ZFIN Image: Vona et al., 2021, Fig. 2

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Figure Caption

Fig. 2

Conservation of the p.Thr165 residue, and clarin 1/clarin 2 alignment. a Overview of clarin 2 protein and modular structure of the PMP-22/EMP/EP20/Claudin superfamily, with amino acid residue coordinates and position of the p.(Thr165Lys) substitution shown (upper panel). An alignment of the amino acid sequences from the segment of clarin 2 (represented by dashed lines) from vertebrate species shows the Thr165 position (asterisk) is well conserved among vertebrates. b Alignment of clarin 2 (UniProtKB: A0PK11, upper alignment) and clarin 1 (UniProtKB: P58418, lower alignment) amino acid residues. Transmembrane domains are marked in grey, conservation is shown in yellow, and consensus sequences are shown below for the 232 amino acid proteins. Missense and nonsense variants in clarin 1 (Deafness Variation Database v8.2) and clarin 2 (present study, asterisk) are marked in red. c The predicted secondary structure of human clarin 2 (NP_001073296.1) wild-type (Thr165) and mutated (Thr165Lys) protein. H represents alpha-helix, S represents beta-strand and C represents coil

Acknowledgments

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