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Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]

 PAR2_HUMAN              Reviewed;         397 AA.
P55085; Q13317; Q13346; Q53XJ8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 167.
RecName: Full=Proteinase-activated receptor 2;
Short=PAR-2;
AltName: Full=Coagulation factor II receptor-like 1;
AltName: Full=G-protein coupled receptor 11;
AltName: Full=Thrombin receptor-like 1;
Contains:
RecName: Full=Proteinase-activated receptor 2, alternate cleaved 1;
Contains:
RecName: Full=Proteinase-activated receptor 2, alternate cleaved 2;
Flags: Precursor;
Name=F2RL1; Synonyms=GPR11, PAR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7556175; DOI=10.1111/j.1432-1033.1995.tb20784.x;
Nystedt S., Emilsson K., Larsson A.-K., Stroembeck B., Sundelin J.;
"Molecular cloning and functional expression of the gene encoding the
human proteinase-activated receptor 2.";
Eur. J. Biochem. 232:84-89(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=8615752; DOI=10.1042/bj3141009;
Boehm S.K., Kong W., Broemme D., Smeekens S.P., Anderson D.C.,
Connolly A.J., Kahn M.L., Nelken N.A., Coughlin S.R., Payan D.G.,
Bunnett N.W.;
"Molecular cloning, expression and potential functions of the human
proteinase-activated receptor-2.";
Biochem. J. 314:1009-1016(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH COPS5.
PubMed=16410250; DOI=10.1074/jbc.M510784200;
Luo W., Wang Y., Hanck T., Stricker R., Reiser G.;
"Jab1, a novel protease-activated receptor-2 (PAR-2)-interacting
protein, is involved in PAR-2-induced activation of activator protein-
1.";
J. Biol. Chem. 281:7927-7936(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-21; GLN-270 AND
ALA-291.
SeattleSNPs variation discovery resource;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-397.
PubMed=8784787;
Kahn M.L., Ishii K., Kuo W.L., Piper M., Connolly A.J., Shi Y.P.,
Wu R., Lin C.C., Coughlin S.R.;
"Conserved structure and adjacent location of the thrombin receptor
and protease-activated receptor 2 genes define a protease-activated
receptor gene cluster.";
Mol. Med. 2:349-357(1996).
[9]
ACTIVATION BY MAST CELL TRYPTASE.
PubMed=9020112; DOI=10.1074/jbc.272.7.4043;
Molino M., Barnathan E.S., Numerof R., Clark J., Dreyer M.,
Cumashi A., Hoxie J.A., Schechter N., Woolkalis M., Brass L.F.;
"Interactions of mast cell tryptase with thrombin receptors and PAR-
2.";
J. Biol. Chem. 272:4043-4049(1997).
[10]
FUNCTION IN EPITHELIAL BARRIER PROTECTION.
PubMed=10086357; DOI=10.1038/18223;
Cocks T.M., Fong B., Chow J.M., Anderson G.P., Frauman A.G.,
Goldie R.G., Henry P.J., Carr M.J., Hamilton J.R., Moffatt J.D.;
"A protective role for protease-activated receptors in the airways.";
Nature 398:156-160(1999).
[11]
TRANSACTIVATION BY F2R.
PubMed=10788464; DOI=10.1074/jbc.275.18.13502;
O'Brien P.J., Prevost N., Molino M., Hollinger M.K., Woolkalis M.J.,
Woulfe D.S., Brass L.F.;
"Thrombin responses in human endothelial cells. Contributions from
receptors other than PAR1 include the transactivation of PAR2 by
thrombin-cleaved PAR1.";
J. Biol. Chem. 275:13502-13509(2000).
[12]
FUNCTION, AND MUTAGENESIS OF SER-363 AND THR-366.
PubMed=10725339; DOI=10.1083/jcb.148.6.1267;
DeFea K.A., Zalevsky J., Thoma M.S., Dery O., Mullins R.D.,
Bunnett N.W.;
"beta-arrestin-dependent endocytosis of proteinase-activated receptor
2 is required for intracellular targeting of activated ERK1/2.";
J. Cell Biol. 148:1267-1281(2000).
[13]
ACTIVATION BY ST14.
PubMed=10831593; DOI=10.1074/jbc.M002941200;
Takeuchi T., Harris J.L., Huang W., Yan K.W., Coughlin S.R.,
Craik C.S.;
"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. 275:26333-26342(2000).
[14]
ACTIVATION BY COAGULATION FACTORS VII AND XA.
PubMed=10805786; DOI=10.1073/pnas.97.10.5255;
Camerer E., Huang W., Coughlin S.R.;
"Tissue factor- and factor X-dependent activation of protease-
activated receptor 2 by factor VIIa.";
Proc. Natl. Acad. Sci. U.S.A. 97:5255-5260(2000).
[15]
FUNCTION, AND ACTIVATION BY GINGIPAINS.
