Cation-transporting P-type ATPase, N-terminal
IPR004014
Definition
This entry represents the conserved N-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H+ ([ec:7.1.2.1]), Na+ ([ec:7.2.2.3]), Ca2+ ([ec:7.2.2.10]), Na+/K+ ([ec:7.2.2.13]), and H+/K+ ([ec:7.2.2.19]). In the H+/K+-and Na+/K+-exchange P-ATPases, this domain is found in the catalytic alpha chain. In gastric H+/K+-ATPases, this domain undergoes reversible sequential phosphorylation inducing conformational changes that may be important for regulating the function of these ATPases [[cite:PMID:12480547], [cite:PMID:12529322]]. 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.
18 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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