PAR2_MOUSE
ID PAR2_MOUSE Reviewed; 399 AA.
AC P55086;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Proteinase-activated receptor 2;
DE Short=PAR-2;
DE AltName: Full=Coagulation factor II receptor-like 1;
DE AltName: Full=G-protein coupled receptor 11;
DE AltName: Full=Thrombin receptor-like 1;
DE Flags: Precursor;
GN Name=F2rl1; Synonyms=Gpcr11, Gpr11, Par2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7890726; DOI=10.1074/jbc.270.11.5950;
RA Nystedt S., Larsson A.-K., Aaberg H., Sundelin J.;
RT "The mouse proteinase-activated receptor-2 cDNA and gene. Molecular cloning
RT and functional expression.";
RL J. Biol. Chem. 270:5950-5955(1995).
RN [2]
RP FUNCTION IN CARDIOVASCULAR RESPONSES.
RX PubMed=9918574;
RA Damiano B.P., Cheung W.M., Santulli R.J., Fung-Leung W.P., Ngo K., Ye R.D.,
RA Darrow A.L., Derian C.K., de Garavilla L., Andrade-Gordon P.;
RT "Cardiovascular responses mediated by protease-activated receptor-2 (PAR-2)
RT and thrombin receptor (PAR-1) are distinguished in mice deficient in PAR-2
RT or PAR-1.";
RL J. Pharmacol. Exp. Ther. 288:671-678(1999).
RN [3]
RP FUNCTION IN INFLAMMATORY RESPONSE, AND DISRUPTION PHENOTYPE.
RX PubMed=11086091; DOI=10.4049/jimmunol.165.11.6504;
RA Lindner J.R., Kahn M.L., Coughlin S.R., Sambrano G.R., Schauble E.,
RA Bernstein D., Foy D., Hafezi-Moghadam A., Ley K.;
RT "Delayed onset of inflammation in protease-activated receptor-2-deficient
RT mice.";
RL J. Immunol. 165:6504-6510(2000).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=11859856; DOI=10.1254/jjp.88.77;
RA Kawagoe J., Takizawa T., Matsumoto J., Tamiya M., Meek S.E., Smith A.J.,
RA Hunter G.D., Plevin R., Saito N., Kanke T., Fujii M., Wada Y.;
RT "Effect of protease-activated receptor-2 deficiency on allergic dermatitis
RT in the mouse ear.";
RL Jpn. J. Pharmacol. 88:77-84(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=14519665; DOI=10.1096/fj.02-1112com;
RA Seeliger S., Derian C.K., Vergnolle N., Bunnett N.W., Nawroth R.,
RA Schmelz M., Von Der Weid P.Y., Buddenkotte J., Sunderkotter C., Metze D.,
RA Andrade-Gordon P., Harms E., Vestweber D., Luger T.A., Steinhoff M.;
RT "Proinflammatory role of proteinase-activated receptor-2 in humans and mice
RT during cutaneous inflammation in vivo.";
RL FASEB J. 17:1871-1885(2003).
RN [6]
RP FUNCTION IN CYTOSKELETAL REARRANGEMENT AND CHEMOTAXIS.
RX PubMed=12821670; DOI=10.1074/jbc.m300573200;
RA Ge L., Ly Y., Hollenberg M., DeFea K.;
RT "A beta-arrestin-dependent scaffold is associated with prolonged MAPK
RT activation in pseudopodia during protease-activated receptor-2-induced
RT chemotaxis.";
RL J. Biol. Chem. 278:34418-34426(2003).
RN [7]
RP POSSIBLE INVOLVEMENT IN LUNG INFLAMMATION.
RX PubMed=16081834; DOI=10.4049/jimmunol.175.4.2598;
RA Su X., Camerer E., Hamilton J.R., Coughlin S.R., Matthay M.A.;
RT "Protease-activated receptor-2 activation induces acute lung inflammation
RT by neuropeptide-dependent mechanisms.";
RL J. Immunol. 175:2598-2605(2005).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=15879675; DOI=10.1254/jphs.scz050138;
RA Takizawa T., Tamiya M., Hara T., Matsumoto J., Saito N., Kanke T.,
RA Kawagoe J., Hattori Y.;
RT "Abrogation of bronchial eosinophilic inflammation and attenuated eotaxin
RT content in protease-activated receptor 2-deficient mice.";
RL J. Pharmacol. Sci. 98:99-102(2005).
