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. 2022 Jul 26;474(8):771–781. doi: 10.1007/s00424-022-02733-4

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — Site of production and structure of uromodulin. Uromodulin is mainly produced by the cells that line the thick ascending limb (TAL), a segment involved in the reabsorption of NaCl and divalent cations, while being not permeable to water. Uromodulin is a glycosylphosphatidylinositol (GPI)-anchored protein which traffics to the apical membrane of the cells, where it is cleaved by the serine protease hepsin and released in the urine where it forms large polymers. These polymers form the matrix of the urinary casts. The predicted structure of uromodulin contains a leader peptide (L); four EGF-like domains (I to IV); a cysteine-rich D8C domain; a bipartite C‑terminal Zona Pellucida domain (ZP_N and ZP_C) connected by a linker; and a GPI-anchoring site at position 614. The seven N‑glycosylation sites are indicated by triangles. Figure adapted from Devuyst et al. [11, 12]