P-type ATPase, cytoplasmic domain N
IPR023299
Definition
This superfamily represents the cytoplasmic domain N found in P-type ATPases. The cytoplasmic loops of the P-type ATPases form three separate modules, commonly named the A, P and N-domains [[cite:PMID:15448704], [cite:PMID:28443028]]. The N-domain comprises the nucleotide binding site PMID:15364580. This domain forms a seven-stranded antiparallel β-sheet with two additional β-strands forming a hairpin and five α-helices PMID:14499619. 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.
36 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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