F2RL2

F2RL2
Identifiers
Aliases	F2RL2, PAR-3, PAR3, coagulation factor II thrombin receptor like 2
External IDs	MGI: 1298208 HomoloGene: 36151 GeneCards: F2RL2
Gene ontology Molecular function • thrombin-activated receptor activity • protein binding • signal transducer activity • phosphatidylinositol phospholipase C activity • G-protein coupled receptor activity Cellular component • integral component of membrane • extracellular region • plasma membrane • integral component of plasma membrane • apical plasma membrane • membrane Biological process • platelet activation • hemostasis • thrombin-activated receptor signaling pathway • G-protein coupled receptor signaling pathway • blood coagulation • response to wounding • signal transduction • positive regulation of Rho protein signal transduction • positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2151	14064
Ensembl	ENSG00000164220	ENSMUSG00000021675
UniProt	O00254	O08675
RefSeq (mRNA)	NM_004101 NM_001256566	NM_010170
RefSeq (protein)	NP_001243495 NP_004092	NP_034300.3 NP_034300
Location (UCSC)	Chr 5: 76.62 – 76.62 Mb	Chr 13: 95.7 – 95.7 Mb
PubMed search
Wikidata
View/Edit Human		View/Edit Mouse

Protease activated receptor 3 (PAR-3) also known as coagulation factor II receptor-like 2 (F2RL2) and thrombin receptor-like 2, is a protein that in humans is encoded by the F2RL2 gene.

Function

Coagulation factor II (thrombin) receptor-like 2 (F2RL2) is a member of the large family of 7-transmembrane receptors that couple to G proteins. F2RL2 is also a member of the protease-activated receptor family and activated by thrombin. F2RL2 is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. F2RL2 is a cofactor for F2RL3 activation by thrombin. It mediates thrombin-triggered phosphoinositide hydrolysis and is expressed in a variety of tissues.

See also

• Protease-activated receptor

Further reading

• Hollenberg MD, Compton SJ (2002). "International Union of Pharmacology. XXVIII. Proteinase-activated receptors.". Pharmacol. Rev. 54 (2): 203–17. doi:10.1124/pr.54.2.203. PMID 12037136. 
• Ishihara H, Connolly AJ, Zeng D, et al. (1997). "Protease-activated receptor 3 is a second thrombin receptor in humans.". Nature. 386 (6624): 502–6. doi:10.1038/386502a0. PMID 9087410. 
• Schmidt VA, Nierman WC, Maglott DR, et al. (1998). "The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets.". J. Biol. Chem. 273 (24): 15061–8. doi:10.1074/jbc.273.24.15061. PMID 9614115. 
• Xu WF, Andersen H, Whitmore TE, et al. (1998). "Cloning and characterization of human protease-activated receptor 4". Proc. Natl. Acad. Sci. U.S.A. 95 (12): 6642–6. doi:10.1073/pnas.95.12.6642. PMC 22580. PMID 9618465. 
• Guyonnet Dupérat V, Jacquelin B, Boisseau P, et al. (1998). "Protease-activated receptor genes are clustered on 5q13". Blood. 92 (1): 25–31. PMID 9639495. 
• Kahn ML, Zheng YW, Huang W, et al. (1998). "A dual thrombin receptor system for platelet activation". Nature. 394 (6694): 690–4. doi:10.1038/29325. PMID 9716134. 
• Kahn ML, Hammes SR, Botka C, Coughlin SR (1998). "Gene and locus structure and chromosomal localization of the protease-activated receptor gene family". J. Biol. Chem. 273 (36): 23290–6. doi:10.1074/jbc.273.36.23290. PMID 9722561. 
• Kahn ML, Nakanishi-Matsui M, Shapiro MJ, et al. (1999). "Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin". J. Clin. Invest. 103 (6): 879–87. doi:10.1172/JCI6042. PMC 408153. PMID 10079109. 
• Hauck RW, Schulz C, Schömig A, et al. (1999). "alpha-Thrombin stimulates contraction of human bronchial rings by activation of protease-activated receptors". Am. J. Physiol. 277 (1 Pt 1): L22–9. PMID 10409227. 
• Nakanishi-Matsui M, Zheng YW, Sulciner DJ, et al. (2000). "PAR3 is a cofactor for PAR4 activation by thrombin". Nature. 404 (6778): 609–13. doi:10.1038/35007085. PMID 10766244. 
• O'Brien PJ, Prevost N, Molino M, et al. (2000). "Thrombin responses in human endothelial cells. Contributions from receptors other than PAR1 include the transactivation of PAR2 by thrombin-cleaved PAR1". J. Biol. Chem. 275 (18): 13502–9. doi:10.1074/jbc.275.18.13502. PMID 10788464. 
• Cumashi A, Ansuini H, Celli N, et al. (2001). "Neutrophil proteases can inactivate human PAR3 and abolish the co-receptor function of PAR3 on murine platelets". Thromb. Haemost. 85 (3): 533–8. PMID 11307827. 
• Sambrano GR, Weiss EJ, Zheng YW, et al. (2001). "Role of thrombin signalling in platelets in haemostasis and thrombosis". Nature. 413 (6851): 74–8. doi:10.1038/35092573. PMID 11544528. 
• Miike S, McWilliam AS, Kita H (2002). "Trypsin induces activation and inflammatory mediator release from human eosinophils through protease-activated receptor-2". J. Immunol. 167 (11): 6615–22. doi:10.4049/jimmunol.167.11.6615. PMID 11714832. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
• Even-Ram SC, Grisaru-Granovsky S, Pruss D, et al. (2003). "The pattern of expression of protease-activated receptors (PARs) during early trophoblast development". J. Pathol. 200 (1): 47–52. doi:10.1002/path.1338. PMID 12692840. 
• Owen WG (2003). "PAR-3 is a low-affinity substrate, high affinity effector of thrombin". Biochem. Biophys. Res. Commun. 305 (1): 166–8. doi:10.1016/S0006-291X(03)00732-0. PMID 12732212. 
• Tanaka N, Morita T, Nezu A, et al. (2003). "Thrombin-induced Ca2+ mobilization in human gingival fibroblasts is mediated by protease-activated receptor-1 (PAR-1)". Life Sci. 73 (3): 301–10. doi:10.1016/S0024-3205(03)00269-8. PMID 12757837. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.