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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.
29-SEP-2021, entry version 195.
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; DOI=10.1007/bf03401632;
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 immune 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:
P55085; P16615: ATP2A2; NbExp=2; IntAct=EBI-4303189, EBI-358933;
P55085; P22681: CBL; NbExp=3; IntAct=EBI-4303189, EBI-518228;
P55085; Q92905: COPS5; NbExp=8; IntAct=EBI-4303189, EBI-594661;
P55085; Q14868: EPR-1; NbExp=4; IntAct=EBI-4303189, EBI-4309771;
P55085; P13726: F3; NbExp=2; IntAct=EBI-4303189, EBI-1040727;
P55085; P0DMV9: HSPA1B; NbExp=2; IntAct=EBI-4303189, EBI-14100688;
P55085; P04156: PRNP; NbExp=3; IntAct=EBI-4303189, EBI-977302;
P55085; Q15363: TMED2; NbExp=6; IntAct=EBI-4303189, EBI-998485;
P55085; P29066: Arrb1; Xeno; NbExp=6; IntAct=EBI-4303189, EBI-4303019;
-!- 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/";
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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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.
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; -.
SMR; P55085; -.
BioGRID; 108449; 79.
DIP; DIP-42044N; -.
IntAct; P55085; 77.
MINT; P55085; -.
STRING; 9606.ENSP00000296677; -.
BindingDB; P55085; -.
ChEMBL; CHEMBL5963; -.
GuidetoPHARMACOLOGY; 348; -.
TCDB; 9.A.14.13.12; the g-protein-coupled receptor (gpcr) family.
GlyGen; P55085; 2 sites.
iPTMnet; P55085; -.
PhosphoSitePlus; P55085; -.
SwissPalm; P55085; -.
BioMuta; F2RL1; -.
DMDM; 1709580; -.
jPOST; P55085; -.
MassIVE; P55085; -.
MaxQB; P55085; -.
PaxDb; P55085; -.
PeptideAtlas; P55085; -.
PRIDE; P55085; -.
ProteomicsDB; 56787; -.
ABCD; P55085; 81 sequenced antibodies.
Antibodypedia; 4569; 325 antibodies.
DNASU; 2150; -.
Ensembl; ENST00000296677; ENSP00000296677; ENSG00000164251.
GeneID; 2150; -.
KEGG; hsa:2150; -.
UCSC; uc003keo.4; human.
CTD; 2150; -.
DisGeNET; 2150; -.
GeneCards; F2RL1; -.
HGNC; HGNC:3538; F2RL1.
HPA; ENSG00000164251; Tissue enhanced (intestine).
MIM; 600933; gene.
neXtProt; NX_P55085; -.
PharmGKB; PA27947; -.
VEuPathDB; HostDB:ENSG00000164251; -.
eggNOG; ENOG502QR8S; Eukaryota.
HOGENOM; CLU_009579_8_2_1; -.
InParanoid; P55085; -.
OrthoDB; 892946at2759; -.
PhylomeDB; P55085; -.
TreeFam; TF330775; -.
PathwayCommons; P55085; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-416476; G alpha (q) signalling events.
SIGNOR; P55085; -.
BioGRID-ORCS; 2150; 7 hits in 1026 CRISPR screens.
ChiTaRS; F2RL1; human.
GeneWiki; Protease_activated_receptor_2; -.
GenomeRNAi; 2150; -.
Pharos; P55085; Tchem.
PRO; PR:P55085; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P55085; protein.
Bgee; ENSG00000164251; Expressed in colonic mucosa and 189 other tissues.
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:0004930; F:G protein-coupled receptor activity; IMP: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: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: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: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:0032682; P:negative regulation of chemokine production; 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:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:UniProtKB.
GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0002720; P:positive regulation of cytokine production 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:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; 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:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; IDA:UniProtKB.
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.
GO; GO:0042311; P:vasodilation; 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; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
Ubl conjugation.
