Extended Data Fig. 1: Sequence alignment of FaNaCs and cASIC1.
From: Structure and mechanism of a neuropeptide-activated channel in the ENaC/DEG superfamily
Sequence alignment of AcFaNaC (accession number XP_012938736.1), AkFaNaC (accession number BAE07082.1), HtFaNaC (accession number AF80601.1), LsFaNaC (accession number AAK20896.1), HaFaNaC (accession number CAA63084.1), and cASIC1 (accession number AAY28986.1). Secondary structures are colored as in Fig. 1d and are indicated by cylinders (helices), arrows (β-strands), solid line (loop), and dashed line (disordered region). Conserved residues are highlighted in red. Purple and yellow crosses mark residues involved in FMRFamide binding from one subunit and the neighboring subunit, respectively. Green triangles mark previously proposed key residues important for peptide affinity differences. The purple triangle marks Phe 474 that shows a dramatic conformational change upon peptide binding. Blue circles mark residues that are potentially important for ion selectivity based on studies on ASIC1. Specific insertion I&II, the β6–β7-loop and the HG and GxS motifs are underlined and labeled. Multiple sequence alignment was performed using Clustal Omega (https://www.ebi.ac.uk/Tools/msa/clustalo/), and this figure is prepared using ESPript server (https://espript.ibcp.fr/ESPript/ESPript/).
