Coagulation factor II receptor

Coagulation factor II (thrombin) receptor
Rendering of F2R from PDB 1NRN
Available structures PDB 1NRN, 1NRO, 1NRP, 1NRQ, 1NRR, 3BEF, 3HKI, 3HKJ, 3LU9
Identifiers
Symbols	F2R; CF2R; HTR; PAR-1; PAR1; TR
External IDs	OMIM: 187930 MGI: 101802 HomoloGene: 1510 IUPHAR: PAR1 GeneCards: F2R Gene
Gene Ontology Molecular function • receptor activity • G-protein coupled receptor activity • G-protein coupled receptor activity • receptor binding • protein binding • thrombin receptor activity Cellular component • extracellular region • Golgi apparatus • plasma membrane • plasma membrane • plasma membrane • integral to plasma membrane • caveola • platelet dense tubular network • neuromuscular junction • postsynaptic membrane Biological process • activation of MAPKK activity • connective tissue replacement involved in inflammatory response wound healing • activation of caspase activity • inflammatory response • G-protein coupled receptor protein signaling pathway • G-protein coupled receptor protein signaling pathway • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway • tyrosine phosphorylation of STAT protein • STAT protein import into nucleus • establishment of synaptic specificity at neuromuscular junction • blood coagulation • positive regulation of cell proliferation • negative regulation of cell proliferation • response to wounding • anatomical structure morphogenesis • positive regulation of phosphatidylinositol 3-kinase cascade • death • platelet activation • platelet activation • regulation of blood coagulation • positive regulation of blood coagulation • positive regulation of cell migration • response to lipopolysaccharide • regulation of interleukin-1 beta production • positive regulation of collagen biosynthetic process • positive regulation of I-kappaB kinase/NF-kappaB cascade • positive regulation of caspase activity • positive regulation of MAPKKK cascade • negative regulation of neuron apoptosis • positive regulation of transcription, DNA-dependent • positive regulation of vasoconstriction • positive regulation of smooth muscle contraction • positive regulation of JAK-STAT cascade • homeostasis of number of cells within a tissue • positive regulation of release of sequestered calcium ion into cytosol • elevation of cytosolic calcium ion concentration involved in G-protein signaling coupled to IP3 second messenger • positive regulation of calcium ion transport • regulation of sensory perception of pain • platelet dense granule organization • thrombin receptor signaling pathway • thrombin receptor signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2149	14062
Ensembl	ENSG00000181104	ENSMUSG00000048376
UniProt	P25116	Q3UK34
RefSeq (mRNA)	NM_001992	NM_010169.3
RefSeq (protein)	NP_001983	NP_034299.2
Location (UCSC)	Chr 5: 76.01 – 76.03 Mb	Chr 13: 96.37 – 96.39 Mb
PubMed search	[1]	[2]

Proteinase-activated receptor 1 (PAR1) also known as the coagulation factor II (thrombin) receptor is a protein that in humans is encoded by the F2R gene. PAR1 is a G protein-coupled receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor.

Ligands

Several selective antagonists for the PAR1 receptor have been developed, for use as anti-clotting agents for the treatment of heart disease.

