F2RL1

From Wikipedia, the free encyclopedia


Coagulation factor II (thrombin) receptor-like 1
Identifiers
Symbol(s) F2RL1; GPR11; PAR2
External IDs OMIM: 600933 MGI101910 HomoloGene21087
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 2150 14063
Ensembl ENSG00000164251 ENSMUSG00000021678
Uniprot P55085 Q3TU81
Refseq NM_005242 (mRNA)
NP_005233 (protein)
NM_007974 (mRNA)
NP_032000 (protein)
Location Chr 5: 76.15 - 76.17 Mb Chr 13: 96.61 - 96.63 Mb
Pubmed search [1] [2]

Coagulation factor II (thrombin) receptor-like 1, also known as F2RL1 or protease activated receptor 2 (PAR2), is a human gene.

Coagulation factor II (thrombin) receptor-like 1 (F2RL1) is a member of the large family of 7-transmembrane 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.[1]

[edit] See also

[edit] References

[edit] Further reading

  • Kunzelmann K, Schreiber R, König J, Mall M (2003). "Ion transport induced by proteinase-activated receptors (PAR2) in colon and airways.". Cell Biochem. Biophys. 36 (2-3): 209–14. PMID 12139406. 
  • Kawabata A (2004). "PAR-2: structure, function and relevance to human diseases of the gastric mucosa.". Expert reviews in molecular medicine 4 (16): 1–17. doi:10.1017/S1462399402004799. PMID 14585156. 
  • Bushell T (2007). "The emergence of proteinase-activated receptor-2 as a novel target for the treatment of inflammation-related CNS disorders.". J. Physiol. (Lond.) 581 (Pt 1): 7–16. doi:10.1113/jphysiol.2007.129577. PMID 17347265. 
  • Nystedt S, Emilsson K, Larsson AK, et al. (1995). "Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2.". Eur. J. Biochem. 232 (1): 84–9. PMID 7556175. 
  • Santulli RJ, Derian CK, Darrow AL, et al. (1995). "Evidence for the presence of a protease-activated receptor distinct from the thrombin receptor in human keratinocytes.". Proc. Natl. Acad. Sci. U.S.A. 92 (20): 9151–5. PMID 7568091. 
  • Nystedt S, Emilsson K, Wahlestedt C, Sundelin J (1994). "Molecular cloning of a potential proteinase activated receptor.". Proc. Natl. Acad. Sci. U.S.A. 91 (20): 9208–12. PMID 7937743. 
  • Mirza H, Yatsula V, Bahou WF (1996). "The proteinase activated receptor-2 (PAR-2) mediates mitogenic responses in human vascular endothelial cells.". J. Clin. Invest. 97 (7): 1705–14. PMID 8601636. 
  • Bohm SK, Kong W, Bromme D, et al. (1996). "Molecular cloning, expression and potential functions of the human proteinase-activated receptor-2.". Biochem. J. 314 ( Pt 3): 1009–16. PMID 8615752. 
  • Böhm SK, Khitin LM, Grady EF, et al. (1996). "Mechanisms of desensitization and resensitization of proteinase-activated receptor-2.". J. Biol. Chem. 271 (36): 22003–16. PMID 8703006. 
  • Kahn M, Ishii K, Kuo WL, et al. (1996). "Conserved structure and adjacent location of the thrombin receptor and protease-activated receptor 2 genes define a protease-activated receptor gene cluster.". Mol. Med. 2 (3): 349–57. PMID 8784787. 
  • Molino M, Barnathan ES, Numerof R, et al. (1997). "Interactions of mast cell tryptase with thrombin receptors and PAR-2.". J. Biol. Chem. 272 (7): 4043–9. PMID 9020112. 
  • Howells GL, Macey MG, Chinni C, et al. (1997). "Proteinase-activated receptor-2: expression by human neutrophils.". J. Cell. Sci. 110 ( Pt 7): 881–7. PMID 9133675. 
  • D'Andrea MR, Derian CK, Leturcq D, et al. (1998). "Characterization of protease-activated receptor-2 immunoreactivity in normal human tissues.". J. Histochem. Cytochem. 46 (2): 157–64. PMID 9446822. 
  • 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. 
  • Steinhoff M, Corvera CU, Thoma MS, et al. (1999). "Proteinase-activated receptor-2 in human skin: tissue distribution and activation of keratinocytes by mast cell tryptase.". Exp. Dermatol. 8 (4): 282–94. PMID 10439226. 
  • Takeuchi T, Harris JL, Huang W, et al. (2000). "Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates.". J. Biol. Chem. 275 (34): 26333–42. doi:10.1074/jbc.M002941200. PMID 10831593. 
  • Loew D, Perrault C, Morales M, et al. (2000). "Proteolysis of the exodomain of recombinant protease-activated receptors: prediction of receptor activation or inactivation by MALDI mass spectrometry.". Biochemistry 39 (35): 10812–22. PMID 10978167. 
  • Knight DA, Lim S, Scaffidi AK, et al. (2001). "Protease-activated receptors in human airways: upregulation of PAR-2 in respiratory epithelium from patients with asthma.". J. Allergy Clin. Immunol. 108 (5): 797–803. doi:10.1067/mai.2001.119025. PMID 11692107. 
  • 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. PMID 11714832. 
  • Asokananthan N, Graham PT, Fink J, et al. (2002). "Activation of protease-activated receptor (PAR)-1, PAR-2, and PAR-4 stimulates IL-6, IL-8, and prostaglandin E2 release from human respiratory epithelial cells.". J. Immunol. 168 (7): 3577–85. PMID 11907122. 

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