PubMed=11447194; DOI=10.1128/IAI.69.8.5121-5130.2001;
Lourbakos A., Potempa J., Travis J., D'Andrea M.R., Andrade-Gordon P.,
Santulli R., Mackie E.J., Pike R.N.;
"Arginine-specific protease from Porphyromonas gingivalis activates
protease-activated receptors on human oral epithelial cells and
induces interleukin-6 secretion.";
Infect. Immun. 69:5121-5130(2001).
[16]
FUNCTION IN JNK AND NF-KAPPA-B PATHWAYS.
PubMed=11413129; DOI=10.1074/jbc.M100377200;
Kanke T., Macfarlane S.R., Seatter M.J., Davenport E., Paul A.,
McKenzie R.C., Plevin R.;
"Proteinase-activated receptor-2-mediated activation of stress-
activated protein kinases and inhibitory kappa B kinases in NCTC 2544
keratinocytes.";
J. Biol. Chem. 276:31657-31666(2001).
[17]
FUNCTION, AND ACTIVATION BY DUST MITE ALLERGENS.
PubMed=11441110; DOI=10.4049/jimmunol.167.2.1014;
Sun G., Stacey M.A., Schmidt M., Mori L., Mattoli S.;
"Interaction of mite allergens Der p3 and Der p9 with protease-
activated receptor-2 expressed by lung epithelial cells.";
J. Immunol. 167:1014-1021(2001).
[18]
FUNCTION IN INFLAMMATORY RESPONSE.
PubMed=11714832; DOI=10.4049/jimmunol.167.11.6615;
Miike S., McWilliam A.S., Kita H.;
"Trypsin induces activation and inflammatory mediator release from
human eosinophils through protease-activated receptor-2.";
J. Immunol. 167:6615-6622(2001).
[19]
GLYCOSYLATION AT ASN-30 AND ASN-222, AND MUTAGENESIS OF ASN-30 AND
ASN-222.
PubMed=12171601; DOI=10.1042/BJ20020706;
Compton S.J., Sandhu S., Wijesuriya S.J., Hollenberg M.D.;
"Glycosylation of human proteinase-activated receptor-2 (hPAR2): role
in cell surface expression and signalling.";
Biochem. J. 368:495-505(2002).
[20]
POSSIBLE INVOLVEMENT IN ALLERGIC DERMATITIS.
PubMed=11859856; DOI=10.1254/jjp.88.77;
Kawagoe J., Takizawa T., Matsumoto J., Tamiya M., Meek S.E.,
Smith A.J., Hunter G.D., Plevin R., Saito N., Kanke T., Fujii M.,
Wada Y.;
"Effect of protease-activated receptor-2 deficiency on allergic
dermatitis in the mouse ear.";
Jpn. J. Pharmacol. 88:77-84(2002).
[21]
DEACTIVATION BY NEUTROPHIL ELASTASE AND CATHEPSIN G.
PubMed=12594060; DOI=10.1165/rcmb.4908;
Dulon S., Cande C., Bunnett N.W., Hollenberg M.D., Chignard M.,
Pidard D.;
"Proteinase-activated receptor-2 and human lung epithelial cells:
disarming by neutrophil serine proteinases.";
Am. J. Respir. Cell Mol. Biol. 28:339-346(2003).
[22]
POSSIBLE INVOLVEMENT IN SKIN DISEASES.
PubMed=14519665; DOI=10.1096/fj.02-1112com;
Seeliger S., Derian C.K., Vergnolle N., Bunnett N.W., Nawroth R.,
Schmelz M., Von Der Weid P.Y., Buddenkotte J., Sunderkotter C.,
Metze D., Andrade-Gordon P., Harms E., Vestweber D., Luger T.A.,
Steinhoff M.;
"Proinflammatory role of proteinase-activated receptor-2 in humans and
mice during cutaneous inflammation in vivo.";
FASEB J. 17:1871-1885(2003).
[23]
FUNCTION.
PubMed=12832443; DOI=10.1189/jlb.0702351;
Bolton S.J., McNulty C.A., Thomas R.J., Hewitt C.R., Wardlaw A.J.;
"Expression of and functional responses to protease-activated
receptors on human eosinophils.";
J. Leukoc. Biol. 74:60-68(2003).
[24]
MUTAGENESIS OF 355-ALA--SER-363.
PubMed=14607272; DOI=10.1016/S0898-6568(03)00095-0;
Seatter M.J., Drummond R., Kanke T., Macfarlane S.R., Hollenberg M.D.,
Plevin R.;
"The role of the C-terminal tail in protease-activated receptor-2-
mediated Ca2+ signalling, proline-rich tyrosine kinase-2 activation,
and mitogen-activated protein kinase activity.";
Cell. Signal. 16:21-29(2004).
[25]
FUNCTION.
