F2R
Description
The F2R (coagulation factor II thrombin receptor) is a protein-coding gene located on chromosome 5.
Proteinase-activated receptor 1 (PAR1), also known as protease-activated receptor 1, coagulation factor II receptor, and thrombin receptor, is a protein encoded by the F2R gene. PAR1 is a G protein-coupled receptor and one of four protease-activated receptors involved in regulating thrombotic responses. Highly expressed in platelets and endothelial cells, PAR1 plays a key role in mediating the interplay between coagulation and inflammation, which is important in the pathogenesis of inflammatory and fibrotic lung diseases. It is also involved in both the disruption and maintenance of endothelial barrier integrity through interaction with either thrombin or activated protein C, respectively.
PAR1 is a transmembrane G-protein-coupled receptor (GPCR) that shares much of its structure with other protease-activated receptors. These characteristics include seven transmembrane alpha helices, four extracellular loops, and three intracellular loops. PAR1 specifically contains 425 amino acid residues arranged for optimal binding of thrombin at its extracellular N-terminus. The C-terminus of PAR1 is located on the intracellular side of the cell membrane as part of its cytoplasmic tail.
PAR1 is activated when the terminal 41 amino acids of its N-terminus are cleaved by thrombin, a serine protease. Thrombin recognizes PAR1 by a Lysine-Aspartate-Proline-Arginine-Serine sequence at the N-terminal, where it cuts the peptide bond between Arginine-41 and Serine-42.
High-affinity receptor for activated thrombin, coupled to G proteins that stimulate phosphoinositide hydrolysis. Plays a role in platelet activation and vascular development.
F2R is also known as CF2R, HTR, PAR-1, PAR1, TR.