• SCH-530,348

See also

• Protease-activated receptor

Further reading

• Coughlin SR, Vu TK, Hung DT, Wheaton VI (1992). "Characterization of a functional thrombin receptor. Issues and opportunities". J. Clin. Invest. 89 (2): 351–5. doi:10.1172/JCI115592. PMC 442859. PMID 1310691. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442859. 
• Howell DC, Laurent GJ, Chambers RC (2002). "Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis". Biochem. Soc. Trans. 30 (2): 211–6. doi:10.1042/BST0300211. PMID 12023853. 
• Tellez C, Bar-Eli M (2003). "Role and regulation of the thrombin receptor (PAR-1) in human melanoma". Oncogene 22 (20): 3130–7. doi:10.1038/sj.onc.1206453. PMID 12789289. 
• Remillard CV, Yuan JX (2005). "PGE2 and PAR-1 in pulmonary fibrosis: a case of biting the hand that feeds you?". Am. J. Physiol. Lung Cell Mol. Physiol. 288 (5): L789–92. doi:10.1152/ajplung.00016.2005. PMID 15821019. 
• Leger AJ, Covic L, Kuliopulos A (2006). "Protease-activated receptors in cardiovascular diseases". Circulation 114 (10): 1070–7. doi:10.1161/CIRCULATIONAHA.105.574830. PMID 16952995. 
• Traynelis SF, Trejo J (2007). "Protease-activated receptor signaling: new roles and regulatory mechanisms". Curr. Opin. Hematol. 14 (3): 230–5. doi:10.1097/MOH.0b013e3280dce568. PMID 17414212. 
• Vu TK, Hung DT, Wheaton VI, Coughlin SR (1991). "Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation". Cell 64 (6): 1057–68. doi:10.1016/0092-8674(91)90261-V. PMID 1672265. 
• Wojtukiewicz MZ, Tang DG, Ben-Josef E, et al. (1995). "Solid tumor cells express functional "tethered ligand" thrombin receptor". Cancer Res. 55 (3): 698–704. PMID 7834643. 
• Hein L, Ishii K, Coughlin SR, Kobilka BK (1994). "Intracellular targeting and trafficking of thrombin receptors. A novel mechanism for resensitization of a G protein-coupled receptor". J. Biol. Chem. 269 (44): 27719–26. PMID 7961693. 
• Mathews II, Padmanabhan KP, Ganesh V, et al. (1994). "Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes". Biochemistry 33 (11): 3266–79. doi:10.1021/bi00177a018. PMID 8136362. 
• Offermanns S, Laugwitz KL, Spicher K, Schultz G (1994). "G proteins of the G12 family are activated via thromboxane A2 and thrombin receptors in human platelets". Proc. Natl. Acad. Sci. U.S.A. 91 (2): 504–8. doi:10.1073/pnas.91.2.504. PMC 42977. PMID 8290554. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42977. 
• Hoffman M, Church FC (1993). "Response of blood leukocytes to thrombin receptor peptides". J. Leukoc. Biol. 54 (2): 145–51. PMID 8395550. 
• Schmidt VA, Vitale E, Bahou WF (1996). "Genomic cloning and characterization of the human thrombin receptor gene. Structural similarity to the proteinase activated receptor-2 gene". J. Biol. Chem. 271 (16): 9307–12. doi:10.1074/jbc.271.16.9809. PMID 8621593. 
• Li F, Baykal D, Horaist C, et al. (1996). "Cloning and identification of regulatory sequences of the human thrombin receptor gene". J. Biol. Chem. 271 (42): 26320–8. doi:10.1074/jbc.271.42.26320. PMID 8824285. 
• Shapiro MJ, Trejo J, Zeng D, Coughlin SR (1997). "Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization". J. Biol. Chem. 271 (51): 32874–80. doi:10.1074/jbc.271.51.32874. PMID 8955127. 
• Ogino Y, Tanaka K, Shimizu N (1997). "Direct evidence for two distinct G proteins coupling with thrombin receptors in human neuroblastoma SH-EP cells". Eur. J. Pharmacol. 316 (1): 105–9. doi:10.1016/S0014-2999(96)00653-X. PMID 8982657. 
• Molino M, Bainton DF, Hoxie JA, et al. (1997). "Thrombin receptors on human platelets. Initial localization and subsequent redistribution during platelet activation". J. Biol. Chem. 272 (9): 6011–7. doi:10.1074/jbc.272.9.6011. PMID 9038223. 
• Renesto P, Si-Tahar M, Moniatte M, et al. (1997). "Specific inhibition of thrombin-induced cell activation by the neutrophil proteinases elastase, cathepsin G, and proteinase 3: evidence for distinct cleavage sites within the aminoterminal domain of the thrombin receptor". Blood 89 (6): 1944–53. PMID 9058715. 

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