PubMed=15155775; DOI=10.1189/jlb.0503221;
Shpacovitch V.M., Varga G., Strey A., Gunzer M., Mooren F.,
Buddenkotte J., Vergnolle N., Sommerhoff C.P., Grabbe S., Gerke V.,
Homey B., Hollenberg M., Luger T.A., Steinhoff M.;
"Agonists of proteinase-activated receptor-2 modulate human neutrophil
cytokine secretion, expression of cell adhesion molecules, and
migration within 3-D collagen lattices.";
J. Leukoc. Biol. 76:388-398(2004).
[26]
UBIQUITINATION BY CBL.
PubMed=15708858; DOI=10.1074/jbc.M500109200;
Jacob C., Cottrell G.S., Gehringer D., Schmidlin F., Grady E.F.,
Bunnett N.W.;
"c-Cbl mediates ubiquitination, degradation, and down-regulation of
human protease-activated receptor 2.";
J. Biol. Chem. 280:16076-16087(2005).
[27]
FUNCTION IN ENDOTHELIAL BARRIER PROTECTION.
PubMed=16359518; DOI=10.1111/j.1538-7836.2005.01610.x;
Feistritzer C., Lenta R., Riewald M.;
"Protease-activated receptors-1 and -2 can mediate endothelial barrier
protection: role in factor Xa signaling.";
J. Thromb. Haemost. 3:2798-2805(2005).
[28]
POSSIBLE INVOLVEMENT IN COLITIS.
PubMed=15919826; DOI=10.1073/pnas.0409535102;
Hansen K.K., Sherman P.M., Cellars L., Andrade-Gordon P., Pan Z.,
Baruch A., Wallace J.L., Hollenberg M.D., Vergnolle N.;
"A major role for proteolytic activity and proteinase-activated
receptor-2 in the pathogenesis of infectious colitis.";
Proc. Natl. Acad. Sci. U.S.A. 102:8363-8368(2005).
[29]
POSSIBLE INVOLVEMENT IN BRONCHIAL EOSINOPHILIC INFLAMMATION.
PubMed=15879675; DOI=10.1254/jphs.SCZ050138;
Takizawa T., Tamiya M., Hara T., Matsumoto J., Saito N., Kanke T.,
Kawagoe J., Hattori Y.;
"Abrogation of bronchial eosinophilic inflammation and attenuated
eotaxin content in protease-activated receptor 2-deficient mice.";
J. Pharmacol. Sci. 98:99-102(2005).
[30]
FUNCTION IN EPITHELIAL BARRIER DISRUPTION.
PubMed=16714334; DOI=10.1152/ajplung.00046.2006;
Winter M.C., Shasby S.S., Ries D.R., Shasby D.M.;
"PAR2 activation interrupts E-cadherin adhesion and compromises the
airway epithelial barrier: protective effect of beta-agonists.";
Am. J. Physiol. 291:L628-L635(2006).
[31]
FUNCTION, AND ACTIVATION BY PRTN3.
PubMed=16478888; DOI=10.1182/blood-2005-05-1875;
Csernok E., Ai M., Gross W.L., Wicklein D., Petersen A., Lindner B.,
Lamprecht P., Holle J.U., Hellmich B.;
"Wegener autoantigen induces maturation of dendritic cells and
licenses them for Th1 priming via the protease-activated receptor-2
pathway.";
Blood 107:4440-4448(2006).
[32]
POSSIBLE INVOLVEMENT IN ENCEPHALOMYELITIS AND MULTIPLE SCLEROSIS.
PubMed=16476770; DOI=10.1084/jem.20052148;
Noorbakhsh F., Tsutsui S., Vergnolle N., Boven L.A., Shariat N.,
Vodjgani M., Warren K.G., Andrade-Gordon P., Hollenberg M.D.,
Power C.;
"Proteinase-activated receptor 2 modulates neuroinflammation in
experimental autoimmune encephalomyelitis and multiple sclerosis.";
J. Exp. Med. 203:425-435(2006).
[33]
FUNCTION IN ACTIN FILAMENT SEVERING.
PubMed=17500066; DOI=10.1074/jbc.M701391200;
Zoudilova M., Kumar P., Ge L., Wang P., Bokoch G.M., DeFea K.A.;
"Beta-arrestin-dependent regulation of the cofilin pathway downstream
of protease-activated receptor-2.";
J. Biol. Chem. 282:20634-20646(2007).
[34]
INTERACTION WITH TMED2.
PubMed=17693410; DOI=10.1074/jbc.M703205200;
Luo W., Wang Y., Reiser G.;
"p24A, a type I transmembrane protein, controls ARF1-dependent
resensitization of protease-activated receptor-2 by influence on
receptor trafficking.";
J. Biol. Chem. 282:30246-30255(2007).
[35]
FUNCTION, AND ACTIVATION BY MOLD ALLERGENS.
PubMed=17404307; DOI=10.4049/jimmunol.178.8.5237;
Chiu L.L., Perng D.W., Yu C.H., Su S.N., Chow L.P.;
"Mold allergen, pen C 13, induces IL-8 expression in human airway
epithelial cells by activating protease-activated receptor 1 and 2.";
J. Immunol. 178:5237-5244(2007).
[36]
FUNCTION, AND ACTIVATION BY BACTERIAL CHITINASE.
