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. 2023 Jun 20;222(9):e202208047. doi: 10.1083/jcb.202208047

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© 2023 Sato-Nishiuchi et al.

This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).

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Figure 5. — Multiple sequence alignment of CCP20 domains. The amino acid sequences of the CCP20 domains of mouse, human, rabbit, chicken, Xenopus, and zebrafish Polydom were aligned by ClustalW. The asterisks denote identical amino acids, while the colons and periods denote strongly similar and weakly similar amino acids, respectively. The glutamate (E) and glycine (G) residues corresponding to E2567 and G2568 in mouse Polydom (highlighted in pink), which are critically required for Tie1 binding, are conserved in these animals.