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. 2017 Sep 5;7:10418. doi: 10.1038/s41598-017-10741-z

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Alignment of the regions corresponding to the first six transmembrane segments of P4-ATPases and SERCA. Protein sequences of the bovine ATP8A2 studied here, the 14 human flippases, 4 yeast flippases, and one plant flippase (UniProt nos. from above: C7EXK4, Q9NTI2, Q9Y2Q0, O43520, P98198, O60423, Q8TF62, O75110, O43861, O60312, O94823, Q9P241, P98196, Q9Y2G3, Q8NB49, P32660, Q12675, Q12674, P39524, and Q9LI83) were aligned with rabbit SERCA1 Ca²⁺-ATPase (UniProt no. P04191) as previously described¹⁴. Letter colours denote positively (blue) or negatively (red) charged, polar (green), or hydrophobic (black) residues. The residues replaced in the three disease mutants studied here are indicated with arrowheads. Numbering refers to the bovine ATP8A2. Grey shading denotes the transmembrane helices identified in SERCA crystal structures. The human P4-ATPases are subdivided into classes of genetically most related proteins: Class 1a (ATP8A1, ATP8A2), Class 1b (ATP8B1, ATP8B2, ATP8B3, ATP8B4), Class 2 (ATP9A, ATP9B), Class 5 (ATP10A, ATP10B, ATP10D), and Class 6 (ATP11A, ATP11B, ATP11C)².