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. 2020 Mar 10;10:4429. doi: 10.1038/s41598-020-61370-y

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© The Author(s) 2020

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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Gpr176 is an N-glycosylated GPCR. (A) Amino acid sequence conservation of the potential N-glycosylation sites in the N-terminal and extracellular loop 3 (ECL3) region of mouse, rat, baboon, and human Gpr176. Sequences that match the consensus N-linked glycosylation motif (N-X-S/T, where X is not P) are highlighted in magenta in the alignments as well as in the snake-plot representation of mouse Gpr176. (B,C) Immunoblot of mouse hypothalamus SCN cell extracts from WT and Gpr176^−/− mice for Gpr176 (B). The WT extracts were treated with vehicle or either PNGase F or O-glycosidase (O-glyc) and immunoblotted for Gpr176 (C). Two independent biological replicates per condition were loaded in (C). Note that a broad, heterogeneous band with an apparent molecular mass of 75 kDa was detectable in only the WT extracts. The asterisk indicates the position of deglycosylated Gpr176.