RN [9]
RP INVOLVEMENT IN INFECTIOUS COLITIS, ACTIVATION BY GRANZYME A, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15919826; DOI=10.1073/pnas.0409535102;
RA Hansen K.K., Sherman P.M., Cellars L., Andrade-Gordon P., Pan Z.,
RA Baruch A., Wallace J.L., Hollenberg M.D., Vergnolle N.;
RT "A major role for proteolytic activity and proteinase-activated receptor-2
RT in the pathogenesis of infectious colitis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8363-8368(2005).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=16476770; DOI=10.1084/jem.20052148;
RA Noorbakhsh F., Tsutsui S., Vergnolle N., Boven L.A., Shariat N.,
RA Vodjgani M., Warren K.G., Andrade-Gordon P., Hollenberg M.D., Power C.;
RT "Proteinase-activated receptor 2 modulates neuroinflammation in
RT experimental autoimmune encephalomyelitis and multiple sclerosis.";
RL J. Exp. Med. 203:425-435(2006).
RN [11]
RP TRANSACTIVATION BY F2R.
RX PubMed=17965715; DOI=10.1038/ni1525;
RA Kaneider N.C., Leger A.J., Agarwal A., Nguyen N., Perides G., Derian C.,
RA Covic L., Kuliopulos A.;
RT "'Role reversal' for the receptor PAR1 in sepsis-induced vascular damage.";
RL Nat. Immunol. 8:1303-1312(2007).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=20584806; DOI=10.1136/ard.2010.130336;
RA Ferrell W.R., Kelso E.B., Lockhart J.C., Plevin R., McInnes I.B.;
RT "Protease-activated receptor 2: a novel pathogenic pathway in a murine
RT model of osteoarthritis.";
RL Ann. Rheum. Dis. 69:2051-2054(2010).
RN [13]
RP FUNCTION.
RX PubMed=19845798; DOI=10.1111/j.1365-2567.2009.03144.x;
RA Ramelli G., Fuertes S., Narayan S., Busso N., Acha-Orbea H., So A.;
RT "Protease-activated receptor 2 signalling promotes dendritic cell antigen
RT transport and T-cell activation in vivo.";
RL Immunology 129:20-27(2010).
RN [14]
RP FUNCTION, AND INTERACTION WITH GNAQ; GNA11; GNA12; GNA13 AND GNA14.
RX PubMed=20215560; DOI=10.1124/mol.109.062018;
RA McCoy K.L., Traynelis S.F., Hepler J.R.;
RT "PAR1 and PAR2 couple to overlapping and distinct sets of G proteins and
RT linked signaling pathways to differentially regulate cell physiology.";
RL Mol. Pharmacol. 77:1005-1015(2010).
CC -!- FUNCTION: Receptor for trypsin and trypsin-like enzymes coupled to G
CC proteins. Its function is mediated through the activation of several
CC signaling pathways including phospholipase C (PLC), intracellular
CC calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-
CC kappaB and Rho. Can also be transactivated by cleaved F2r/Par1.
CC Involved in modulation of inflammatory responses and regulation of
CC innate and adaptive immunity, and acts as a sensor for proteolytic
CC enzymes generated during infection. Generally is promoting
CC inflammation. Can signal synergistically with Tlr4 and probably Tlr2 in
CC inflammatory responses and modulates Tlr3 signaling. Has a protective
CC role in establishing the endothelial barrier; the activity involves
CC coagulation factor X. Regulates endothelial cell barrier integrity
CC during neutrophil extravasation, probably following proteolytic
CC cleavage by PRTN3 (By similarity). Proposed to have a bronchoprotective
CC role in airway epithelium, but also shown to compromise the airway
CC epithelial barrier by interrupting E-cadherin adhesion. Involved in the
CC regulation of vascular tone; activation results in hypotension
CC presumably mediated by vasodilation. Associates with a subset of G
CC proteins alpha subunits such as GNAQ, GNA11, GNA14, GNA12 and GNA13,
CC but probably not with G(o)-alpha, G(i) subunit alpha-1 and G(i) subunit
CC alpha-2. Believed to be a class B receptor which internalizes as a
CC complex with arrestin and traffic with it to endosomal vesicles,
CC presumably as desensitized receptor, for extended periods of time.
