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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)

 PAR2_MOUSE              Reviewed;         399 AA.
P55086;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-JUN-2018, entry version 146.
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;
Flags: Precursor;
Name=F2rl1; Synonyms=Gpcr11, Gpr11, Par2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7890726; DOI=10.1074/jbc.270.11.5950;
Nystedt S., Larsson A.-K., Aaberg H., Sundelin J.;
"The mouse proteinase-activated receptor-2 cDNA and gene. Molecular
cloning and functional expression.";
J. Biol. Chem. 270:5950-5955(1995).
[2]
FUNCTION IN CARDIOVASCULAR RESPONSES.
PubMed=9918574;
Damiano B.P., Cheung W.M., Santulli R.J., Fung-Leung W.P., Ngo K.,
Ye R.D., Darrow A.L., Derian C.K., de Garavilla L., Andrade-Gordon P.;
"Cardiovascular responses mediated by protease-activated receptor-2
(PAR-2) and thrombin receptor (PAR-1) are distinguished in mice
deficient in PAR-2 or PAR-1.";
J. Pharmacol. Exp. Ther. 288:671-678(1999).
[3]
FUNCTION IN INFLAMMATORY RESPONSE, AND DISRUPTION PHENOTYPE.
PubMed=11086091; DOI=10.4049/jimmunol.165.11.6504;
Lindner J.R., Kahn M.L., Coughlin S.R., Sambrano G.R., Schauble E.,
Bernstein D., Foy D., Hafezi-Moghadam A., Ley K.;
"Delayed onset of inflammation in protease-activated receptor-2-
deficient mice.";
J. Immunol. 165:6504-6510(2000).
[4]
DISRUPTION PHENOTYPE.
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).
[5]
DISRUPTION PHENOTYPE.
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).
[6]
FUNCTION IN CYTOSKELETAL REARRANGEMENT AND CHEMOTAXIS.
PubMed=12821670; DOI=10.1074/jbc.M300573200;
Ge L., Ly Y., Hollenberg M., DeFea K.;
"A beta-arrestin-dependent scaffold is associated with prolonged MAPK
activation in pseudopodia during protease-activated receptor-2-induced
chemotaxis.";
J. Biol. Chem. 278:34418-34426(2003).
[7]
POSSIBLE INVOLVEMENT IN LUNG INFLAMMATION.
PubMed=16081834; DOI=10.4049/jimmunol.175.4.2598;
Su X., Camerer E., Hamilton J.R., Coughlin S.R., Matthay M.A.;
"Protease-activated receptor-2 activation induces acute lung
inflammation by neuropeptide-dependent mechanisms.";
J. Immunol. 175:2598-2605(2005).
[8]
DISRUPTION PHENOTYPE.
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).
[9]
INVOLVEMENT IN INFECTIOUS COLITIS, ACTIVATION BY GRANZYME A, AND
DISRUPTION PHENOTYPE.
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).
[10]
DISRUPTION PHENOTYPE.
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).
[11]
TRANSACTIVATION BY F2R.
PubMed=17965715; DOI=10.1038/ni1525;
Kaneider N.C., Leger A.J., Agarwal A., Nguyen N., Perides G.,
Derian C., Covic L., Kuliopulos A.;
"'Role reversal' for the receptor PAR1 in sepsis-induced vascular
damage.";
Nat. Immunol. 8:1303-1312(2007).
[12]
DISRUPTION PHENOTYPE.
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).
[13]
FUNCTION.
PubMed=19845798; DOI=10.1111/j.1365-2567.2009.03144.x;
Ramelli G., Fuertes S., Narayan S., Busso N., Acha-Orbea H., So A.;
"Protease-activated receptor 2 signalling promotes dendritic cell
antigen transport and T-cell activation in vivo.";
Immunology 129:20-27(2010).
[14]
FUNCTION, AND INTERACTION WITH GNAQ; GNA11; GNA12; GNA13 AND GNA14.
PubMed=20215560; DOI=10.1124/mol.109.062018;
McCoy K.L., Traynelis S.F., Hepler J.R.;
"PAR1 and PAR2 couple to overlapping and distinct sets of G proteins
and linked signaling pathways to differentially regulate cell
physiology.";
Mol. Pharmacol. 77:1005-1015(2010).
-!- FUNCTION: Receptor for trypsin and trypsin-like enzymes coupled to
G proteins. Its function is mediated through the activation of
several signaling pathways including phospholipase C (PLC),
intracellular calcium, mitogen-activated protein kinase (MAPK), I-
kappaB kinase/NF-kappaB and Rho. Can also be transactivated by
cleaved F2r/Par1. Involved in modulation of inflammatory responses
and regulation of innate and adaptive immunity, and acts as a
sensor for proteolytic enzymes generated during infection.
