Coagulation factor II receptor

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Coagulation factor II (thrombin) receptor
Identifiers
Symbols	F2R; CF2R; HTR; PAR1; TR
External IDs	OMIM: 187930 MGI: 101802 HomoloGene: 1510 IUPHAR: PAR1 GeneCards: F2R Gene
Gene Ontology Molecular function • rhodopsin-like receptor activity • receptor activity • receptor binding • thrombin receptor activity Cellular component • Golgi apparatus • plasma membrane • integral to plasma membrane Biological process • regulation of progression through cell cycle • apoptosis • caspase activation • cell motility • signal transduction • G-protein coupled receptor protein signaling pathway • tyrosine phosphorylation of STAT protein • STAT protein nuclear translocation • multicellular organismal development • blood coagulation • response to wounding • anatomical structure morphogenesis • positive regulation of I-kappaB kinase/NF-kappaB cascade Sources: Amigo / EGO
RNA expression pattern
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More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2149	14062
Ensembl	ENSG00000181104	ENSMUSG00000048376
UniProt	P25116	Q3UK34
RefSeq (mRNA)	NM_001992	NM_010169
RefSeq (protein)	NP_001983	NP_034299
Location (UCSC)	Chr 5: 76.05 - 76.07 Mb	Chr 13: 96.7 - 96.72 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 Freely accessible. PMID 1310691. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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 Freely accessible. PMID 8290554. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

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