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. 2020 May 8;11:798. doi: 10.3389/fimmu.2020.00798

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Copyright © 2020 Nono, Lutz and Brehm.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Alignment of the C-terminal amino acid sequences of EmACT and seven other representatives of the TGF-β superfamily. The paired dibasic cleavage motif is shown within a red open box. Residues that are identical are highlighted in black, similarities in gray. Gaps introduced to maximize the alignment are represented by dashes. Two conserved cysteines found only in TGF-β/activin subfamily are shown with asterisks. Numbers at the start and finish of each line correspond to the amino acid numbers in each respective sequence. Accession numbers for the sequences shown are as follows: Echinococcus multilocularis act, HF912278; Schistosoma mansoni InAct, A4UAH0; Human Inhibin beta A, P08476; Human TGF-β 1, P01137; Drosophila melanogaster Activin, O61643; Caenorhabditis elegans DAF-7, P92172; Fasciola hepatica TGF-like Molecule FhTLM; Brugia malayi TGF-beta homolog, BmTGH2, AAD19903.1; Human BMP-2, P12643; and Drosophila melanogaster DPP, P07713.