EDNRB_BOVIN
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 03-AUG-2022, entry version 151.
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; P28088; -.
DR PRIDE; P28088; -.
DR Ensembl; ENSBTAT00000006979; ENSBTAP00000006979; ENSBTAG00000005299.
DR Ensembl; ENSBTAT00000070002; ENSBTAP00000064163; ENSBTAG00000005299.
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; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_28_0_1; -.
DR InParanoid; P28088; -.
DR OMA; GFDMITT; -.
DR OrthoDB; 876925at2759; -.
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 tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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:0007249; P:I-kappaB kinase/NF-kappaB signaling; 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:0060465; P:pharynx development; IEA:Ensembl.
DR GO; GO:0072112; P:podocyte differentiation; 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 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 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