PubMed=18474671; DOI=10.1165/rcmb.2007-0410OC;
Hong J.H., Hong J.Y., Park B., Lee S.I., Seo J.T., Kim K.E.,
Sohn M.H., Shin D.M.;
"Chitinase activates protease-activated receptor-2 in human airway
epithelial cells.";
Am. J. Respir. Cell Mol. Biol. 39:530-535(2008).
[37]
FUNCTION.
PubMed=18424071; DOI=10.1016/j.cellsig.2008.02.015;
Goon Goh F., Sloss C.M., Cunningham M.R., Nilsson M., Cadalbert L.,
Plevin R.;
"G-protein-dependent and -independent pathways regulate proteinase-
activated receptor-2 mediated p65 NFkappaB serine 536 phosphorylation
in human keratinocytes.";
Cell. Signal. 20:1267-1274(2008).
[38]
FUNCTION, AND INTERACTION WITH TLR4.
PubMed=18622013; DOI=10.1074/jbc.M804800200;
Rallabhandi P., Nhu Q.M., Toshchakov V.Y., Piao W., Medvedev A.E.,
Hollenberg M.D., Fasano A., Vogel S.N.;
"Analysis of proteinase-activated receptor 2 and TLR4 signal
transduction: a novel paradigm for receptor cooperativity.";
J. Biol. Chem. 283:24314-24325(2008).
[39]
FUNCTION IN ANTIVIRAL RESPONSE.
PubMed=18453611; DOI=10.4049/jimmunol.180.10.6903;
Feld M., Shpacovitch V.M., Ehrhardt C., Kerkhoff C., Hollenberg M.D.,
Vergnolle N., Ludwig S., Steinhoff M.;
"Agonists of proteinase-activated receptor-2 enhance IFN-gamma-
inducible effects on human monocytes: role in influenza A infection.";
J. Immunol. 180:6903-6910(2008).
[40]
DEUBIQUITINATION.
PubMed=19684015; DOI=10.1074/jbc.M109.025692;
Hasdemir B., Murphy J.E., Cottrell G.S., Bunnett N.W.;
"Endosomal deubiquitinating enzymes control ubiquitination and down-
regulation of protease-activated receptor 2.";
J. Biol. Chem. 284:28453-28466(2009).
[41]
PHOSPHORYLATION.
PubMed=19815543; DOI=10.1074/jbc.M109.048942;
Ricks T.K., Trejo J.;
"Phosphorylation of protease-activated receptor-2 differentially
regulates desensitization and internalization.";
J. Biol. Chem. 284:34444-34457(2009).
[42]
FUNCTION IN ANTIVIRAL RESPONSE.
PubMed=19494303; DOI=10.4049/jimmunol.0803743;
Khoufache K., LeBouder F., Morello E., Laurent F., Riffault S.,
Andrade-Gordon P., Boullier S., Rousset P., Vergnolle N., Riteau B.;
"Protective role for protease-activated receptor-2 against influenza
virus pathogenesis via an IFN-gamma-dependent pathway.";
J. Immunol. 182:7795-7802(2009).
[43]
FUNCTION, AND ACTIVATION BY TRYPSIN AND FUNGAL ASPARTATE PROTEASE.
PubMed=19864598; DOI=10.4049/jimmunol.0901220;
Matsuwaki Y., Wada K., White T.A., Benson L.M., Charlesworth M.C.,
Checkel J.L., Inoue Y., Hotta K., Ponikau J.U., Lawrence C.B.,
Kita H.;
"Recognition of fungal protease activities induces cellular activation
and eosinophil-derived neurotoxin release in human eosinophils.";
J. Immunol. 183:6708-6716(2009).
[44]
POSSIBLE INVOLVEMENT IN ARTHRITIS.
PubMed=20584806; DOI=10.1136/ard.2010.130336;
Ferrell W.R., Kelso E.B., Lockhart J.C., Plevin R., McInnes I.B.;
"Protease-activated receptor 2: a novel pathogenic pathway in a murine
model of osteoarthritis.";
Ann. Rheum. Dis. 69:2051-2054(2010).
[45]
FUNCTION IN JNK PATHWAY.
PubMed=19781631; DOI=10.1016/j.cellsig.2009.09.028;
McIntosh K., Cunningham M.R., Cadalbert L., Lockhart J., Boyd G.,
Ferrell W.R., Plevin R.;
"Proteinase-activated receptor-2 mediated inhibition of TNFalpha-
stimulated JNK activation - a novel paradigm for G(q/11) linked
GPCRs.";
Cell. Signal. 22:265-273(2010).
[46]
FUNCTION IN ENDOTHELIAL BARRIER PROTECTION.
PubMed=20826780; DOI=10.1074/jbc.M110.163642;
Bae J.S., Yang L., Rezaie A.R.;
"Factor X/Xa elicits protective signaling responses in endothelial
cells directly via PAR-2 and indirectly via endothelial protein C
receptor-dependent recruitment of PAR-1.";
J. Biol. Chem. 285:34803-34812(2010).
[47]
POSSIBLE INVOLVEMENT IN PERIODONTITIS.
