##gff-version 3 P55085 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P55085 UniProtKB Propeptide 26 36 . . . ID=PRO_0000012750;Note=Removed for receptor activation P55085 UniProtKB Chain 37 397 . . . ID=PRO_0000412954;Note=Proteinase-activated receptor 2 P55085 UniProtKB Chain 38 397 . . . ID=PRO_0000412956;Note=Proteinase-activated receptor 2%2C alternate cleaved 1 P55085 UniProtKB Chain 39 397 . . . ID=PRO_0000012751;Note=Proteinase-activated receptor 2%2C alternate cleaved 2 P55085 UniProtKB Topological domain 37 71 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Transmembrane 72 101 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Topological domain 102 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Transmembrane 109 137 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Topological domain 138 149 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Transmembrane 150 177 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Topological domain 178 183 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Transmembrane 184 211 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Topological domain 212 235 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Transmembrane 236 269 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Topological domain 270 277 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Transmembrane 278 317 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Topological domain 318 323 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Transmembrane 324 347 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Topological domain 348 397 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Region 373 397 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P55085 UniProtKB Site 36 37 . . . Note=Cleavage%3B by trypsin P55085 UniProtKB Lipidation 361 361 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21627585;Dbxref=PMID:21627585 P55085 UniProtKB Glycosylation 30 30 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12171601;Dbxref=PMID:12171601 P55085 UniProtKB Glycosylation 222 222 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12171601;Dbxref=PMID:12171601 P55085 UniProtKB Disulfide bond 148 226 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00521,ECO:0000269|PubMed:28445455,ECO:0007744|PDB:5NDD,ECO:0007744|PDB:5NDZ,ECO:0007744|PDB:5NJ6;Dbxref=PMID:28445455 P55085 UniProtKB Natural variant 21 21 . . . ID=VAR_012846;Note=S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs2243072 P55085 UniProtKB Natural variant 30 30 . . . ID=VAR_049435;Note=N->S;Dbxref=dbSNP:rs616235 P55085 UniProtKB Natural variant 270 270 . . . ID=VAR_012847;Note=R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs2243062 P55085 UniProtKB Natural variant 291 291 . . . ID=VAR_012848;Note=T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs2243083 P55085 UniProtKB Mutagenesis 30 30 . . . Note=Decreases cell surface expression%3B when associate with A-222. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12171601;Dbxref=PMID:12171601 P55085 UniProtKB Mutagenesis 30 30 . . . Note=Increase of sensitivity towards tryptase. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12171601;Dbxref=PMID:12171601 P55085 UniProtKB Mutagenesis 135 135 . . . Note=Slight reduction in ligand-mediated receptor activation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 154 154 . . . Note=Severe reduction in ligand-mediated receptor activation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 157 157 . . . Note=Severe reduction in ligand-mediated receptor activation. G->C%2CM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 210 210 . . . Note=No defect in ligand-mediated receptor activation. Y->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 222 222 . . . Note=Decreases cell surface expression%3B when associated with A-30. Loss of sensitivity towards all tested proteases. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12171601;Dbxref=PMID:12171601 P55085 UniProtKB Mutagenesis 222 222 . . . Note=No defect in ligand-mediated receptor activation. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 227 227 . . . Note=No defect in ligand-mediated receptor activation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 227 227 . . . Note=Slight reduction in ligand-mediated receptor activation. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 228 228 . . . Note=Severe reduction in ligand-mediated receptor activation. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 327 327 . . . Note=Slight reduction in ligand-mediated receptor activation. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28445455;Dbxref=PMID:28445455 P55085 UniProtKB Mutagenesis 355 363 . . . Note=Abolishes signaling through accumulation of intracellular calcium and phosphoinositide%3B no effect in signaling through MAPK. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14607272;Dbxref=PMID:14607272 P55085 UniProtKB Mutagenesis 361 361 . . . Note=Loss of palmitoylation%3B increases surface expression and internalization following trypsin activation%2C decreases sensitivity and intracellular calcium signaling%2C increases ERK activation through G(i) subunit alpha. C->A P55085 UniProtKB Mutagenesis 363 363 . . . Note=Reduces receptor desensitization and internalization%2C activates ERK1/2%3B when associated with A-366. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10725339;Dbxref=PMID:10725339 P55085 UniProtKB Mutagenesis 366 366 . . . Note=Reduces receptor desensitization and internalization%2C activates ERK1/2%3B when associated with A-363. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10725339;Dbxref=PMID:10725339 P55085 UniProtKB Sequence conflict 138 138 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55085 UniProtKB Sequence conflict 291 291 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55085 UniProtKB Helix 63 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 72 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 77 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 109 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 128 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 145 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 186 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 207 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Turn 219 222 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Beta strand 223 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 233 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 236 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 252 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 279 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 301 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 323 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 333 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 336 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD P55085 UniProtKB Helix 349 358 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NDD