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Endothelin receptor type B (ET-B) (ET-BR) (Endothelin receptor non-selective type)

 EDNRB_BOVIN             Reviewed;         441 AA.
P28088; Q0VCB3; Q9TSB9;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
30-AUG-2017, entry version 132.
RecName: Full=Endothelin receptor type B {ECO:0000305};
Short=ET-B;
Short=ET-BR;
AltName: Full=Endothelin receptor non-selective type;
Flags: Precursor;
Name=EDNRB;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN
SEQUENCE.
PubMed=1660473;
Saito Y., Mizuno T., Itakura M., Suzuki Y., Ito T., Hagiwara H.,
Hirose S.;
"Primary structure of bovine endothelin ETB receptor and
identification of signal peptidase and metal proteinase cleavage
sites.";
J. Biol. Chem. 266:23433-23437(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Thymus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 124-127; 262-269; 304-315; 417-421 AND 424-432.
TISSUE=Lung;
PubMed=1653249;
Kozuka M., Ito T., Hirose S., Lodhi K.M., Hagiwara H.;
"Purification and characterization of bovine lung endothelin
receptor.";
J. Biol. Chem. 266:16892-16896(1991).
[4]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Lung;
PubMed=8529649; DOI=10.1111/j.1432-1033.1995.251_c.x;
Hick S., Heidemann I., Soskic V., Muller-Esterl W.,
Godovac-Zimmermann J.;
"Isolation of the endothelin B receptor from bovine lung. Structure,
signal sequence, and binding site.";
Eur. J. Biochem. 234:251-257(1995).
[5]
PROTEIN SEQUENCE OF 27-32, PALMITOYLATION AT CYS-402 AND CYS-404,
PHOSPHORYLATION AT SER-304; SER-418; TYR-438; SER-439; SER-440 AND
SER-441, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lung;
PubMed=9422751; DOI=10.1074/jbc.273.2.924;
Roos M., Soskic V., Poznanovic S., Godovac-Zimmermann J.;
"Post-translational modifications of endothelin receptor B from bovine
lungs analyzed by mass spectrometry.";
J. Biol. Chem. 273:924-931(1998).
-!- FUNCTION: Non-specific receptor for endothelin 1, 2, and 3.
Mediates its action by association with G proteins that activate a
phosphatidylinositol-calcium second messenger system.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P24530}; Multi-pass membrane protein.
Note=internalized after activation by endothelins.
{ECO:0000250|UniProtKB:P24530}.
-!- PTM: It is not sure whether phosphorylation is on Ser-434 or Ser-
435. {ECO:0000269|PubMed:9422751}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Endothelin receptor subfamily. EDNRB sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- CAUTION: N-terminal sequencing (PubMed:9422751) indicates the
presence of a signal peptide but an unprocessed form where the
signal sequence is not cleaved has also been detected
(PubMed:8529649). It is unclear if this exists in vivo.
{ECO:0000305|PubMed:8529649, ECO:0000305|PubMed:9422751}.
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EMBL; D10994; BAA01762.1; -; Genomic_DNA.
EMBL; D90456; BAA14422.1; -; mRNA.
EMBL; BC120256; AAI20257.1; -; mRNA.
PIR; A41591; A41591.
RefSeq; NP_776734.1; NM_174309.2.
RefSeq; XP_005213931.1; XM_005213874.3.
UniGene; Bt.487; -.
ProteinModelPortal; P28088; -.
SMR; P28088; -.
STRING; 9913.ENSBTAP00000006979; -.
BindingDB; P28088; -.
ChEMBL; CHEMBL4401; -.
iPTMnet; P28088; -.
PaxDb; P28088; -.
PRIDE; P28088; -.
Ensembl; ENSBTAT00000006979; ENSBTAP00000006979; ENSBTAG00000005299.
GeneID; 281750; -.
KEGG; bta:281750; -.
CTD; 1910; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000119177; -.
HOGENOM; HOG000272623; -.
HOVERGEN; HBG051443; -.
InParanoid; P28088; -.
KO; K04198; -.
OMA; TAEIMTP; -.
OrthoDB; EOG091G0CJV; -.
TreeFam; TF331292; -.
Reactome; R-BTA-375276; Peptide ligand-binding receptors.
Reactome; R-BTA-416476; G alpha (q) signalling events.
PRO; PR:P28088; -.
Proteomes; UP000009136; Chromosome 12.
Bgee; ENSBTAG00000005299; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004962; F:endothelin receptor activity; ISS:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048484; P:enteric nervous system development; IEA:Ensembl.
GO; GO:0035645; P:enteric smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0048246; P:macrophage chemotaxis; IEA:Ensembl.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IEA:Ensembl.
GO; GO:0014043; P:negative regulation of neuron maturation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
GO; GO:0007497; P:posterior midgut development; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0006885; P:regulation of pH; IEA:Ensembl.
GO; GO:0014826; P:vein smooth muscle contraction; IEA:Ensembl.
InterPro; IPR000499; Endthln_rcpt.
InterPro; IPR001112; ETB_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00571; ENDOTHELINBR.
PRINTS; PR00366; ENDOTHELINR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; G-protein coupled receptor; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Reference proteome; Signal;
Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 26 {ECO:0000269|PubMed:1660473,
ECO:0000269|PubMed:9422751}.
CHAIN 27 441 Endothelin receptor type B.
/FTId=PRO_0000012726.
TOPO_DOM 27 100 Extracellular. {ECO:0000255}.
TRANSMEM 101 125 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 126 136 Cytoplasmic. {ECO:0000255}.
TRANSMEM 137 162 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 163 174 Extracellular. {ECO:0000255}.
TRANSMEM 175 196 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 197 217 Cytoplasmic. {ECO:0000255}.
TRANSMEM 218 242 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 243 270 Extracellular. {ECO:0000255}.
TRANSMEM 271 295 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 296 323 Cytoplasmic. {ECO:0000255}.
TRANSMEM 324 349 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 350 361 Extracellular. {ECO:0000255}.
TRANSMEM 362 388 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 389 441 Cytoplasmic. {ECO:0000255}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000269|PubMed:9422751}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000269|PubMed:9422751}.
MOD_RES 434 434 Phosphoserine. {ECO:0000305}.
MOD_RES 435 435 Phosphoserine. {ECO:0000305}.
MOD_RES 438 438 Phosphotyrosine.
{ECO:0000269|PubMed:9422751}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000269|PubMed:9422751}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000269|PubMed:9422751}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000269|PubMed:9422751}.
LIPID 402 402 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9422751}.
LIPID 404 404 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9422751}.
DISULFID 173 254 {ECO:0000255|PROSITE-ProRule:PRU00521}.
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


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