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. 2018 Jan 10;8:251. doi: 10.1038/s41598-017-18355-1

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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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Multiple alignment of the Stylophora actinoporin and three well studied sea anemone actinoporins: equinatoxin II (EqT-II, Actinia equina), stycholysin II (Stn-II, Stichodactyla helianthus) and fragaceatoxin C (Fra-C, Actinia fragacea). The regions highlighted in red are the C and N- terminal α- helixes, the red triangles point out residues that have shown to be important for membrane attachment^61,69, the blue arrow shows the RGD motif involved in oligomerization¹⁰⁵ and the green stars represent residues that have shown to be important for sphingomyelin recognition^58,61. The blue region shows the conservation of the P-[W/Y/F]-D membrane binding motif^106,107.