ID   EDNRB_COTJA             Reviewed;         347 AA.
AC   Q90328;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Endothelin receptor type B {ECO:0000305};
DE            Short=ET-B;
DE            Short=ET-BR;
DE   AltName: Full=Endothelin receptor non-selective type;
DE   Flags: Fragment;
GN   Name=EDNRB;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8790384; DOI=10.1073/pnas.93.18.9645;
RA   Nataf V., Lecoin L., Eichmann A., le Douarin N.M.;
RT   "Endothelin-B receptor is expressed by neural crest cells in the avian
RT   embryo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:9645-9650(1996).
CC   -!- FUNCTION: Non-specific receptor for endothelin 1, 2, and 3. Mediates
CC       its action by association with G proteins that activate a
CC       phosphatidylinositol-calcium second messenger system (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Endothelin receptor subfamily. EDNRB sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X99295; CAA67681.1; -; mRNA.
DR   AlphaFoldDB; Q90328; -.
DR   SMR; Q90328; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004962; F:endothelin receptor activity; IEA:InterPro.
DR   GO; GO:0048484; P:enteric nervous system development; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR   InterPro; IPR000499; Endthln_rcpt.
DR   InterPro; IPR001112; ETB_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00571; ENDOTHELINBR.
DR   PRINTS; PR00366; ENDOTHELINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Lipoprotein;
KW   Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..347
FT                   /note="Endothelin receptor type B"
FT                   /id="PRO_0000069441"
FT   TOPO_DOM        <1..7
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..69
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..103
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..149
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..177
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..202
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        203..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..256
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..268
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..295
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..347
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           309
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           311
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        80..161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
SQ   SEQUENCE   347 AA;  39826 MW;  3F6A03F8E6895D30 CRC64;
     EIKETFKYIN TVVSCLVFVL GIIGNSTLLR IIYKNKCMRN GPNILIASLA LGDLLHIIID
     IPISVYKLLA EDWPFGVEMC KLVPFIQKAS VGITVLSLCA LSIDRYRAVA SWSRIKGIGV
     PKWTAVEIVL IWVISVVLAV PEAIAFDMIT MEYRGKDLRI CLLHPTQKTS FMMFYKQAKD
     WWLFSFYFCL PLAITALFYT LMTCEMLRKK SGMQIALNDH LKQRREVAKT VFCLVLVFAL
     CWLPLHLSRI LKLTIYDQKD PNRCELLSFF LVMDYIGINM ASLNSCINPI ALYLVSKRFQ
     NCFKSCLCCW CQSKDLLSLE ERQSCLKFKA NDHGYDNFRS SNKYSSS