GENTAUR Molecular Products.

 PAR2_MOUSE              Reviewed;         399 AA.
 P55086;
 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
 01-OCT-1996, sequence version 1.
 28-MAR-2018, entry version 145.
 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}.
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 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; ENSGT00910000143980; -.
 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

Related products :