PubMed=20530726; DOI=10.1177/0022034510373765;
Holzhausen M., Cortelli J.R., da Silva V.A., Franco G.C.,
Cortelli S.C., Vergnolle N.;
"Protease-activated receptor-2 (PAR(2)) in human periodontitis.";
J. Dent. Res. 89:948-953(2010).
[48]
FUNCTION.
PubMed=19865078; DOI=10.1038/mi.2009.120;
Nhu Q.M., Shirey K., Teijaro J.R., Farber D.L., Netzel-Arnett S.,
Antalis T.M., Fasano A., Vogel S.N.;
"Novel signaling interactions between proteinase-activated receptor 2
and Toll-like receptors in vitro and in vivo.";
Mucosal Immunol. 3:29-39(2010).
[49]
FUNCTION IN ANTIMICROBIAL RESPONSE.
PubMed=21501162; DOI=10.1111/j.1365-2567.2011.03443.x;
Shpacovitch V.M., Feld M., Holzinger D., Kido M., Hollenberg M.D.,
Levi-Schaffer F., Vergnolle N., Ludwig S., Roth J., Luger T.,
Steinhoff M.;
"Role of proteinase-activated receptor-2 in anti-bacterial and
immunomodulatory effects of interferon-gamma on human neutrophils and
monocytes.";
Immunology 133:329-339(2011).
[50]
PALMITOYLATION AT CYS-361.
PubMed=21627585; DOI=10.1042/BJ20101958;
Botham A., Guo X., Xiao Y.P., Morice A.H., Compton S.J.,
Sadofsky L.R.;
"Palmitoylation of human proteinase-activated receptor-2
differentially regulates receptor triggered ERK1/2 activation, calcium
signalling, and endocytosis.";
Biochem. J. 438:359-367(2011).
-!- FUNCTION: Receptor for trypsin and trypsin-like enzymes coupled to
G proteins. Its function is mediated through the activation of
several signaling pathways including phospholipase C (PLC),
intracellular calcium, mitogen-activated protein kinase (MAPK), I-
kappaB kinase/NF-kappaB and Rho. Can also be transactivated by
cleaved F2R/PAR1. Involved in modulation of inflammatory responses
and regulation of innate and adaptive immunity, and acts as a
sensor for proteolytic enzymes generated during infection.
Generally is promoting inflammation. Can signal synergistically
with TLR4 and probably TLR2 in inflammatory responses and
modulates TLR3 signaling. Has a protective role in establishing
the endothelial barrier; the activity involves coagulation factor
X. Proposed to have a bronchoprotective role in airway epithelium,
but also shown to compromise the airway epithelial barrier by
interrupting E-cadherin adhesion. Involved in the regulation of
vascular tone; activation results in hypotension presumably
mediated by vasodilation. Associates with a subset of G proteins
alpha subunits such as G alpha-q, G alpha-11, G alpha-14, G alpha-
12 and G alpha-13, but probably not with G(o) alpha, G(i) subunit
alpha-1 and G(i) subunit alpha-2. However, according to
PubMed:21627585 can signal through G(i) subunit alpha. Believed to
be a class B receptor which internalizes as a complex with
arrestin and traffic with it to endosomal vesicles, presumably as
desensitized receptor, for extended periods of time. Mediates
inhibition of TNF-alpha stimulated JNK phosphorylation via
coupling to G alpha-q/11; the function involves dissociation of
RIPK1 and TRADD from TNFR1. Mediates phosphorylation of nuclear
factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves
IKBKB and is predominantly independent of G proteins. Involved in
cellular migration. Involved in cytoskeletal rearrangement and
chemotaxis through beta-arrestin-promoted scaffolds; the function
is independent of G alpha-q/11 and involves promotion of cofilin
dephosphoryltaion and actin filament severing. Induces
redistribution of COPS5 from the plasma membrane to the cytosol
and activation of the JNK cascade is mediated by COPS5. Involved
in the recruitment of leukocytes to the sites of inflammation and
is the major PAR receptor capable of modulating eosinophil
function such as proinflammatory cytokine secretion, superoxide
production and degranulation. During inflammation promotes
dendritic cell maturation, trafficking to the lymph nodes and
subsequent T-cell activation. Involved in antimicrobial response
of innate immnune cells; activation enhances phagocytosis of Gram-
positive and killing of Gram-negative bacteria. Acts
synergistically with interferon-gamma in enhancing antiviral
responses. Implicated in a number of acute and chronic
inflammatory diseases such as of the joints, lungs, brain,
gastrointestinal tract, periodontium, skin, and vascular systems,
and in autoimmune disorders. {ECO:0000269|PubMed:10086357,
ECO:0000269|PubMed:10725339, ECO:0000269|PubMed:11413129,
ECO:0000269|PubMed:11441110, ECO:0000269|PubMed:11447194,
ECO:0000269|PubMed:11714832, ECO:0000269|PubMed:12832443,
ECO:0000269|PubMed:15155775, ECO:0000269|PubMed:16359518,
ECO:0000269|PubMed:16410250, ECO:0000269|PubMed:16478888,
ECO:0000269|PubMed:16714334, ECO:0000269|PubMed:17404307,
ECO:0000269|PubMed:17500066, ECO:0000269|PubMed:18424071,
ECO:0000269|PubMed:18453611, ECO:0000269|PubMed:18474671,
ECO:0000269|PubMed:18622013, ECO:0000269|PubMed:19494303,
ECO:0000269|PubMed:19781631, ECO:0000269|PubMed:19864598,
ECO:0000269|PubMed:19865078, ECO:0000269|PubMed:20826780,
ECO:0000269|PubMed:21501162}.
