Aliases for F2R Gene
External Ids for F2R Gene
Coagulation factor II receptor is a 7-transmembrane receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor. F2R is a G-protein coupled receptor family member. [provided by RefSeq, Jul 2008]
GeneCards Summary for F2R Gene
F2R (Coagulation Factor II (Thrombin) Receptor) is a Protein Coding gene. Diseases associated with F2R include melanoma metastasis. Among its related pathways are PI3K-Akt signaling pathway and Ras signaling pathway. GO annotations related to this gene include G-protein coupled receptor activity and G-protein alpha-subunit binding. An important paralog of this gene is GPR132.
UniProtKB/Swiss-Prot for F2R Gene
High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.
Protease-activated receptors (PARs, also known as thrombin receptors) are G-protein-coupled receptors, activated by cleavage of their N-terminal domains by serine proteases. Hydrolysis reveals a tethered peptide ligand, which interacts with the receptor within extracellular loop-2 to affect transmembrane signaling. Four subtypes of receptors have so far been cloned (PAR1-4). PAR1 is the most well characterized member of this receptor family and is activated by the endogenous serine protease thrombin. Thrombin has a primary role in vessel wound healing and revascularization and acts via PAR1 receptors on platelets, endothelial cells, smooth muscle cells, neutrophils, leukocytes, neurons and glial cells to facilitate a coordinated response to vessel damage. Thrombin-mediated PAR1 activation induces platelet aggregation. Thrombin stimulates 5-HT, ATP and thromboxane A2 release, integrin alphaIIb/beta3 activation, and P-selectin and CD40 translocation to facilitate the binding of platelets to endothelial cells. Activation of endothelial cells is a key component in clotting and wound healing, and is mediated by PAR1 stimulation. Activation of PAR1 by thrombin stimulates von Willebrand factor release, tissue factor expression and adhesion molecule expression, which further promotes clotting and coagulation as well as facilitating the rapid adherence of neutrophils, monocytes and lymphocytes to endothelial cells. Thrombin has direct promitogenic activity in fibroblasts, vascular smooth muscle cells, endothelial cells and some myeloid cells. Thrombin-mediated PAR1 activation also induces expression of promitogenic factors and their receptors such as PDGF/PDGFR and ET-1/ETA and ET-B. PAR1 is known to couple to several heterotrimeric G proteins and regulates multiple kinase signaling pathways including PI 3-K, Src family tyrosine kinases, JNK, Rho kinases, JAK2 and FAK.