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. 2020 Jan 10;11:194. doi: 10.1038/s41467-019-14040-1

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© The Author(s) 2020

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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Fig. 6 — a Crystal structure of the SEA domain from zebrafish Gpr126. b (left) NMR structure of Mucin-1 SEA domain (PDB: 2ACM) and (right) Gpr126 SEA domain superimposed over Mucin-1 SEA domain. The loop containing the autoproteolysis site in Mucin-1 is indicated by a yellow arrow. The root-mean-square deviation (RMSD) of atoms between overlaid structures is 2.761 Å. c (left) Crystal structure of the Notch2 SEA domain (PDB: 2OO4) and (right) Gpr126 SEA domain superimposed over Notch2 SEA domain. The loop containing the furin-cleavage site (deleted in crystal structure construct) is indicated by an orange arrow. The RMSD of atoms between overlaid structures is 4.767 Å. d Sequence alignment of partial SEA domain from human Mucin-1, human Notch2, human GPR126, and zebrafish Gpr126. e Homology model of human GPR126 SEA model generated using SWISSMODEL. The arrow points to modelled furin-cleavage site. f Protein topology map of SEA domain. Furin-cleavage site is indicated by red scissors. Residues N-terminal to cleavage site are dark blue and residues C-terminal to cleavage site are light blue. Dashed lines represent backbone hydrogen bonds between beta sheets.