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. 2015 Jan 8;8:14. doi: 10.1186/s13071-014-0609-0

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© Gao et al; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Aca-lpp-1 encodes a lipid phosphate phosphatase. A. Aca-LPP-1b translated amino acid sequence aligned with its C. elegans ortholog T28D9.3b1. Identical residues are in red, and conserved residues in blue. The phosphatase active site domains are highlighted in yellow, and the conserved residues required for activity are marked with an asterisk. The transmembrane domains are highlighted in green, and the conserved N-linked glycosylation site is marked by a dollar sign. B. Structure of LPP-1 showing transmembrane domains. Active site residues are found on extracellular loops 2 and 3. C. Maximum likelihood tree showing relationship of Aca-LPP-1 to other LPP-1 proteins. The percentage of trees in which the associated taxa clustered together is shown next to the branches. The A. thaliana sequence was designated as the out group. Ace, EYC42428.1; Cel, NP_001022378; At AAM63082; Mm, AAH61161; Hs, EAW54922; Dm, NP_649394.