The Proteinase-activated receptor 2 (PAR2) is a member of the proteinase-activated receptor subfamily. It is activated through proteolytic exposure of an occult tethered ligand by trypsin and trypsin-like proteases. This is in contrast to other members of the subfamily which are activated by the protease thrombin. PAR2 has been implicated in acute inflammatory response, asthma, and pain transmission. PAR2 expression has been documented in the periphery. ESTs have been isolated from adrenal, brain, breast, heart/melanocyte/uterus, kidney, lung, and vessel libraries.
Coagulation factor II (thrombin) receptor-like 1 (F2RL1)is a member of the large family of 7-transmembrane-region receptors that couple to guanosine-nucleotide-binding proteins. F2RL1 is also a member of the protease-activated receptor family. It is activated by trypsin, but not by thrombin. It is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. The F2RL1 gene contains two exons and is widely expressed in human tissues. The predicted protein sequence is 83% identical to the mouse receptor sequence. [provided by RefSeq].