. It contains the TGES-loop which is essential for the metal ion binding which results in tight association between the A and P (phosphorylation) domains PMID:15448704. It does not contain the phosphorylation site. It is thought that the large movement of the actuator domain, which is transmitted to the transmembrane helices, is essential to the long distance coupling between formation/decomposition of the acyl phosphate in the cytoplasmic P-domain and the changes in the ion-binding sites buried deep in the membranous region PMID:18930923. This domain has a modulatory effect on the phosphoenzyme processing steps through its nucleotide binding [[cite:PMID:18075584], [cite:PMID:16710301]]. P-ATPases (also known as E1-E2 ATPases) ([ec:7.2.2.6]) are found in bacteria and in a number of eukaryotic plasma membranes and organelles PMID:9419228. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, which transport specific types of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+and Cu2+ [[cite:PMID:37838176], [cite:PMID:37264943]]. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2. Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.
30 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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