CC Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via
CC coupling to GNAQ and GNA11; the function involves dissociation of Ripk1
CC and Tradd from Tnfr1. Mediates phosphorylation of nuclear factor NF-
CC kappa-B RELA subunit at 'Ser-536'; the function involves Ikbkb and is
CC predominantly independent of G proteins. Involved in cellular
CC migration. Involved in cytoskeletal rearrangement and chemotaxis
CC through beta-arrestin-promoted scaffolds; the function is independent
CC of GNAQ and GNA11 and involves promotion of cofilin dephosphorylation
CC and actin filament severing. Induces redistribution of Cops5 from the
CC plasma membrane to the cytosol and activation of the JNK cascade is
CC mediated by Cops5. Involved in the recruitment of leukocytes to the
CC sites of inflammation and is the major PAR receptor capable of
CC modulating eosinophil function such as pro-inflammatory cytokine
CC secretion, superoxide production and degranulation. During inflammation
CC promotes dendritic cell maturation, trafficking to the lymph nodes and
CC subsequent T-cell activation. Involved in antimicrobial response of
CC innate immune cells; activation enhances phagocytosis of Gram-positive
CC and killing of Gram-negative bacteria. Acts synergistically with
CC interferon-gamma in enhancing antiviral responses (By similarity).
CC {ECO:0000250|UniProtKB:P55085, ECO:0000269|PubMed:11086091,
CC ECO:0000269|PubMed:12821670, ECO:0000269|PubMed:19845798,
CC ECO:0000269|PubMed:20215560, ECO:0000269|PubMed:9918574}.
CC -!- SUBUNIT: Interacts with TLR4, COPS5 and TMED2 (By similarity).
CC Interacts with GNAQ, GNA11, GNA12, GNA13 and GNA14. {ECO:0000250,
CC ECO:0000269|PubMed:20215560}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein.
CC -!- PTM: A proteolytic cleavage generates a new N-terminus that functions
CC as a tethered ligand. Activating serine proteases include trypsin, mast
CC cell tryptase, coagulation factors VII and Xa, myeloblastin/PRTN3 and
CC membrane-type serine protease 1/ST14. Proposed subsequent cleavage by
CC serine proteases is leading to receptor deactivation and include
CC neutrophil elastase and cathepsin G. At least in part, implicated
CC proteases are also shown to activate the receptor; the glycosylation
CC status of the receptor is thought to contribute to the difference.
CC {ECO:0000250|UniProtKB:P55085}.
CC -!- PTM: N-glycosylated and sialylated. {ECO:0000250|UniProtKB:P55085}.
CC -!- PTM: Multiple phosphorylated on serine and threonine residues in the
CC cytoplasmic region upon receptor activation; required for receptor
CC desensitization and recruitment of beta-arrestin.
CC -!- PTM: Monoubiquitinated by Cbl at the plasma membrane and in early
CC endosomes; not required for receptor endocytosis but for translocation
CC to late endosomes or lysosomes. Deubiquitination involves Stambp and
CC Usp8; required for lysosomal trafficking and receptor degradation (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Delayed onset of inflammation. Reduced
CC progression of osteoarthritis, infectious colitis, allergic dermatitis
CC and experimental autoimmune encephalomyelitis. Upon induced allergic
CC and toxic contact dermatitis ear swelling responses, plasma
CC extravasation and leuocyte adherence are significantly attenuated. Upon
CC ovalbumin (OA) sensitization and following challenge infiltration of
CC eosinophils and increase of eotaxin content in bronchoalveolar lavage
CC fluid are abrogated. {ECO:0000269|PubMed:11086091,
CC ECO:0000269|PubMed:11859856, ECO:0000269|PubMed:14519665,
CC ECO:0000269|PubMed:15879675, ECO:0000269|PubMed:15919826,
CC ECO:0000269|PubMed:16476770, ECO:0000269|PubMed:20584806}.
