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. 2023 Sep 4;9(10):1697–1708. doi: 10.1038/s41477-023-01510-0

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© The Author(s) 2023

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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Extended Data Fig. 2 — Sequence alignments of ABCG25 and its human homologues with determined structures, including hABCG1, hABCG2, hABCG5 and hABCG8. The amino acid sequences are available at Uniprot (https://www.uniprot.org) with the following accession codes: ABCG25 - Q84TH5, hABCG1 - P45844, hABCG2 - Q9UNQ0, hABCG5 - Q9H222, hABCG8 - Q9H221. Sequences are aligned using Clustal O (1.2.4). Secondary structural elements of ABCG25 are indicated above the sequence. Invariant amino acids are shaded red. Key residues involved in ATP-binding and hydrolysis are indicated by pink star. Residues surrounding ABA are indicated by blue stars.