Introduction of ADGRG5
ADGRG5, also known as G-protein coupled receptor 114 (GPR114) or G-protein coupled receptor PGR27 (PGR27), is a protein encoded by the ADGRG5 gene. It is a member of the adhesion GPCR family which are characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
|Basic Information of ADGRG5|
|Protein Name||Adhesion G-protein coupled receptor G5|
|Aliases||G-protein coupled receptor 114, G-protein coupled receptor PGR27|
|Organism||Homo sapiens (Human)|
Function of ADGRG5 Membrane Protein
The G protein-coupled receptors (GPCRs) are a large family of integral membrane proteins that generally act as cell surface receptors responsible for the transduction of a remarkable diversity of endogenous signals into a cellular response. Expression of some adhesion GPCR subfamilies initially appeared confined to distinct cell types or organs, like the immune system or the central nervous system (CNS). As a member of GPCRs, ADGRG5 has the basic molecular architecture with seven hydrophobic regions of 25-35 consecutive residues. Studies have shown that ADGRG5 is specifically expressed in human eosinophils as well as in mouse lymphocytes, monocytes, macrophage, and dendritic cells. And, a variant (rs9937918) of ADGRG5 has been found to be associated with differences in vitamin D3 metabolism. What’s more, it has been reported that ADGRG5 may also have the ability to mediate hematopoietic stem cell repopulation and retention of myeloid cells within the bone marrow niche.
Application of ADGRG5 Membrane Protein in Literature
1. Stoveken HM., et.al. Gedunin-and Khivorin-Derivatives Are Small-Molecule Partial Agonists for Adhesion G Protein-Coupled Receptors GPR56/ADGRG1 and GPR114/ADGRG5. Molecular pharmacology. 2018, 93(5): 477-88. PubMed ID: 29476042
This article finds a novel group of aGPCR partial agonists that will serve as invaluable resources for understanding the unique class receptors.
2. Wilde C., et.al. The constitutive activity of the adhesion GPCR GPR114/ADGRG5 is mediated by its tethered agonist. The FASEB Journal. 2015, 30(2): 666-73. PubMed ID: 26499266
This article suggests that the N-terminal half of the Stachel sequence confers the agonistic activity, whereas the C-terminal part orientates the agonistic core sequence to the transmembrane domain. It indicates that the proposed mechanism of Stachel-mediated activation is relevant not only to GPR114 but to a GPCRs in general.
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