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Contents

   



(Top)
 


1 Function  





2 See also  





3 References  





4 Further reading  














F2RL3







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F2RL3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesF2RL3, PAR4, F2R like thrombin/trypsin receptor 3, F2R like thrombin or trypsin receptor 3
External IDsOMIM: 602779; MGI: 1298207; HomoloGene: 36148; GeneCards: F2RL3; OMA:F2RL3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003950

NM_007975

RefSeq (protein)

NP_003941

NP_032001

Location (UCSC)Chr 19: 16.89 – 16.89 MbChr 8: 73.49 – 73.49 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protease-activated receptor 4 (PAR-4), also known as coagulation factor II (thrombin) receptor-like 3, is a protein that in humans is encoded by the F2RL3 gene.[5]

Function[edit]

Coagulation factor II (thrombin) receptor-like 3 (F2RL3) is a member of the large family of 7-transmembrane-region receptors that couple to guanosine-nucleotide-binding proteins. F2RL3 is also a member of the protease-activated receptor family. F2RL3 is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. F2RL3 is activated by thrombin and trypsin.[5]

See also[edit]

References[edit]

  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ a b "Entrez Gene: F2RL3 coagulation factor II (thrombin) receptor-like 3".
  • Further reading[edit]

  • 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. Bibcode:1998PNAS...95.6642X. doi:10.1073/pnas.95.12.6642. PMC 22580. PMID 9618465.
  • Kahn ML, Zheng YW, Huang W, et al. (1998). "A dual thrombin receptor system for platelet activation". Nature. 394 (6694): 690–4. Bibcode:1998Natur.394..690K. doi:10.1038/29325. PMID 9716134. S2CID 4408582.
  • 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. S2CID 32777201.
  • 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.
  • Andersen H, Greenberg DL, Fujikawa K, et al. (1999). "Protease-activated receptor 1 is the primary mediator of thrombin-stimulated platelet procoagulant activity". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11189–93. Bibcode:1999PNAS...9611189A. doi:10.1073/pnas.96.20.11189. PMC 18009. PMID 10500152.
  • Sambrano GR, Huang W, Faruqi T, et al. (2000). "Cathepsin G activates protease-activated receptor-4 in human platelets". J. Biol. Chem. 275 (10): 6819–23. doi:10.1074/jbc.275.10.6819. PMID 10702240. S2CID 33219053.
  • Nakanishi-Matsui M, Zheng YW, Sulciner DJ, et al. (2000). "PAR3 is a cofactor for PAR4 activation by thrombin". Nature. 404 (6778): 609–13. Bibcode:2000Natur.404..609N. doi:10.1038/35007085. PMID 10766244. S2CID 4410800.
  • 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. S2CID 9302877.
  • 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. doi:10.4049/jimmunol.168.7.3577. PMID 11907122. S2CID 45171728.
  • Henriksen RA, Hanks VK (2002). "PAR-4 agonist AYPGKF stimulates thromboxane production by human platelets". Arterioscler. Thromb. Vasc. Biol. 22 (5): 861–6. doi:10.1161/01.ATV.0000014742.56572.25. PMID 12006403. S2CID 24246544.
  • Covic L, Singh C, Smith H, Kuliopulos A (2003). "Role of the PAR4 thrombin receptor in stabilizing platelet-platelet aggregates as revealed by a patient with Hermansky-Pudlak syndrome". Thromb. Haemost. 87 (4): 722–7. doi:10.1055/s-0037-1613071. PMID 12008957. S2CID 32831294.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • 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.
  • Adam F, Verbeuren TJ, Fauchère JL, et al. (2003). "Thrombin-induced platelet PAR4 activation: role of glycoprotein Ib and ADP". J. Thromb. Haemost. 1 (4): 798–804. doi:10.1046/j.1538-7836.2003.00138.x. PMID 12871418. S2CID 12762388.
  • Wu CC, Hwang TL, Liao CH, et al. (2004). "The role of PAR4 in thrombin-induced thromboxane production in human platelets". Thromb. Haemost. 90 (2): 299–308. doi:10.1160/TH03-02-0103. PMID 12888878. S2CID 4983617.
  • Kawai T, Akira S, Reed JC (2003). "ZIP kinase triggers apoptosis from nuclear PML oncogenic domains". Mol. Cell. Biol. 23 (17): 6174–86. doi:10.1128/MCB.23.17.6174-6186.2003. PMC 180930. PMID 12917339.
  • Jacques SL, Kuliopulos A (2004). "Protease-activated receptor-4 uses dual prolines and an anionic retention motif for thrombin recognition and cleavage". Biochem. J. 376 (Pt 3): 733–40. doi:10.1042/BJ20030954. PMC 1223816. PMID 13678420.
  • Han Y, Nurden A, Combrié R, Pasquet JM (2004). "Redistribution of glycoprotein Ib within platelets in response to protease-activated receptors 1 and 4: roles of cytoskeleton and calcium". J. Thromb. Haemost. 1 (10): 2206–15. doi:10.1046/j.1538-7836.2003.00436.x. PMID 14521606. S2CID 24420859.
  • This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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