Generally is promoting inflammation. Can signal synergistically
with Tlr4 and probably Tlr2 in inflammatory responses and
modulates Tlr3 signaling. Has a protective role in establishing
the endothelial barrier; the activity involves coagulation factor
X. Regulates endothelial cell barrier integrity during neutrophil
extravasation, probably following proteolytic cleavage by PRTN3
(By similarity). Proposed to have a bronchoprotective role in
airway epithelium, but also shown to compromise the airway
epithelial barrier by interrupting E-cadherin adhesion. Involved
in the regulation of vascular tone; activation results in
hypotension presumably mediated by vasodilation. Associates with a
subset of G proteins alpha subunits such as GNAQ, GNA11, GNA14,
GNA12 and GNA13, but probably not with G(o) alpha, G(i) subunit
alpha-1 and G(i) subunit alpha-2. 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 (By similarity). {ECO:0000250|UniProtKB:P55085,
ECO:0000269|PubMed:11086091, ECO:0000269|PubMed:12821670,
ECO:0000269|PubMed:19845798, ECO:0000269|PubMed:20215560,
ECO:0000269|PubMed:9918574}.
-!- SUBUNIT: Interacts with TLR4, COPS5 and TMED2 (By similarity).
Interacts with GNAQ, GNA11, GNA12, GNA13 and GNA14. {ECO:0000250,
ECO:0000269|PubMed:20215560}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein.
-!- PTM: A proteolytic cleavage generates a new N-terminus that
functions as a tethered ligand. Activating serine proteases
include trypsin, mast cell tryptase, coagulation factors VII and
Xa, myeloblastin/PRTN3 and membrane-type serine protease 1/ST14.
Proposed subsequent cleaveage by serine proteases is leading to
receptor deactivation and include neutrophil elastase and
cathepsin G. At least in part, implicated proteases are also shown
to activate the receptor; the glycosylation status of the receptor
is thought to contribute to the difference.
{ECO:0000250|UniProtKB:P55085}.
-!- PTM: N-glycosylated and sialylated.
{ECO:0000250|UniProtKB:P55085}.
-!- PTM: Multiple phosphorylated on serine and threonine residues in
the cytoplasmic region upon receptor activation; required for
receptor desensitization and recruitment of beta-arrestin.
-!- 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 (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Delayed onset of inflammation. Reduced
progression of osteoarthritis, infectious colitis, allergic
dermatitis and experimental autoimmune encephalomyelitis. Upon
induced allergic and toxic contact dermatitis ear swelling
responses, plasma extravasation and leuocyte adherence are
significantly attenuated. Upon ovalbumin (OA) sensitization and
following challenge infiltration of eosinophils and increase of
eotaxin content in bronchoalveolar lavage fluid are abrogated.
{ECO:0000269|PubMed:11086091, ECO:0000269|PubMed:11859856,
ECO:0000269|PubMed:14519665, ECO:0000269|PubMed:15879675,
ECO:0000269|PubMed:15919826, ECO:0000269|PubMed:16476770,
ECO:0000269|PubMed:20584806}.
-!- 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.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; Z48043; CAA88097.1; -; mRNA.
CCDS; CCDS26700.1; -.
PIR; I48705; I48705.
RefSeq; NP_032000.3; NM_007974.4.
UniGene; Mm.1614; -.
ProteinModelPortal; P55086; -.
SMR; P55086; -.
STRING; 10090.ENSMUSP00000022185; -.
ChEMBL; CHEMBL3734647; -.
iPTMnet; P55086; -.
PhosphoSitePlus; P55086; -.
PaxDb; P55086; -.
PeptideAtlas; P55086; -.
PRIDE; P55086; -.
Ensembl; ENSMUST00000022185; ENSMUSP00000022185; ENSMUSG00000021678.
GeneID; 14063; -.
KEGG; mmu:14063; -.
UCSC; uc011zda.2; mouse.
CTD; 2150; -.
MGI; MGI:101910; F2rl1.
eggNOG; ENOG410IGEM; Eukaryota.
eggNOG; ENOG4111CWR; LUCA.
GeneTree; ENSGT00920000148955; -.
HOGENOM; HOG000116291; -.
HOVERGEN; HBG105658; -.
InParanoid; P55086; -.
KO; K04234; -.
OMA; GDMFNYF; -.
OrthoDB; EOG091G0C2F; -.
PhylomeDB; P55086; -.
TreeFam; TF330775; -.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
Reactome; R-MMU-416476; G alpha (q) signalling events.
ChiTaRS; F2rl1; mouse.
PRO; PR:P55086; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021678; -.
CleanEx; MM_F2RL1; -.
ExpressionAtlas; P55086; baseline and differential.
Genevisible; P55086; MM.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:UniProtKB.
