##gff-version 3 P28088 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1660473,ECO:0000269|PubMed:9422751;Dbxref=PMID:1660473,PMID:9422751 P28088 UniProtKB Chain 27 441 . . . ID=PRO_0000012726;Note=Endothelin receptor type B P28088 UniProtKB Topological domain 27 100 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Transmembrane 101 125 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Topological domain 126 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Transmembrane 137 162 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Topological domain 163 174 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Transmembrane 175 196 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Topological domain 197 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Transmembrane 218 242 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Topological domain 243 270 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Transmembrane 271 295 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Topological domain 296 323 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Transmembrane 324 349 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Topological domain 350 361 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Transmembrane 362 388 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Topological domain 389 441 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P28088 UniProtKB Region 30 87 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P28088 UniProtKB Compositional bias 47 69 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P28088 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Modified residue 418 418 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305 P28088 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305 P28088 UniProtKB Modified residue 438 438 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Modified residue 440 440 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Modified residue 441 441 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Lipidation 402 402 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Lipidation 404 404 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9422751;Dbxref=PMID:9422751 P28088 UniProtKB Disulfide bond 173 254 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521