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. 2022 Jun 29;609(7927):605–610. doi: 10.1038/s41586-022-04883-y

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© The Author(s) 2022

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. 1 — Alignment between AtPIN1–8 with the following UniProt accession numbers. AtPIN1: Q9C6B8, AtPIN2: Q9LU77, AtPIN3: Q9S7Z8, AtPIN4: Q8RWZ6, AtPIN5: Q9FFD0, AtPIN6: Q9SQH6, AtPIN7: Q940Y5, AtPIN8: Q9LFP6. Conserved residues are highlighted with gray-scale, where black is perfectly conserved. Colored tubes represent α-helices found in the scaffold domain (blue) and transporter domain (green). Key residues are numbered above the α-helix markings. Residues highlighted participate in IAA carboxylate recognition (orange) or IAA hydrophobic recognition (yellow), are part of the support site (blue) or form the central prolines of the crossover motif (pink).