-!- SUBUNIT: Interacts with TLR4, COPS5 and TMED2. Interacts with
GNAQ, GNA11, GNA12, GNA13 and GNA14 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P22681:CBL; NbExp=3; IntAct=EBI-4303189, EBI-518228;
Q92905:COPS5; NbExp=8; IntAct=EBI-4303189, EBI-594661;
Q14868:EPR-1; NbExp=4; IntAct=EBI-4303189, EBI-4309771;
Q15363:TMED2; NbExp=6; IntAct=EBI-4303189, EBI-998485;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Widely expressed in tissues with especially
high levels in pancreas, liver, kidney, small intestine, and
colon. Moderate expression is detected in many organs, but none in
brain or skeletal muscle.
-!- PTM: A proteolytic cleavage generates a new N-terminus that
functions as a tethered ligand. Activating serine proteases
include trypsin, mast cell tryptase, coagulation factors VII and
Xa, myeloblastin/PRTN3 and membrane-type serine protease 1/ST14.
Proposed subsequent cleaveage by serine proteases is leading to
receptor deactivation and include neutrophil elastase and
cathepsin G. At least in part, implicated proteases are also shown
to activate the receptor; the glycosylation status of the receptor
is thought to contribute to the difference. In addition to
conventional trypsin-like proteases is proposed to be activated by
other proteases and glycosidases derived from bacteria, fungi and
insects: serine protease allergens such as dust mite Der p3 and
Der p9 and mold Pen c13, Porphyromonas gingivalis arginine-
specific (trypsin-like) cysteine proteinases called gingipains,
Streptomyces griseus exogenous chitinase, and an Alternaria
alternata aspartate protease. Cleavage by the Alternaria alternata
aspartate protease generates non-conventional processed forms.
{ECO:0000269|PubMed:12171601}.
-!- PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:12171601}.
-!- PTM: Multiple phosphorylated on serine and threonine residues in
the cytoplasmic region upon receptor activation; required for
receptor desensitization and recruitment of beta-arrestin.
{ECO:0000269|PubMed:19815543}.
-!- PTM: Monoubiquitinated by CBL at the plasma membrane and in early
endosomes; not required for receptor endocytosis but for
translocation to late endosomes or lysosomes. Deubiquitination
involves STAMBP and USP8; required for lysosomal trafficking and
receptor degradation.
-!- MISCELLANEOUS: Synthetic PAR agonist peptides (APs) that mimic the
first six amino acids of the newly formed N-terminus activate the
native, uncleaved receptor nonenzymatically by binding directly to
the corresponding second extracellular loop to mediate signaling.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Protease-activated receptor
entry;
URL="https://en.wikipedia.org/wiki/Protease-activated_receptor";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f2rl1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z49993; CAA90290.1; -; Genomic_DNA.
EMBL; Z49994; CAA90290.1; JOINED; Genomic_DNA.
EMBL; U34038; AAB47871.1; -; mRNA.
EMBL; AY336105; AAP97012.1; -; mRNA.
EMBL; AF400075; AAK77914.1; -; Genomic_DNA.
EMBL; BT009856; AAP88858.1; -; mRNA.
EMBL; CH471084; EAW95782.1; -; Genomic_DNA.
EMBL; BC012453; AAH12453.1; -; mRNA.
EMBL; BC018130; AAH18130.1; -; mRNA.
EMBL; U36753; AAA90957.1; -; Genomic_DNA.
CCDS; CCDS4033.1; -.
PIR; S66518; S66518.
RefSeq; NP_005233.3; NM_005242.5.
UniGene; Hs.744181; -.
PDB; 5NDD; X-ray; 2.80 A; A=59-269, A=276-377.
PDB; 5NDZ; X-ray; 3.60 A; A=59-269, A=276-377.
PDB; 5NJ6; X-ray; 4.00 A; A=55-269, A=276-377.
PDBsum; 5NDD; -.
PDBsum; 5NDZ; -.
PDBsum; 5NJ6; -.
ProteinModelPortal; P55085; -.
SMR; P55085; -.
BioGrid; 108449; 14.
DIP; DIP-42044N; -.
IntAct; P55085; 6.
