Sequence alignment of phospholipid flippases.

(<b>A</b>) Lipid flippases used in the alignment. <b>(B)</b> Sequence alignment of human ATP8A2, <i>P. falciparum</i> PfATP2, and six putative lipid-translocating ATPases from <i>S. mansoni</i>. The actuator (A), nucleotide binding (N), and phosphorylation (P) domains are shown, as well as the first six transmembrane segments (M1-6). Key conserved residues D (in A domain) and D (P domain) involved in the phosphorylation (DKTGT) and dephosphorylation (DGET) cycle are highlighted by a star. The purple circles highlight the conserved N and I residues located in M4 domain that are important for recognition and release of lipid, respectively. The green triangle indicates the K residues in the M5 domain required for the sensitivity to the lipid subtype [<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1012216#ppat.1012216.ref026" target="_blank">26</a>,<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1012216#ppat.1012216.ref047" target="_blank">47</a>]. (PDF)