Coagulation factor II receptor

Coagulation factor II (thrombin) receptor
Identifiers
Symbol(s)	F2R; CF2R; HTR; PAR1; TR
External IDs	OMIM: 187930 MGI: 101802 Homologene: 1510
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
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	2149	14062
Ensembl	ENSG00000181104	ENSMUSG00000048376
Uniprot	P25116	Q3UK34
Refseq	NM_001992 (mRNA) NP_001983 (protein)	NM_010169 (mRNA) NP_034299 (protein)
Location	Chr 5: 76.05 - 76.07 Mb	Chr 13: 96.7 - 96.72 Mb
Pubmed search	[1]	[2]

Coagulation factor II (thrombin) receptor, also known as F2R or protease activated receptor 1 (PAR1) is a human 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.

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. PMID 1310691.
• 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/. 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. 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. 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. PMID 8290554.
• Hoffman M, Church FC (1993). "Response of blood leukocytes to thrombin receptor peptides.". J. Leukoc. Biol. 54 (2): 145-51. PMID 8395550.
• Bahou WF, Nierman WC, Durkin AS, et al. (1993). "Chromosomal assignment of the human thrombin receptor gene: localization to region q13 of chromosome 5.". Blood 82 (5): 1532-7. PMID 8395910.
• 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. 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. 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. 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. 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. 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. Template:Membrane-protein-stub