MINT; MINT-1326650; -.
STRING; 9606.ENSP00000296677; -.
BindingDB; P55085; -.
ChEMBL; CHEMBL5963; -.
GuidetoPHARMACOLOGY; 348; -.
TCDB; 9.A.14.13.12; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P55085; -.
PhosphoSitePlus; P55085; -.
SwissPalm; P55085; -.
BioMuta; F2RL1; -.
DMDM; 1709580; -.
MaxQB; P55085; -.
PaxDb; P55085; -.
PeptideAtlas; P55085; -.
PRIDE; P55085; -.
DNASU; 2150; -.
Ensembl; ENST00000296677; ENSP00000296677; ENSG00000164251.
GeneID; 2150; -.
KEGG; hsa:2150; -.
UCSC; uc003keo.4; human.
CTD; 2150; -.
DisGeNET; 2150; -.
EuPathDB; HostDB:ENSG00000164251.4; -.
GeneCards; F2RL1; -.
HGNC; HGNC:3538; F2RL1.
HPA; CAB012989; -.
HPA; HPA014091; -.
MalaCards; F2RL1; -.
MIM; 600933; gene.
neXtProt; NX_P55085; -.
PharmGKB; PA27947; -.
eggNOG; ENOG410IGEM; Eukaryota.
eggNOG; ENOG4111CWR; LUCA.
HOGENOM; HOG000116291; -.
HOVERGEN; HBG105658; -.
InParanoid; P55085; -.
KO; K04234; -.
OrthoDB; EOG091G0C2F; -.
PhylomeDB; P55085; -.
TreeFam; TF330775; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-416476; G alpha (q) signalling events.
SIGNOR; P55085; -.
GeneWiki; Protease_activated_receptor_2; -.
GenomeRNAi; 2150; -.
PMAP-CutDB; P55085; -.
PRO; PR:P55085; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164251; -.
CleanEx; HS_F2RL1; -.
ExpressionAtlas; P55085; baseline and differential.
Genevisible; P55085; HS.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031143; C:pseudopodium; ISS:UniProtKB.
GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
GO; GO:0031681; F:G-protein beta-subunit binding; ISS:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; IMP:UniProtKB.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0015057; F:thrombin-activated receptor activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; IEA:InterPro.
GO; GO:0035926; P:chemokine (C-C motif) ligand 2 secretion; IDA:UniProtKB.
GO; GO:0090195; P:chemokine secretion; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0061028; P:establishment of endothelial barrier; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0072643; P:interferon-gamma secretion; ISS:UniProtKB.
GO; GO:0050702; P:interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0072608; P:interleukin-10 secretion; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; IDA:UniProtKB.
GO; GO:0070661; P:leukocyte proliferation; ISS:UniProtKB.
GO; GO:0097029; P:mature conventional dendritic cell differentiation; IDA:UniProtKB.
GO; GO:0090198; P:negative regulation of chemokine secretion; IDA:UniProtKB.
GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; IMP:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB.
GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:UniProtKB.
GO; GO:0097755; P:positive regulation of blood vessel diameter; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; IBA:GO_Central.
GO; GO:0043311; P:positive regulation of eosinophil degranulation; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0003104; P:positive regulation of glomerular filtration; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IDA:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IDA:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IDA:BHF-UCL.
GO; GO:0070963; P:positive regulation of neutrophil mediated killing of gram-negative bacterium; IDA:UniProtKB.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISS:UniProtKB.
GO; GO:1900135; P:positive regulation of renin secretion into blood stream; ISS:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:UniProtKB.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:UniProtKB.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IMP:UniProtKB.
GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; IMP:UniProtKB.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0030193; P:regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0002286; P:T cell activation involved in immune response; ISS:UniProtKB.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR002281; Pro_rcpt_2.
InterPro; IPR003912; Protea_act_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01428; PROTEASEAR.
PRINTS; PR01152; PROTEASEAR2.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Signal; Transducer; Transmembrane; Transmembrane helix;
Ubl conjugation.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 36 Removed for receptor activation.
/FTId=PRO_0000012750.
CHAIN 37 397 Proteinase-activated receptor 2.
/FTId=PRO_0000412954.
CHAIN 38 397 Proteinase-activated receptor 2,
alternate cleaved 1.
/FTId=PRO_0000412956.
CHAIN 39 397 Proteinase-activated receptor 2,
alternate cleaved 2.
/FTId=PRO_0000012751.
TOPO_DOM 37 75 Extracellular. {ECO:0000255}.
TRANSMEM 76 101 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 102 110 Cytoplasmic. {ECO:0000255}.
TRANSMEM 111 130 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 131 149 Extracellular. {ECO:0000255}.
TRANSMEM 150 171 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 172 190 Cytoplasmic. {ECO:0000255}.
TRANSMEM 191 211 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 212 241 Extracellular. {ECO:0000255}.
TRANSMEM 242 260 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 261 285 Cytoplasmic. {ECO:0000255}.
