ID   EDNRB_BOVIN             Reviewed;         441 AA.
AC   P28088; Q0VCB3; Q9TSB9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 160.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1660473; DOI=10.1016/s0021-9258(18)54515-4;
RA   Saito Y., Mizuno T., Itakura M., Suzuki Y., Ito T., Hagiwara H., Hirose S.;
RT   "Primary structure of bovine endothelin ETB receptor and identification of
RT   signal peptidase and metal proteinase cleavage sites.";
RL   J. Biol. Chem. 266:23433-23437(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 124-127; 262-269; 304-315; 417-421 AND 424-432.
RC   TISSUE=Lung;
RX   PubMed=1653249; DOI=10.1016/s0021-9258(18)55386-2;
RA   Kozuka M., Ito T., Hirose S., Lodhi K.M., Hagiwara H.;
RT   "Purification and characterization of bovine lung endothelin receptor.";
RL   J. Biol. Chem. 266:16892-16896(1991).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Lung;
RX   PubMed=8529649; DOI=10.1111/j.1432-1033.1995.251_c.x;
RA   Hick S., Heidemann I., Soskic V., Muller-Esterl W., Godovac-Zimmermann J.;
RT   "Isolation of the endothelin B receptor from bovine lung. Structure, signal
RT   sequence, and binding site.";
RL   Eur. J. Biochem. 234:251-257(1995).
RN   [5]
RP   PROTEIN SEQUENCE OF 27-32, PALMITOYLATION AT CYS-402 AND CYS-404,
RP   PHOSPHORYLATION AT SER-304; SER-418; TYR-438; SER-439; SER-440 AND SER-441,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lung;
RX   PubMed=9422751; DOI=10.1074/jbc.273.2.924;
RA   Roos M., Soskic V., Poznanovic S., Godovac-Zimmermann J.;
RT   "Post-translational modifications of endothelin receptor B from bovine
RT   lungs analyzed by mass spectrometry.";
RL   J. Biol. Chem. 273:924-931(1998).
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   -!- PTM: It is not sure whether phosphorylation is on Ser-434 or Ser-435.
CC       {ECO:0000269|PubMed:9422751}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Endothelin receptor subfamily. EDNRB sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- CAUTION: N-terminal sequencing (PubMed:9422751) indicates the presence
CC       of a signal peptide but an unprocessed form where the signal sequence
CC       is not cleaved has also been detected (PubMed:8529649). It is unclear
CC       if this exists in vivo. {ECO:0000305|PubMed:8529649,
CC       ECO:0000305|PubMed:9422751}.
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DR   EMBL; D10994; BAA01762.1; -; Genomic_DNA.
DR   EMBL; D90456; BAA14422.1; -; mRNA.
DR   EMBL; BC120256; AAI20257.1; -; mRNA.
DR   PIR; A41591; A41591.
DR   RefSeq; NP_776734.1; NM_174309.2.
DR   RefSeq; XP_005213931.1; XM_005213874.3.
DR   AlphaFoldDB; P28088; -.
DR   SMR; P28088; -.
DR   STRING; 9913.ENSBTAP00000006979; -.
DR   BindingDB; P28088; -.
DR   ChEMBL; CHEMBL4401; -.
DR   iPTMnet; P28088; -.
DR   SwissPalm; P28088; -.
DR   PaxDb; 9913-ENSBTAP00000006979; -.
DR   Ensembl; ENSBTAT00000006979.4; ENSBTAP00000006979.3; ENSBTAG00000005299.5.
DR   Ensembl; ENSBTAT00000070002.1; ENSBTAP00000064163.1; ENSBTAG00000005299.5.
DR   GeneID; 281750; -.
DR   KEGG; bta:281750; -.
DR   CTD; 1910; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005299; -.
DR   VGNC; VGNC:28330; EDNRB.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263512; -.
DR   HOGENOM; CLU_009579_28_0_1; -.
DR   InParanoid; P28088; -.
DR   OMA; YDQSDPN; -.
DR   OrthoDB; 2905228at2759; -.
DR   TreeFam; TF331292; -.
DR   Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-BTA-416476; G alpha (q) signalling events.
DR   PRO; PR:P28088; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000005299; Expressed in pigment epithelium of eye and 98 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004962; F:endothelin receptor activity; ISS:UniProtKB.
DR   GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR   GO; GO:0032341; P:aldosterone metabolic process; IEA:Ensembl.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0160093; P:chordate pharynx development; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0035645; P:enteric smooth muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0030202; P:heparin metabolic process; IEA:Ensembl.
DR   GO; GO:0048246; P:macrophage chemotaxis; IEA:Ensembl.
DR   GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR   GO; GO:0014043; P:negative regulation of neuron maturation; IEA:Ensembl.
DR   GO; GO:0051248; P:negative regulation of protein metabolic process; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR   GO; GO:0097402; P:neuroblast migration; IEA:Ensembl.
DR   GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
DR   GO; GO:0072112; P:podocyte differentiation; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0007497; P:posterior midgut development; IEA:Ensembl.
DR   GO; GO:0071806; P:protein transmembrane transport; IEA:Ensembl.
DR   GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR   GO; GO:0006885; P:regulation of pH; IEA:Ensembl.
DR   GO; GO:0097018; P:renal albumin absorption; IEA:Ensembl.
DR   GO; GO:0035812; P:renal sodium excretion; IEA:Ensembl.
DR   GO; GO:0070294; P:renal sodium ion absorption; IEA:Ensembl.
DR   GO; GO:0002001; P:renin secretion into blood stream; IEA:Ensembl.
DR   GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR   GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl.
DR   GO; GO:0042310; P:vasoconstriction; IBA:GO_Central.
DR   GO; GO:0014826; P:vein smooth muscle contraction; IEA:Ensembl.
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   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:1660473,
FT                   ECO:0000269|PubMed:9422751"
FT   CHAIN           27..441
FT                   /note="Endothelin receptor type B"
FT                   /id="PRO_0000012726"
FT   TOPO_DOM        27..100
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..125
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..162
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..196
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..242
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..295
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..323
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..349
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        350..361
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..388
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          30..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         438
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   LIPID           402
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   LIPID           404
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:9422751"
FT   DISULFID        173..254
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   441 AA;  49371 MW;  F634462C544DB0D2 CRC64;
     MQPLPSLCGR ALVALILACG VAGIQAEERE FPPAGATQPL PGTGEMMETP TETSWPGRSN
     ASDPRSSATP QIPRGGRMAG IPPRTPPPCD GPIEIKETFK YINTVVSCLV FVLGIIGNST
     LLRIIYKNKC MRNGPNILIA SLALGDLLHI IIDIPINTYK LLAKDWPFGV EMCKLVPFIQ
     KASVGITVLS LCALSIDRYR AVASWSRIKG IGVPKWTAVE IVLIWVVSVV LAVPEAVGFD
     IITSDHIGNK LRICLLHPTQ KTAFMQFYKT AKDWWLFSFY FCLPLAITAL FYTLMTCEML
     RKKSGMQIAL NDHLKQRREV AKTVFCLVLV FALCWLPLHL SRILKLTLYD QHDPRRCEFL
     SFLLVLDYIG INMASLNSCI NPIALYLVSK RFKNCFKSCL CCWCQSFEEK QSLEEKQSCL
     KFKANDHGYD NFRSSNKYSS S
//