Ghrelin receptor in GtoPdb v.2023.1

The ghrelin receptor (nomenclature as agreed by the NC-IUPHAR Subcommittee for Ghrelin [19]) is activated a 28 amino-acid peptide originally isolated from rat stomach, where it cleaved 117 precursor (GHRL, Q9UBU3). human gene encoding has 83% sequence homology to prepro-ghrelin, although mature peptides and differ only two amino acids [75]. Alternative splicing results in formation of second peptide, [des-Gln14]ghrelin with equipotent biological activity [50]. A unique post-translational modification (octanoylation Ser3, catalysed Ο-acyltransferase (MBOAT4, Q96T53) [134] occurs both peptides, essential full binding receptors hypothalamus pituitary, release growth hormone pituitary [59]. Structure studies showed first five N-terminal be minimum required [4], mutagenesis indicated overlap site those small molecule agonists allosteric modulators function [45]. An endogenous antagonist inverse agonist called Liver enriched antimicrobial 2 (Leap2), expressed primarily hepatocytes enterocytes proximal intestine [36, 69] inhibits receptor-induced GH secretion food intake [36]. Leap2 inversely regulated under various metabolic conditions [72]. In cell systems, constitutively active [46], but this abolished naturally occurring mutation (A204E) that decreased surface expression associated familial short stature [94].