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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.
12-SEP-2018, entry version 175.
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], AND TISSUE SPECIFICITY.
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], AND TISSUE SPECIFICITY.
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).
[51]
FUNCTION, TISSUE SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
PubMed=23202369; DOI=10.1161/ATVBAHA.112.300474;
Kuckleburg C.J., Newman P.J.;
"Neutrophil proteinase 3 acts on protease-activated receptor-2 to
enhance vascular endothelial cell barrier function.";
Arterioscler. Thromb. Vasc. Biol. 33:275-284(2013).
[52]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 59-269 AND 276-377,
FUNCTION, DISULFIDE BOND, TOPOLOGY, AND MUTAGENESIS OF HIS-135;
PHE-154; GLY-157; TYR-210; ASN-222; HIS-227; ASP-228 AND ILE-327.
PubMed=28445455; DOI=10.1038/nature22309;
Cheng R.K.Y., Fiez-Vandal C., Schlenker O., Edman K., Aggeler B.,
Brown D.G., Brown G.A., Cooke R.M., Dumelin C.E., Dore A.S.,
Geschwindner S., Grebner C., Hermansson N.O., Jazayeri A.,
Johansson P., Leong L., Prihandoko R., Rappas M., Soutter H.,
Snijder A., Sundstrom L., Tehan B., Thornton P., Troast D., Wiggin G.,
Zhukov A., Marshall F.H., Dekker N.;
"Structural insight into allosteric modulation of protease-activated
receptor 2.";
Nature 545:112-115(2017).
-!- FUNCTION: Receptor for trypsin and trypsin-like enzymes coupled to
G proteins (PubMed:28445455). 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 (PubMed:28445455). 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. Regulates endothelial cell barrier integrity
during neutrophil extravasation, probably following proteolytic
cleavage by PRTN3 (PubMed:23202369). Proposed to have a
bronchoprotective role in airway epithelium, but also shown to
compromise the airway epithelial barrier by interrupting E-
cadherin adhesion (PubMed:10086357). 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 GNAQ, GNA11, GNA14, GNA12 and GNA13, 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 GNAQ and GNA11; 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
GNAQ and GNA11 and involves promotion of cofilin dephosphorylation
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,
ECO:0000269|PubMed:23202369, ECO:0000269|PubMed:28445455}.
-!- SUBUNIT: Interacts with TLR4, COPS5 and TMED2. Interacts with
GNAQ, GNA11, GNA12, GNA13 and GNA14 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P29066:Arrb1 (xeno); NbExp=6; IntAct=EBI-4303189, EBI-4303019;
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;
P13726:F3; NbExp=2; IntAct=EBI-4303189, EBI-1040727;
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
(PubMed:7556175, PubMed:8615752). Moderate expression is detected
in many organs, but none in brain or skeletal muscle
(PubMed:7556175, PubMed:8615752). Expressed in endothelial cells
(PubMed:23202369). {ECO:0000269|PubMed:23202369,
ECO:0000269|PubMed:7556175, ECO:0000269|PubMed:8615752}.
-!- PTM: A proteolytic cleavage generates a new N-terminus that
functions as a tethered ligand (PubMed:10831593, PubMed:19864598,
PubMed:9020112, PubMed:10805786, PubMed:16478888). Activating
serine proteases include trypsin, mast cell tryptase, coagulation
factors VII and Xa, myeloblastin/PRTN3 and membrane-type serine
protease 1/ST14 (PubMed:10831593, PubMed:19864598, PubMed:9020112,
PubMed:10805786, PubMed:16478888, PubMed:23202369). Subsequent
cleavage by serine proteases, including neutrophil elastase and
cathepsin G, leads to receptor deactivation (PubMed:12594060). 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 (PubMed:12171601). In addition to
conventional trypsin-like proteases activated by other proteases
and glycosidases derived from bacteria, fungi and insects
(PubMed:11447194, PubMed:11441110, PubMed:17404307,
PubMed:18474671, PubMed:19864598). Activated by serine protease
allergens such as dust mite Der p3 and Der p9 and mold Pen c13
(PubMed:11441110, PubMed:17404307). Activated by P.gingivalis
arginine-specific (trypsin-like) cysteine proteinases called
gingipains (PubMed:11447194). Activated by S.griseus exogenous
chitinase (PubMed:18474671). Activated by A.alternata aspartate
protease; the cleavage generates non-conventional processed forms
(PubMed:19864598). {ECO:0000269|PubMed:10805786,
ECO:0000269|PubMed:10831593, ECO:0000269|PubMed:11441110,
ECO:0000269|PubMed:11447194, ECO:0000269|PubMed:12171601,
ECO:0000269|PubMed:12594060, ECO:0000269|PubMed:16478888,
ECO:0000269|PubMed:17404307, ECO:0000269|PubMed:18474671,
ECO:0000269|PubMed:19864598, ECO:0000269|PubMed:23202369,
ECO:0000269|PubMed:9020112}.
-!- 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 https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) 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; 9.
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; -.
ProteomicsDB; 56787; -.
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; -.
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; Expressed in 173 organ(s), highest expression level in colonic mucosa.
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:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
GO; GO:0015057; F:thrombin-activated receptor activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; IEA:InterPro.
GO; GO:0045217; P:cell-cell junction maintenance; IMP:UniProtKB.
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; IMP:UniProtKB.
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:0043547; P:positive regulation of GTPase activity; IMP: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 by RNA polymerase II; 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 71 Extracellular.
{ECO:0000269|PubMed:28445455}.
TRANSMEM 72 101 Helical; Name=1.
{ECO:0000269|PubMed:28445455}.
TOPO_DOM 102 108 Cytoplasmic.
{ECO:0000269|PubMed:28445455}.
