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=='''The Adiponectin receptor 1'''==

<StructureSection load='3wxv' size='340' side='right' caption='Adiponectin receptor 1 (AdipoR1) structure' scene=''>

[[The Adiponectin receptor 1]] is one of the two receptors for the hormone called adiponectin.

The function of adipoR1 is directly linked with the '''adiponectin'''. It is an hormone, and more precisely an adipokine <ref name="doc1">Tanabe, Hiroaki, Yoshifumi Fujii, Miki Okada-Iwabu, Masato Iwabu, Yoshihiro Nakamura, Toshiaki Hosaka, Kanna Motoyama, et al. « Crystal structures of the human adiponectin receptors ». Nature 520, nᵒ 7547 (1 avril 2015): 312‑16. https://doi.org/10.1038/nature14301</ref> <ref name="doc8">Kadowaki, Takashi et al. “Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome.” The Journal of clinical investigation vol. 116,7 (2006): 1784-92. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1483172/</ref>, present in the blood at high concentration, approximatively 0,01 % of the total amount of proteins in plasma<ref name="doc7">Whitehead, J. P., A. A. Richards, I. J. Hickman, G. A. Macdonald, et J. B. Prins. « Adiponectin – a Key Adipokine in the Metabolic Syndrome ». Diabetes, Obesity and Metabolism 8, nᵒ 3 (2006): 264‑80. https://doi.org/10.1111/j.1463-1326.2005.00510.x.</ref>.The human adiponectin monomer as molecular weight of about 28 kDa and is composed of 244 amino acids. However, the molecular weight of the hormone depends on the multimerization of this one <ref name="doc7"/>.  The hormone is mainly created by adipocytes present in brown and white adipose tissues but according to researches it could also be produced in some non-adipose tissues as in skeletal muscle <ref name="doc7"/><ref name="doc8"/>.Two forms of adiponectin exist: the full-length adiponectin, presents in the liver and the globular adiponectin presents in skeletal muscles and in the liver.The adiponectin receptor 1 is a receptor sensitive in particular to the globular form<ref name="doc8"/>. This hormone is known to be anti-diabetic, antiatherogenic and a regulator of tissue inflammation and insulin sensitivity<ref name="doc9">Yamauchi, Toshimasa, Junji Kamon, Yusuke Ito, Atsushi Tsuchida, Takehiko Yokomizo, Shunbun Kita, Takuya Sugiyama, et al. « Cloning of adiponectin receptors that mediate antidiabetic metabolic effects ». Nature 423, nᵒ 6941 (1 juin 2003): 762‑69. https://doi.org/10.1038/nature01705.</ref>. These properties of the adiponectin are linked to the fatty oxidation trigger by the hormone and the adipoR1 receptor. Different fatty acid oxidation pathway exists. The major pathway regulated by adipoR1 is the AMP kinase channel, but this pathway is not completely known. However, several studies show that adipoR1 decreases the hepatic glucose production by activating this channel. AdipoR1 is also able to limit the expression of enzymes, like glucose-6-phosphatase, [[phosphoenolpyruvate carboxykinase]] and carboxykinase1, involved in gluconeogenesis<ref name="doc9">Capeau, Jacqueline. « The Story of Adiponectin and Its Receptors AdipoR1 and R2: To Follow ». Journal of Hepatology 47, nᵒ 5 (1 novembre 2007): 736‑38. https://doi.org/10.1016/j.jhep.2007.06.002.</ref>  

The '''Adiponectin receptor''' 1 is an integral membrane protein composed of 375 amino acids and its molecular weight is 42,4 kDa. This protein can be decomposed into different parts: an internal <scene name='82/829353/N-terminus_domain/2'>N-terminus domain</scene> (residues 89 to 120), a short intracellular domain called <scene name='82/829353/Helice0/2'>helix 0</scene> (residues 121 to 129), <scene name='82/829353/7helices/1'>seven transmembrane helices</scene> (residues 134 to 364) and an external <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene> (residues 365 to 375). <ref name="doc1"/>