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 24-JAN-2024, entry version 179. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P55086; 2 sites, No reported glycans. DR GlyGen; P55086; 2 sites. DR iPTMnet; P55086; -. DR PhosphoSitePlus; P55086; -. DR PaxDb; 10090-ENSMUSP00000022185; -. DR PeptideAtlas; P55086; -. DR ProteomicsDB; 294012; -. DR Antibodypedia; 4569; 382 antibodies from 36 providers. DR DNASU; 14063; -. DR Ensembl; ENSMUST00000022185.10; ENSMUSP00000022185.9; ENSMUSG00000021678.10. DR GeneID; 14063; -. DR KEGG; mmu:14063; -. DR UCSC; uc011zda.2; mouse. DR AGR; MGI:101910; -. 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; SQSHVYA; -. DR OrthoDB; 4075920at2759; -. 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; 2 hits in 77 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 121 other cell types or tissues. DR ExpressionAtlas; P55086; baseline and differential. DR GO; GO:0005769; C:early endosome; 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:0002020; F:protease binding; ISO:MGI. DR GO; GO:0001648; F:proteinase-activated receptor activity; IMP:MGI. 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:0046676; P:negative regulation of insulin secretion; IMP: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:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISO:MGI. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB. 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: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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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:0032729; P:positive regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0099109; P:potassium channel activating, G protein-coupled receptor signaling pathway; IMP:MGI. DR GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI. DR GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB. DR GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; 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 CDD; cd15370; 7tmA_PAR2; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR002281; Pro_rcpt_2. DR InterPro; IPR003912; Protea_act_rcpt. DR PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR24232:SF21; PROTEINASE-ACTIVATED RECEPTOR 2; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01428; PROTEASEAR. DR PRINTS; PR01152; PROTEASEAR2. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P55086; MM. 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 //