SIGNAL 1..25
/evidence="ECO:0000255"
PROPEP 26..36
/note="Removed for receptor activation"
/id="PRO_0000012750"
CHAIN 37..397
/note="Proteinase-activated receptor 2"
/id="PRO_0000412954"
CHAIN 38..397
/note="Proteinase-activated receptor 2, alternate cleaved
1"
/id="PRO_0000412956"
CHAIN 39..397
/note="Proteinase-activated receptor 2, alternate cleaved
2"
/id="PRO_0000012751"
TOPO_DOM 37..71
/note="Extracellular"
/evidence="ECO:0000269|PubMed:28445455"
TRANSMEM 72..101
/note="Helical; Name=1"
/evidence="ECO:0000269|PubMed:28445455"
TOPO_DOM 102..108
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:28445455"
TRANSMEM 109..137
/note="Helical; Name=2"
/evidence="ECO:0000269|PubMed:28445455"
TOPO_DOM 138..149
/note="Extracellular"
/evidence="ECO:0000269|PubMed:28445455"
TRANSMEM 150..177
/note="Helical; Name=3"
/evidence="ECO:0000269|PubMed:28445455"
TOPO_DOM 178..183
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:28445455"
TRANSMEM 184..211
/note="Helical; Name=4"
/evidence="ECO:0000269|PubMed:28445455"
TOPO_DOM 212..235
/note="Extracellular"
/evidence="ECO:0000269|PubMed:28445455"
TRANSMEM 236..269
/note="Helical; Name=5"
/evidence="ECO:0000269|PubMed:28445455"
TOPO_DOM 270..277
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:28445455"
TRANSMEM 278..317
/note="Helical; Name=6"
/evidence="ECO:0000269|PubMed:28445455"
TOPO_DOM 318..323
/note="Extracellular"
/evidence="ECO:0000269|PubMed:28445455"
TRANSMEM 324..347
/note="Helical; Name=7"
/evidence="ECO:0000269|PubMed:28445455"
TOPO_DOM 348..397
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:28445455"
REGION 373..397
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
SITE 36..37
/note="Cleavage; by trypsin"
LIPID 361
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:21627585"
CARBOHYD 30
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:12171601"
CARBOHYD 222
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:12171601"
DISULFID 148..226
/evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:28445455, ECO:0007744|PDB:5NDD,
ECO:0007744|PDB:5NDZ, ECO:0007744|PDB:5NJ6"
VARIANT 21
/note="S -> F (in dbSNP:rs2243072)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_012846"
VARIANT 30
/note="N -> S (in dbSNP:rs616235)"
/id="VAR_049435"
VARIANT 270
/note="R -> Q (in dbSNP:rs2243062)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_012847"
VARIANT 291
/note="T -> A (in dbSNP:rs2243083)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_012848"
MUTAGEN 30
/note="N->A: Decreases cell surface expression; when
associate with A-222."
/evidence="ECO:0000269|PubMed:12171601"
MUTAGEN 30
/note="N->A: Increase of sensitivity towards tryptase."
/evidence="ECO:0000269|PubMed:12171601"
MUTAGEN 135
/note="H->Y: Slight reduction in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 154
/note="F->A: Severe reduction in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 157
/note="G->C,M: Severe reduction in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 210
/note="Y->L: No defect in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 222
/note="N->A: Decreases cell surface expression; when
associated with A-30. Loss of sensitivity towards all
tested proteases."
/evidence="ECO:0000269|PubMed:12171601"
MUTAGEN 222
/note="N->Q: No defect in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 227
/note="H->A: No defect in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 227
/note="H->Q: Slight reduction in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 228
/note="D->A,N: Severe reduction in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 327
/note="I->L: Slight reduction in ligand-mediated receptor
activation."
/evidence="ECO:0000269|PubMed:28445455"
MUTAGEN 355..363
/note="Missing: Abolishes signaling through accumulation of
intracellular calcium and phosphoinositide; no effect in
signaling through MAPK."
/evidence="ECO:0000269|PubMed:14607272"
MUTAGEN 361
/note="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
/note="S->A: Reduces receptor desensitization and
internalization, activates ERK1/2; when associated with A-
366."
/evidence="ECO:0000269|PubMed:10725339"
MUTAGEN 366
/note="T->A: Reduces receptor desensitization and
internalization, activates ERK1/2; when associated with A-
363."
