ID EDNRB_RAT Reviewed; 442 AA. AC P21451; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 27-MAR-2024, entry version 167. 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 {ECO:0000312|RGD:2536}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=1312429; DOI=10.1210/endo.130.4.1312429; RA Hori S., Komatsu Y., Shigemoto R., Mizuno N., Nakanishi S.; RT "Distinct tissue distribution and cellular localization of two messenger RT ribonucleic acids encoding different subtypes of rat endothelin RT receptors."; RL Endocrinology 130:1885-1895(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=2175397; DOI=10.1038/348732a0; RA Sakurai T., Yanagisawa M., Takuwa Y., Miyazaki H., Kimura S., Goto K., RA Masaki T.; RT "Cloning of a cDNA encoding a non-isopeptide-selective subtype of the RT endothelin receptor."; RL Nature 348:732-735(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8371713; RA Cheng H.F., Su Y.M., Yeh J.R., Chang K.J.; RT "Alternative transcript of the nonselective-type endothelin receptor from RT rat brain."; RL Mol. Pharmacol. 44:533-538(1993). 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 -!- TISSUE SPECIFICITY: Widely distributed in cell types of a variety of CC tissues. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X57764; CAA40916.1; -; mRNA. DR EMBL; S65355; AAB28172.1; -; mRNA. DR PIR; S13425; S13425. DR RefSeq; NP_059029.1; NM_017333.1. DR RefSeq; XP_006252493.1; XM_006252431.3. DR RefSeq; XP_017455275.1; XM_017599786.1. DR AlphaFoldDB; P21451; -. DR SMR; P21451; -. DR STRING; 10116.ENSRNOP00000014747; -. DR BindingDB; P21451; -. DR ChEMBL; CHEMBL4631; -. DR DrugCentral; P21451; -. DR GuidetoPHARMACOLOGY; 220; -. DR GlyCosmos; P21451; 2 sites, No reported glycans. DR GlyGen; P21451; 2 sites. DR PhosphoSitePlus; P21451; -. DR PaxDb; 10116-ENSRNOP00000014747; -. DR Ensembl; ENSRNOT00000014747.6; ENSRNOP00000014747.4; ENSRNOG00000010997.6. DR Ensembl; ENSRNOT00055013494; ENSRNOP00055010815; ENSRNOG00055008002. DR Ensembl; ENSRNOT00060009647; ENSRNOP00060007253; ENSRNOG00060005817. DR Ensembl; ENSRNOT00065010267; ENSRNOP00065007500; ENSRNOG00065006642. DR GeneID; 50672; -. DR KEGG; rno:50672; -. DR UCSC; RGD:2536; rat. DR AGR; RGD:2536; -. DR CTD; 1910; -. DR RGD; 2536; Ednrb. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01100000263512; -. DR HOGENOM; CLU_009579_28_0_1; -. DR InParanoid; P21451; -. DR OMA; YDQSDPN; -. DR OrthoDB; 2905228at2759; -. DR PhylomeDB; P21451; -. DR Reactome; R-RNO-375276; Peptide ligand-binding receptors. DR Reactome; R-RNO-416476; G alpha (q) signalling events. DR PRO; PR:P21451; -. DR Proteomes; UP000002494; Chromosome 15. DR Bgee; ENSRNOG00000010997; Expressed in lung and 19 other cell types or tissues. DR GO; GO:0031965; C:nuclear membrane; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0004962; F:endothelin receptor activity; IDA:RGD. DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:RGD. DR GO; GO:0017046; F:peptide hormone binding; ISO:RGD. DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IPI:RGD. DR GO; GO:0032341; P:aldosterone metabolic process; ISO:RGD. DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD. DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB. DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD. DR GO; GO:0019934; P:cGMP-mediated signaling; IMP:RGD. DR GO; GO:0160093; P:chordate pharynx development; ISO:RGD. DR GO; GO:0048066; P:developmental pigmentation; ISO:RGD. DR GO; GO:0086100; P:endothelin receptor signaling pathway; ISO:RGD. DR GO; GO:0048484; P:enteric nervous system development; ISO:RGD. DR GO; GO:0035645; P:enteric smooth muscle cell differentiation; ISO:RGD. DR GO; GO:0042045; P:epithelial fluid transport; IMP:RGD. DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:RGD. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0010467; P:gene expression; ISO:RGD. DR GO; GO:0030202; P:heparin metabolic process; ISO:RGD. DR GO; GO:0048246; P:macrophage chemotaxis; ISO:RGD. DR GO; GO:0030318; P:melanocyte differentiation; IDA:RGD. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD. DR GO; GO:0014043; P:negative regulation of neuron maturation; ISO:RGD. DR GO; GO:0051248; P:negative regulation of protein metabolic process; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0001755; P:neural crest cell migration; ISO:RGD. DR GO; GO:0097402; P:neuroblast migration; ISO:RGD. DR GO; GO:0007422; P:peripheral nervous system development; ISO:RGD. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:RGD. DR GO; GO:0043473; P:pigmentation; IMP:RGD. DR GO; GO:0072112; P:podocyte differentiation; ISO:RGD. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD. DR GO; GO:0060406; P:positive regulation of penile erection; IMP:RGD. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD. DR GO; GO:0035810; P:positive regulation of urine volume; IMP:RGD. DR GO; GO:0007497; P:posterior midgut development; ISO:RGD. DR GO; GO:0071806; P:protein transmembrane transport; ISO:RGD. DR GO; GO:0008217; P:regulation of blood pressure; IMP:RGD. DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:RGD. DR GO; GO:0031620; P:regulation of fever generation; IMP:RGD. DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD. DR GO; GO:0006885; P:regulation of pH; ISO:RGD. DR GO; GO:0097018; P:renal albumin absorption; ISO:RGD. DR GO; GO:0035812; P:renal sodium excretion; ISO:RGD. DR GO; GO:0070294; P:renal sodium ion absorption; ISO:RGD. DR GO; GO:0002001; P:renin secretion into blood stream; ISO:RGD. DR GO; GO:1990839; P:response to endothelin; IMP:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:0010033; P:response to organic substance; ISO:RGD. DR GO; GO:0048265; P:response to pain; IMP:RGD. DR GO; GO:1904383; P:response to sodium phosphate; ISO:RGD. DR GO; GO:0055078; P:sodium ion homeostasis; ISO:RGD. DR GO; GO:0042310; P:vasoconstriction; IMP:RGD. DR GO; GO:0042311; P:vasodilation; IMP:RGD. DR GO; GO:0014826; P:vein smooth muscle contraction; ISO:RGD. 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. DR Genevisible; P21451; RN. 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_0000012733" 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 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 60 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 97 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 174..255 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 66..69 FT /note="SSAP -> FRT (in Ref. 2; CAA40916)" FT /evidence="ECO:0000305" SQ SEQUENCE 442 AA; 49455 MW; BDA628D78E8071CB CRC64; MQSSASRCGR ALVALLLACG LLGVWGEKRG FPPAQATPSL LGTKEVMTPP TKTSWTRGSN SSLMRSSAPA EVTKGGRVAG VPPRSFPPPC QRKIEINKTF KYINTIVSCL VFVLGIIGNS TLLRIIYKNK CMRNGPNILI ASLALGDLLH IIIDIPINAY KLLAGDWPFG AEMCKLVPFI QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF DVITSDYKGK PLRVCMLNPF QKTAFMQFYK TAKDWWLFSF YFCLPLAITA IFYTLMTCEM LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTLY DQSNPQRCEL LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQTFEE KQSLEEKQSC LKFKANDHGY DNFRSSNKYS SS //