GO; GO:0031681; F:G-protein beta-subunit binding; IDA:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; IMP:UniProtKB.
GO; GO:0032795; F:heterotrimeric G-protein binding; TAS:UniProtKB.
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; ISO:MGI.
GO; GO:0035926; P:chemokine (C-C motif) ligand 2 secretion; ISS: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; ISO:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
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; IDA:UniProtKB.
GO; GO:0050702; P:interleukin-1 beta secretion; ISS:UniProtKB.
GO; GO:0072608; P:interleukin-10 secretion; ISS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; ISS:UniProtKB.
GO; GO:0070661; P:leukocyte proliferation; IDA:UniProtKB.
GO; GO:0097029; P:mature conventional dendritic cell differentiation; IDA:UniProtKB.
GO; GO:0090198; P:negative regulation of chemokine secretion; ISO:MGI.
GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; ISO:MGI.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISO:MGI.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; ISS: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; ISO:MGI.
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; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; ISS:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:MGI.
GO; GO:0070963; P:positive regulation of neutrophil mediated killing of gram-negative bacterium; ISO:MGI.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
GO; GO:1900135; P:positive regulation of renin secretion into blood stream; IDA:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; ISO:MGI.
GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; ISO:MGI.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
GO; GO:0002286; P:T cell activation involved in immune response; IDA: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;
Cell membrane; Complete proteome; 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 {ECO:0000255}.
PROPEP 26 38 Removed for receptor activation.
{ECO:0000250}.
/FTId=PRO_0000012752.
CHAIN 39 399 Proteinase-activated receptor 2.
/FTId=PRO_0000012753.
TOPO_DOM 39 73 Extracellular.
{ECO:0000250|UniProtKB:P55085}.
TRANSMEM 74 103 Helical; Name=1.
{ECO:0000250|UniProtKB:P55085}.
TOPO_DOM 104 110 Cytoplasmic.
{ECO:0000250|UniProtKB:P55085}.
TRANSMEM 111 139 Helical; Name=2.
{ECO:0000250|UniProtKB:P55085}.
TOPO_DOM 140 151 Extracellular.
{ECO:0000250|UniProtKB:P55085}.
TRANSMEM 152 179 Helical; Name=3.
{ECO:0000250|UniProtKB:P55085}.
TOPO_DOM 180 185 Cytoplasmic.
{ECO:0000250|UniProtKB:P55085}.
TRANSMEM 186 213 Helical; Name=4.
{ECO:0000250|UniProtKB:P55085}.
TOPO_DOM 214 237 Extracellular.
{ECO:0000250|UniProtKB:P55085}.
TRANSMEM 238 271 Helical; Name=5.
{ECO:0000250|UniProtKB:P55085}.
TOPO_DOM 272 279 Cytoplasmic.
{ECO:0000250|UniProtKB:P55085}.
TRANSMEM 280 319 Helical; Name=6.
{ECO:0000250|UniProtKB:P55085}.
TOPO_DOM 320 325 Extracellular.
{ECO:0000250|UniProtKB:P55085}.
TRANSMEM 326 349 Helical; Name=7.
{ECO:0000250|UniProtKB:P55085}.
TOPO_DOM 350 399 Cytoplasmic.
{ECO:0000250|UniProtKB:P55085}.
COMPBIAS 385 394 Poly-Ser.
SITE 38 39 Cleavage; by trypsin. {ECO:0000250}.
LIPID 363 363 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 150 228 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 399 AA; 44752 MW; A93749425ED0B194 CRC64;
MRSLSLAWLL GGITLLAASV SCSRTENLAP GRNNSKGRSL IGRLETQPPI TGKGVPVEPG
FSIDEFSASI LTGKLTTVFL PVVYIIVFVI GLPSNGMALW IFLFRTKKKH PAVIYMANLA
LADLLSVIWF PLKISYHLHG NNWVYGEALC KVLIGFFYGN MYCSILFMTC LSVQRYWVIV
NPMGHPRKKA NIAVGVSLAI WLLIFLVTIP LYVMKQTIYI PALNITTCHD VLPEEVLVGD
MFNYFLSLAI GVFLFPALLT ASAYVLMIKT LRSSAMDEHS EKKRQRAIRL IITVLAMYFI
CFAPSNLLLV VHYFLIKTQR QSHVYALYLV ALCLSTLNSC IDPFVYYFVS KDFRDHARNA
LLCRSVRTVN RMQISLSSNK FSRKSGSYSS SSTSVKTSY


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EIAAB29888 Coagulation factor II receptor-like 3,F2RL3,Homo sapiens,Human,PAR4,PAR-4,Proteinase-activated receptor 4,Thrombin receptor-like 3
U0826h CLIA 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
E0826h ELISA 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-8325.0025 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


 

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