CC -!- MISCELLANEOUS: Synthetic PAR agonist peptides (APs) that mimic the
CC first six amino acids of the newly formed N-terminus activate the
CC native, uncleaved receptor nonenzymatically by binding directly to the
CC corresponding second extracellular loop to mediate signaling.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z48043; CAA88097.1; -; mRNA.
DR CCDS; CCDS26700.1; -.
DR PIR; I48705; I48705.
DR RefSeq; NP_032000.3; NM_007974.4.
DR AlphaFoldDB; P55086; -.
DR SMR; P55086; -.
DR STRING; 10090.ENSMUSP00000022185; -.
DR ChEMBL; CHEMBL3734647; -.
DR GlyGen; P55086; 2 sites.
DR iPTMnet; P55086; -.
DR PhosphoSitePlus; P55086; -.
DR PaxDb; P55086; -.
DR PeptideAtlas; P55086; -.
DR PRIDE; P55086; -.
DR ProteomicsDB; 294012; -.
DR Antibodypedia; 4569; 312 antibodies from 36 providers.
DR DNASU; 14063; -.
DR Ensembl; ENSMUST00000022185; ENSMUSP00000022185; ENSMUSG00000021678.
DR GeneID; 14063; -.
DR KEGG; mmu:14063; -.
DR UCSC; uc011zda.2; mouse.
DR CTD; 2150; -.
DR MGI; MGI:101910; F2rl1.
DR VEuPathDB; HostDB:ENSMUSG00000021678; -.
DR eggNOG; ENOG502QR8S; Eukaryota.
DR GeneTree; ENSGT01050000244840; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P55086; -.
DR OMA; LAHDMFN; -.
DR OrthoDB; 892946at2759; -.
DR PhylomeDB; P55086; -.
DR TreeFam; TF330775; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 14063; 1 hit in 72 CRISPR screens.
DR ChiTaRS; F2rl1; mouse.
DR PRO; PR:P55086; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P55086; protein.
DR Bgee; ENSMUSG00000021678; Expressed in epithelium of stomach and 118 other tissues.
DR ExpressionAtlas; P55086; baseline and differential.
DR Genevisible; P55086; MM.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:UniProtKB.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:UniProtKB.
DR GO; GO:0032795; F:heterotrimeric G-protein binding; TAS:UniProtKB.
DR GO; GO:0015057; F:thrombin-activated receptor activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR GO; GO:0045217; P:cell-cell junction maintenance; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050900; P:leukocyte migration; ISS:UniProtKB.
DR GO; GO:0070661; P:leukocyte proliferation; IDA:UniProtKB.
DR GO; GO:0097029; P:mature conventional dendritic cell differentiation; IDA:UniProtKB.
DR GO; GO:0032682; P:negative regulation of chemokine production; ISO:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
DR GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; ISO:MGI.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0043311; P:positive regulation of eosinophil degranulation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0003104; P:positive regulation of glomerular filtration; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:MGI.
DR GO; GO:0070963; P:positive regulation of neutrophil mediated killing of gram-negative bacterium; ISO:MGI.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
DR GO; GO:1900135; P:positive regulation of renin secretion into blood stream; IDA:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; ISO:MGI.
DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; ISO:MGI.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI.
DR GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; ISS:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0002286; P:T cell activation involved in immune response; IDA:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IDA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002281; Pro_rcpt_2.
DR InterPro; IPR003912; Protea_act_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01428; PROTEASEAR.
DR PRINTS; PR01152; PROTEASEAR2.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Immunity; Inflammatory response; Innate immunity; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..38
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012752"
FT CHAIN 39..399
FT /note="Proteinase-activated receptor 2"
FT /id="PRO_0000012753"
FT TOPO_DOM 39..73
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TRANSMEM 74..103
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TOPO_DOM 104..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TRANSMEM 111..139
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TOPO_DOM 140..151
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TRANSMEM 152..179
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TOPO_DOM 180..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TRANSMEM 186..213
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TOPO_DOM 214..237
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TRANSMEM 238..271
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TOPO_DOM 272..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TRANSMEM 280..319
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TOPO_DOM 320..325
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TRANSMEM 326..349
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT TOPO_DOM 350..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55085"
FT SITE 38..39
FT /note="Cleavage; by trypsin"
FT /evidence="ECO:0000250"
FT LIPID 363
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ 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
