Apelin receptor in GtoPdb v.2023.1

Anthony P. Davenport; Matthias Kleinz; Janet J. Maguire; Thomas L. Williams; Peiran Yang

doi:10.2218/gtopdb/F7/2023.1

Anthony P. Davenport University of Cambridge https://orcid.org/0000-0002-2096-3117
Matthias Kleinz University of Cambridge
Janet J. Maguire University of Cambridge https://orcid.org/0000-0002-9254-7040
Thomas L. Williams University of Cambridge
Peiran Yang University of Cambridge

Abstract

The apelin receptor (nomenclature as agreed by the NC-IUPHAR Subcommittee on the apelin receptor [73] and subsequently updated [75]) responds to apelin, a 36 amino-acid peptide derived initially from bovine stomach. apelin-36, apelin-13 and [Pyr¹]apelin-13 are the predominant endogenous ligands which are cleaved from a 77 amino-acid precursor peptide (APLN, Q9ULZ1) [88]. A second family of peptides discovered independently and named Elabela [13] or Toddler, that has little sequence similarity to apelin, is present, and functional at the apelin receptor in the adult cardiovascular system [97, 71]. The enzymatic pathways generating biologically active apelin and Elabela isoforms have not been determined but both propeptides include sites for potential proprotein convertase processing [81]. Structure-activity relationship Elabela analogues have been described [65, 90]. The stoichiometry of apelin receptor-heterotrimeric G protein complexes has been studied using cryogenic-electron microscopy [98].

DOI: https://doi.org/10.2218/gtopdb/F7/2023.1