TRANSMEM 109 137 Helical; Name=2.
{ECO:0000269|PubMed:28445455}.
TOPO_DOM 138 149 Extracellular.
{ECO:0000269|PubMed:28445455}.
TRANSMEM 150 177 Helical; Name=3.
{ECO:0000269|PubMed:28445455}.
TOPO_DOM 178 183 Cytoplasmic.
{ECO:0000269|PubMed:28445455}.
TRANSMEM 184 211 Helical; Name=4.
{ECO:0000269|PubMed:28445455}.
TOPO_DOM 212 235 Extracellular.
{ECO:0000269|PubMed:28445455}.
TRANSMEM 236 269 Helical; Name=5.
{ECO:0000269|PubMed:28445455}.
TOPO_DOM 270 277 Cytoplasmic.
{ECO:0000269|PubMed:28445455}.
TRANSMEM 278 317 Helical; Name=6.
{ECO:0000269|PubMed:28445455}.
TOPO_DOM 318 323 Extracellular.
{ECO:0000269|PubMed:28445455}.
TRANSMEM 324 347 Helical; Name=7.
{ECO:0000269|PubMed:28445455}.
TOPO_DOM 348 397 Cytoplasmic.
{ECO:0000269|PubMed:28445455}.
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:0000244|PDB:5NDD,
ECO:0000244|PDB:5NDZ,
ECO:0000244|PDB:5NJ6,
ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:28445455}.
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 135 135 H->Y: Slight reduction in ligand-mediated
receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 154 154 F->A: Severe reduction in ligand-mediated
receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 157 157 G->C,M: Severe reduction in ligand-
mediated receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 210 210 Y->L: No defect in ligand-mediated
receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 222 222 N->A: Decreases cell surface expression;
when associated with A-30. Loss of
sensitivity towards all tested proteases.
{ECO:0000269|PubMed:12171601}.
MUTAGEN 222 222 N->Q: No defect in ligand-mediated
receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 227 227 H->A: No defect in ligand-mediated
receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 227 227 H->Q: Slight reduction in ligand-mediated
receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 228 228 D->A,N: Severe reduction in ligand-
mediated receptor activation.
{ECO:0000269|PubMed:28445455}.
MUTAGEN 327 327 I->L: Slight reduction in ligand-mediated
receptor activation.
{ECO:0000269|PubMed:28445455}.
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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EIAAB29889 Coagulation factor II receptor-like 3,F2rl3,Mouse,Mus musculus,Par4,PAR-4,Proteinase-activated receptor 4,Thrombin receptor-like 3
EIAAB29885 Bos taurus,Bovine,Coagulation factor II receptor-like 2,F2RL2,PAR3,PAR-3,Proteinase-activated receptor 3,Thrombin receptor-like 2
18-461-10291 Proteinase-activated receptor 3 - PAR-3; Thrombin receptor-like 2; Coagulation factor II receptor-like 2 Polyclonal 0.05 ml
18-461-10170 Proteinase-activated receptor 1 - PAR-1; Thrombin receptor; Coagulation factor II receptor Polyclonal 0.05 ml
18-461-10137 Proteinase-activated receptor 4 - PAR-4; Thrombin receptor-like 3; Coagulation factor II receptor-like 3 Polyclonal 0.05 ml
18-461-10355 Proteinase-activated receptor 4 - PAR-4; Thrombin receptor-like 3; Coagulation factor II receptor-like 3 Polyclonal 0.05 ml
18-461-10356 Proteinase-activated receptor 4 - PAR-4; Thrombin receptor-like 3; Coagulation factor II receptor-like 3 Polyclonal 0.05 ml
18-461-10138 Proteinase-activated receptor 4 - PAR-4; Thrombin receptor-like 3; Coagulation factor II receptor-like 3 Polyclonal 0.05 ml
EIAAB29888 Coagulation factor II receptor-like 3,F2RL3,Homo sapiens,Human,PAR4,PAR-4,Proteinase-activated receptor 4,Thrombin receptor-like 3
EIAAB29884 Coagulation factor II receptor-like 2,F2RL2,Homo sapiens,Human,PAR3,PAR-3,Proteinase-activated receptor 3,Thrombin receptor-like 2
U0826h CLIA CF2R,Coagulation factor II receptor,F2R,Homo sapiens,Human,PAR1,PAR-1,Proteinase-activated receptor 1,Thrombin receptor,TR 96T
E0826h ELISA CF2R,Coagulation factor II receptor,F2R,Homo sapiens,Human,PAR1,PAR-1,Proteinase-activated receptor 1,Thrombin receptor,TR 96T
E0826h ELISA kit CF2R,Coagulation factor II receptor,F2R,Homo sapiens,Human,PAR1,PAR-1,Proteinase-activated receptor 1,Thrombin receptor,TR 96T
H-8325.0025 TRAP_6 (2_6) Salt Trifluoroacetate Binding _ Synonym FLLRN, Coagulation Factor II Receptor (2_6) (human), PAR_1 (2_6) (human), Proteinase Activated Receptor 1 (2_6) (human), Thrombin Receptor (2_6) 25.0 mg
H-8325.0005 TRAP_6 (2_6) Salt Trifluoroacetate Binding _ Synonym FLLRN, Coagulation Factor II Receptor (2_6) (human), PAR_1 (2_6) (human), Proteinase Activated Receptor 1 (2_6) (human), Thrombin Receptor (2_6) 5.0 mg
H-8325.0025 TRAP_6 (2_6) Salt Trifluoroacetate Binding _ Synonym FLLRN, Coagulation Factor II Receptor (2_6) (human), PAR_1 (2_6) (human), Proteinase Activated Receptor 1 (2_6) (human), Thrombin Receptor (2_6) 25.0 mg


 

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