ID   EDNRB_CANLF             Reviewed;         442 AA.
AC   P56497; Q5KSU8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 3.
DT   27-MAR-2024, entry version 122.
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: Precursor;
GN   Name=EDNRB;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tsukui T., Yasuda N., Maeda S., Koyanagi M., Hashimoto R., Masuda K.,
RA   Ohno K., Sakaguchi M., Tsujimoto H., Iwabuchi S.;
RT   "Expression analysis of endothelin receptor type B gene in canine atopic
RT   dermatitis.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-426.
RA   Zemke D., Yuzbasiyan-Gurkan V.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P24530};
CC       Multi-pass membrane protein. Note=internalized after activation by
CC       endothelins. {ECO:0000250|UniProtKB:P24530}.
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; AB183285; BAD83850.1; -; mRNA.
DR   EMBL; AF034530; AAC26970.1; -; mRNA.
DR   RefSeq; NP_001010943.2; NM_001010943.2.
DR   AlphaFoldDB; P56497; -.
DR   SMR; P56497; -.
DR   STRING; 9615.ENSCAFP00000007760; -.
DR   GlyCosmos; P56497; 1 site, No reported glycans.
DR   PaxDb; 9612-ENSCAFP00000007760; -.
DR   GeneID; 403862; -.
DR   KEGG; cfa:403862; -.
DR   CTD; 1910; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P56497; -.
DR   OrthoDB; 2905228at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004962; F:endothelin receptor activity; ISS:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0048066; P:developmental pigmentation; IBA:GO_Central.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048484; P:enteric nervous system development; IEA:InterPro.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; IBA:GO_Central.
DR   CDD; cd15976; 7tmA_ET-BR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000499; Endthln_rcpt.
DR   InterPro; IPR001112; ETB_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR46099:SF3; ENDOTHELIN RECEPTOR TYPE B; 1.
DR   PANTHER; PTHR46099; G_PROTEIN_RECEP_F1_2 DOMAIN-CONTAINING PROTEIN; 1.
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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..442
FT                   /note="Endothelin receptor type B"
FT                   /id="PRO_0000012727"
FT   TOPO_DOM        27..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..126
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..163
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..175
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..197
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..243
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..271
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..296
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..324
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..350
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..389
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..442
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          69..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28088"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28088"
FT   MOD_RES         439
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P28088"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28088"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28088"
FT   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28088"
FT   LIPID           402
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           403
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           405
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        174..255
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   442 AA;  49722 MW;  3E9EE7AE581D7E15 CRC64;
     MQPPPSLCGR ALVALVLACG LSRIWGEERG FPPDRATPLL QTAEIMTPPT KTLWPKGSNA
     SLARSLAPAE VPKGDRTAGS PPRTISPPPC EGSIEIKETF KYINTVVSCL VFVLGIIGNS
     TLLRIIYKNK CMRNGPNILI ASLALGDLLH IIIDIPITVY KLLAEDWPFG VEMCKLVPFI
     QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAVGF
     DMITIDYKGR YLRICLLHPT QKTAFMQFYK TAKDWWLFSF YFCLPLAITA FFYTLMTCEM
     LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTIY DQNDPNRCEL
     LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQSFEE KQSLEEKQSC
     LKFKANDHGY DNFRSSNKYS SS
//