Coagulation factor II thrombin receptor-like 2 (F2RL2)

Coagulation factor II thrombin receptor-like 2 (F2RL2), also known as proteinase-activated receptor 3 (PAR3), is a member of the protease-activated receptor (PAR) subfamily within the seven-transmembrane G protein-coupled receptor (GPCR) superfamily[1][2][3][5][7]. It is activated by thrombin, which cleaves its N-terminal extracellular domain to generate a tethered ligand that activates the receptor. F2RL2 functions as a cofactor for PAR4 activation and is essential in hemostasis and thrombosis. It is expressed in multiple tissues and participates in diverse processes including signal transduction, platelet activation, pain modulation, metabolic regulation (including stimulation of insulin secretion from pancreatic beta-cells), and, when dysregulated, carcinoma biology and inflammation. While not currently a direct drug target in approved therapeutics, it is an important mediator of thrombin signaling and considered a potential future therapeutic target in thrombosis, metabolic, and oncological diseases[1][2][3][7].

Other names

Proteinase-activated receptor 3PAR3PAR-3Coagulation factor II receptor-like 2Thrombin receptor-like 2proteinase-activated receptor-3

Proteolytic activation by thrombin, which cleaves the extracellular domain to reveal a tethered ligand, initiating G protein-coupled signaling - Functions as a cofactor for PAR4 activation