TRANSMEM 286 308 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 309 323 Extracellular. {ECO:0000255}.
TRANSMEM 324 347 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 348 397 Cytoplasmic. {ECO:0000255}.
COMPBIAS 383 390 Poly-Ser.
SITE 36 37 Cleavage; by trypsin.
LIPID 361 361 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21627585}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12171601}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12171601}.
DISULFID 148 226 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 21 21 S -> F (in dbSNP:rs2243072).
{ECO:0000269|Ref.4}.
/FTId=VAR_012846.
VARIANT 30 30 N -> S (in dbSNP:rs616235).
/FTId=VAR_049435.
VARIANT 270 270 R -> Q (in dbSNP:rs2243062).
{ECO:0000269|Ref.4}.
/FTId=VAR_012847.
VARIANT 291 291 T -> A (in dbSNP:rs2243083).
{ECO:0000269|Ref.4}.
/FTId=VAR_012848.
MUTAGEN 30 30 N->A: Decreases cell surface expression;
when associate with A-222.
{ECO:0000269|PubMed:12171601}.
MUTAGEN 30 30 N->A: Increase of sensitivity towards
tryptase. {ECO:0000269|PubMed:12171601}.
MUTAGEN 222 222 N->A: Decreases cell surface expression;
when associate with A-30.
{ECO:0000269|PubMed:12171601}.
MUTAGEN 222 222 N->A: Loss of sensitivity towards all
tested proteases.
{ECO:0000269|PubMed:12171601}.
MUTAGEN 355 363 Missing: Abolishes signaling through
accumulation of intracellular calcium and
phosphoinositide; no effect in signaling
through MAPK.
{ECO:0000269|PubMed:14607272}.
MUTAGEN 361 361 C->A: Loss of palmitoylation; increases
surface expression and internalization
following trypsin activation, decreases
sensitivity and intracellular calcium
signaling, increases ERK activation
through G(i) subunit alpha.
MUTAGEN 363 363 S->A: Reduces receptor desensitization
and internalization, activates ERK1/2;
when associated with A-366.
{ECO:0000269|PubMed:10725339}.
MUTAGEN 366 366 T->A: Reduces receptor desensitization
and internalization, activates ERK1/2;
when associated with A-363.
{ECO:0000269|PubMed:10725339}.
CONFLICT 138 138 G -> A (in Ref. 2; AAB47871).
{ECO:0000305}.
CONFLICT 291 291 T -> S (in Ref. 7; AAH18130).
{ECO:0000305}.
HELIX 63 68 {ECO:0000244|PDB:5NDD}.
HELIX 72 75 {ECO:0000244|PDB:5NDD}.
HELIX 77 102 {ECO:0000244|PDB:5NDD}.
HELIX 109 125 {ECO:0000244|PDB:5NDD}.
HELIX 128 136 {ECO:0000244|PDB:5NDD}.
HELIX 145 178 {ECO:0000244|PDB:5NDD}.
HELIX 186 205 {ECO:0000244|PDB:5NDD}.
HELIX 207 210 {ECO:0000244|PDB:5NDD}.
STRAND 215 218 {ECO:0000244|PDB:5NDD}.
TURN 219 222 {ECO:0000244|PDB:5NDD}.
STRAND 223 229 {ECO:0000244|PDB:5NDD}.
HELIX 233 235 {ECO:0000244|PDB:5NDD}.
HELIX 236 249 {ECO:0000244|PDB:5NDD}.
HELIX 252 269 {ECO:0000244|PDB:5NDD}.
HELIX 279 298 {ECO:0000244|PDB:5NDD}.
HELIX 301 316 {ECO:0000244|PDB:5NDD}.
HELIX 323 332 {ECO:0000244|PDB:5NDD}.
HELIX 333 335 {ECO:0000244|PDB:5NDD}.
HELIX 336 347 {ECO:0000244|PDB:5NDD}.
HELIX 349 358 {ECO:0000244|PDB:5NDD}.
SEQUENCE 397 AA; 44126 MW; F1A4E1D5AB9B362B CRC64;
MRSPSAAWLL GAAILLAASL SCSGTIQGTN RSSKGRSLIG KVDGTSHVTG KGVTVETVFS
VDEFSASVLT GKLTTVFLPI VYTIVFVVGL PSNGMALWVF LFRTKKKHPA VIYMANLALA
DLLSVIWFPL KIAYHIHGNN WIYGEALCNV LIGFFYGNMY CSILFMTCLS VQRYWVIVNP
MGHSRKKANI AIGISLAIWL LILLVTIPLY VVKQTIFIPA LNITTCHDVL PEQLLVGDMF
NYFLSLAIGV FLFPAFLTAS AYVLMIRMLR SSAMDENSEK KRKRAIKLIV TVLAMYLICF
TPSNLLLVVH YFLIKSQGQS HVYALYIVAL CLSTLNSCID PFVYYFVSHD FRDHAKNALL
CRSVRTVKQM QVSLTSKKHS RKSSSYSSSS TTVKTSY


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