/evidence="ECO:0000269|PubMed:10725339"
CONFLICT 138
/note="G -> A (in Ref. 2; AAB47871)"
/evidence="ECO:0000305"
CONFLICT 291
/note="T -> S (in Ref. 7; AAH18130)"
/evidence="ECO:0000305"
HELIX 63..68
/evidence="ECO:0007829|PDB:5NDD"
HELIX 72..75
/evidence="ECO:0007829|PDB:5NDD"
HELIX 77..102
/evidence="ECO:0007829|PDB:5NDD"
HELIX 109..125
/evidence="ECO:0007829|PDB:5NDD"
HELIX 128..136
/evidence="ECO:0007829|PDB:5NDD"
HELIX 145..178
/evidence="ECO:0007829|PDB:5NDD"
HELIX 186..205
/evidence="ECO:0007829|PDB:5NDD"
HELIX 207..210
/evidence="ECO:0007829|PDB:5NDD"
STRAND 215..218
/evidence="ECO:0007829|PDB:5NDD"
TURN 219..222
/evidence="ECO:0007829|PDB:5NDD"
STRAND 223..229
/evidence="ECO:0007829|PDB:5NDD"
HELIX 233..235
/evidence="ECO:0007829|PDB:5NDD"
HELIX 236..249
/evidence="ECO:0007829|PDB:5NDD"
HELIX 252..269
/evidence="ECO:0007829|PDB:5NDD"
HELIX 279..298
/evidence="ECO:0007829|PDB:5NDD"
HELIX 301..316
/evidence="ECO:0007829|PDB:5NDD"
HELIX 323..332
/evidence="ECO:0007829|PDB:5NDD"
HELIX 333..335
/evidence="ECO:0007829|PDB:5NDD"
HELIX 336..347
/evidence="ECO:0007829|PDB:5NDD"
HELIX 349..358
/evidence="ECO:0007829|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


Related products :

Catalog number Product name Quantity
18-461-10068 Proteinase-activated receptor 2 - PAR-2; Thrombin receptor-like 1; Coagulation factor II receptor-like 1; G-protein coupled receptor 11 Polyclonal 0.05 ml
18-461-10067 Proteinase-activated receptor 2 - PAR-2; Thrombin receptor-like 1; Coagulation factor II receptor-like 1; G-protein coupled receptor 11 Polyclonal 0.05 ml
EIAAB29879 Coagulation factor II receptor-like 1,F2rl1,Gpcr11,Gpr11,G-protein coupled receptor 11,Mouse,Mus musculus,Par2,PAR-2,Proteinase-activated receptor 2,Thrombin receptor-like 1
EIAAB29881 Coagulation factor II receptor-like 1,F2RL1,GPR11,G-protein coupled receptor 11,Homo sapiens,Human,PAR2,PAR-2,Proteinase-activated receptor 2,Thrombin receptor-like 1
EIAAB29890 Coagulation factor II receptor-like 3,F2rl3,Par4,PAR-4,Proteinase-activated receptor 4,Rat,Rattus norvegicus,Thrombin receptor-like 3
EIAAB29878 Coagulation factor II receptor-like 1,F2rl1,Par2,PAR-2,Proteinase-activated receptor 2,Rat,Rattus norvegicus,Thrombin receptor-like 1
EIAAB29880 Bos taurus,Bovine,Coagulation factor II receptor-like 1,F2RL1,PAR2,PAR-2,Proteinase-activated receptor 2,Thrombin receptor-like 1
EIAAB29883 Coagulation factor II receptor-like 2,F2rl2,Par3,PAR-3,Proteinase-activated receptor 3,Rat,Rattus norvegicus,Thrombin receptor-like 2
EIAAB29882 Coagulation factor II receptor-like 2,F2rl2,Mouse,Mus musculus,Par3,PAR-3,Proteinase-activated receptor 3,Thrombin receptor-like 2
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
Pathways :
WP1348: Androgen Receptor Signaling Pathway
WP1345: T Cell Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP2292: Chemokine signaling pathway
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1929: Thrombin signalling through proteinase activated receptors (PARs)
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP2272: Pathogenic Escherichia coli infection
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP2328: Allograft rejection
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP566: canonical wnt - zebrafish
WP926: TGF-beta Receptor Signaling Pathway
WP1965: VEGF-receptor Signal Transduction
WP285: B Cell Receptor Signaling Pathway
WP1004: Kit Receptor Signaling Pathway
WP138: Androgen receptor signaling pathway
WP1025: B Cell Receptor Signaling Pathway
WP1449: Regulation of toll-like receptor signaling pathway

Related Genes :
[F2RL1 GPR11 PAR2] 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]
[F2rl1 Gpcr11 Gpr11 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1)
[F2rl1 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (Thrombin receptor-like 1)
[F2RL1 PAR2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (Thrombin receptor-like 1)
[F2RL3 PAR4] Proteinase-activated receptor 4 (PAR-4) (Coagulation factor II receptor-like 3) (Thrombin receptor-like 3)
[F2rl3 Par4] Proteinase-activated receptor 4 (PAR-4) (Coagulation factor II receptor-like 3) (Thrombin receptor-like 3)
