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. 2017 Jul 26;7:6519. doi: 10.1038/s41598-017-06685-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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Glycosylation of wild type EphA4 Fc. (A) A schematic of EphA4 Fc (not to scale) identifying the EphA4 region (light grey) and the Fc region (dark grey). The EphA4 signal peptide (S) is located at the N-terminus of the protein and is followed by the ligand-binding domain (LBD), cysteine-rich domain (CRD) and two fibronectin type III repeats (FN1) and (FN2)⁴. The IgG4 Fc portion of the protein includes the hinge (H) region and the C_H2 and C_H3 constant immunoglobulin domains. Observed tryptic peptides containing the four N-linked sites (N235, N340, N408 and N625) are displayed with the N-linked consensus sites underlined. The amino- and carboxyl-terminal residues of the tryptic peptides have been annotated with the respective amino acid numbers from the EphA4 Fc sequence. Any additional observed proteolytic cleavage by trypsin or Glu-C within the tryptic peptide sequences have also been annotated with the respective amino acid numbers. (B) Qualitative distribution of the glycan compositions observed from EphA4 Fc at N-linked sites N235, N340, N408 and N625.