[Rack1 Gnb2-rs1 Gnb2l1] Receptor of activated protein C kinase 1 (12-3) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) (p205) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[F2rl3 Par4] Proteinase-activated receptor 4 (PAR-4) (Coagulation factor II receptor-like 3) (Thrombin receptor-like 3)
[RACK1 GNB2L1 HLC7 PIG21] Receptor of activated protein C kinase 1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Small ribosomal subunit protein RACK1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[Rack1 Gnb2l1] Receptor of activated protein C kinase 1 (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed]
[RACK1 GNB2L1] Receptor of activated protein C kinase 1 (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed]
[RACK1 GNB2L1] Receptor of activated protein C kinase 1 (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed]
[Med1 Crsp210 Drip205 Pbp Pparbp Trap220 Trip2] Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2)
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; p3; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[gag] Gag polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-)]
[] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like protease nsp3 (EC 3.4.19.12) (EC 3.4.22.-) (Non-structural protein 3) (nsp3) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase nsp5 (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like protease nsp3 (EC 3.4.19.12) (EC 3.4.22.-) (Non-structural protein 3) (nsp3) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase nsp5 (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase nsp12 (Pol) (RdRp) (EC 2.7.7.48) (Non-structural protein 12) (nsp12); Helicase nsp13 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Non-structural protein 13) (nsp13); Proofreading exoribonuclease nsp14 (ExoN) (EC 3.1.13.-) (Guanine-N7 methyltransferase) (Non-structural protein 14) (nsp14); Uridylate-specific endoribonuclease nsp15 (EC 4.6.1.-) (NendoU) (Non-structural protein 15) (nsp15); 2'-O-methyltransferase nsp16 (EC 2.1.1.57) (Non-structural protein 16) (nsp16)]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; p3; Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[GPER1 CEPR CMKRL2 DRY12 GPER GPR30] G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (Flow-induced endothelial G-protein coupled receptor 1) (FEG-1) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (GPCR-Br) (IL8-related receptor DRY12) (Lymphocyte-derived G-protein coupled receptor) (LYGPR) (Membrane estrogen receptor) (mER)
[MED1 ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2] Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)
[daf-2 Y55D5A.5] Insulin-like receptor (IR) (EC 2.7.10.1) (Abnormal dauer formation protein 2) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta]
[Tnk2 Ack1] Activated CDC42 kinase 1 (ACK-1) (EC 2.7.10.2) (EC 2.7.11.1) (Non-receptor protein tyrosine kinase Ack) (Tyrosine kinase non-receptor protein 2)
[PTPRN ICA3 ICA512] Receptor-type tyrosine-protein phosphatase-like N (R-PTP-N) (Islet cell antigen 512) (ICA 512) (Islet cell autoantigen 3) (PTP IA-2) [Cleaved into: ICA512-N-terminal fragment (ICA512-NTF); ICA512-transmembrane fragment (ICA512-TMF); ICA512-cleaved cytosolic fragment (ICA512-CCF)]
[TNK2 ACK1 ACK2] Activated CDC42 kinase 1 (ACK-1) (EC 2.7.10.2) (EC 2.7.11.1) (Activated CDC42 kinase 2) (Tyrosine kinase non-receptor protein 2)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[Ptprn Ptp35] Receptor-type tyrosine-protein phosphatase-like N (R-PTP-N) (PTP IA-2) [Cleaved into: ICA512-N-terminal fragment (ICA512-NTF); ICA512-transmembrane fragment (ICA512-TMF); ICA512-cleaved cytosolic fragment (ICA512-CCF)]
[Ptprn] Receptor-type tyrosine-protein phosphatase-like N (R-PTP-N) (105 kDa islet cell antigen) (BEM-3) (Brain-enriched membrane-associated protein tyrosine phosphatase) (ICA105) (ICA512) (PTP IA-2) (PTPLP) [Cleaved into: ICA512-N-terminal fragment (ICA512-NTF); ICA512-transmembrane fragment (ICA512-TMF); ICA512-cleaved cytosolic fragment (ICA512-CCF)]

Bibliography :