ID   EDNRB_MOUSE             Reviewed;         442 AA.
AC   P48302; Q542M3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 185.
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|MGI:MGI:102720};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8001159; DOI=10.1016/0092-8674(94)90017-5;
RA   Hosoda K., Hammer R.E., Richardson J.A., Baynash A.G., Cheung J.C.,
RA   Giaid A., Yanagisawa M.;
RT   "Targeted and natural (piebald-lethal) mutations of endothelin-B receptor
RT   gene produce megacolon associated with spotted coat color in mice.";
RL   Cell 79:1267-1276(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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. Essential
CC       component in the normal development of two neuronal crest-derived cell
CC       lineages.
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; U32329; AAB60508.1; -; mRNA.
DR   EMBL; AK076426; BAC36337.1; -; mRNA.
DR   EMBL; AK082103; BAC38409.1; -; mRNA.
DR   EMBL; AK083415; BAC38908.1; -; mRNA.
DR   EMBL; AK085532; BAC39465.1; -; mRNA.
DR   EMBL; BC026553; AAH26553.1; -; mRNA.
DR   CCDS; CCDS27317.1; -.
DR   RefSeq; NP_001129533.1; NM_001136061.3.
DR   RefSeq; NP_001263225.1; NM_001276296.2.
DR   RefSeq; NP_001409100.1; NM_001422171.1.
DR   RefSeq; NP_031930.1; NM_007904.5.
DR   AlphaFoldDB; P48302; -.
DR   SMR; P48302; -.
DR   FunCoup; P48302; 1339.
DR   STRING; 10090.ENSMUSP00000022718; -.
DR   BindingDB; P48302; -.
DR   ChEMBL; CHEMBL1681617; -.
DR   GlyCosmos; P48302; 1 site, No reported glycans.
DR   GlyGen; P48302; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; P48302; -.
DR   PhosphoSitePlus; P48302; -.
DR   SwissPalm; P48302; -.
DR   PaxDb; 10090-ENSMUSP00000022718; -.
DR   ProteomicsDB; 277798; -.
DR   Antibodypedia; 4509; 484 antibodies from 40 providers.
DR   DNASU; 13618; -.
DR   Ensembl; ENSMUST00000022718.11; ENSMUSP00000022718.4; ENSMUSG00000022122.16.
DR   Ensembl; ENSMUST00000172237.2; ENSMUSP00000126057.2; ENSMUSG00000022122.16.
DR   Ensembl; ENSMUST00000227824.2; ENSMUSP00000154806.2; ENSMUSG00000022122.16.
DR   GeneID; 13618; -.
DR   KEGG; mmu:13618; -.
DR   UCSC; uc007uww.3; mouse.
DR   AGR; MGI:102720; -.
DR   CTD; 1910; -.
DR   MGI; MGI:102720; Ednrb.
DR   VEuPathDB; HostDB:ENSMUSG00000022122; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01150000286932; -.
DR   HOGENOM; CLU_009579_28_0_1; -.
DR   InParanoid; P48302; -.
DR   OMA; YDQSDPN; -.
DR   OrthoDB; 10037617at2759; -.
DR   PhylomeDB; P48302; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 13618; 5 hits in 77 CRISPR screens.
DR   PRO; PR:P48302; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P48302; protein.
DR   Bgee; ENSMUSG00000022122; Expressed in iris and 274 other cell types or tissues.
DR   GO; GO:0031965; C:nuclear membrane; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004962; F:endothelin receptor activity; IDA:MGI.
DR   GO; GO:0017046; F:peptide hormone binding; ISO:GO_Central.
DR   GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:GO_Central.
DR   GO; GO:0032341; P:aldosterone metabolic process; IMP:MGI.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IDA:MGI.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISO:GO_Central.
DR   GO; GO:0160093; P:chordate pharynx development; IDA:MGI.
DR   GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0048484; P:enteric nervous system development; IDA:BHF-UCL.
DR   GO; GO:0035645; P:enteric smooth muscle cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0042045; P:epithelial fluid transport; ISO:GO_Central.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IEA:UniProtKB-ARBA.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0030202; P:heparin proteoglycan metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0048246; P:macrophage chemotaxis; ISO:GO_Central.
DR   GO; GO:0030318; P:melanocyte differentiation; IDA:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:GO_Central.
DR   GO; GO:0014043; P:negative regulation of neuron maturation; IDA:BHF-UCL.
DR   GO; GO:0051248; P:negative regulation of protein metabolic process; ISO:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0072112; P:podocyte differentiation; IEA:UniProtKB-ARBA.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:GO_Central.
DR   GO; GO:0060406; P:positive regulation of penile erection; ISO:GO_Central.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:GO_Central.
DR   GO; GO:0035810; P:positive regulation of urine volume; ISO:GO_Central.
DR   GO; GO:0007497; P:posterior midgut development; IMP:MGI.
DR   GO; GO:0071806; P:protein transmembrane transport; IEA:UniProtKB-ARBA.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; ISO:GO_Central.
DR   GO; GO:0031620; P:regulation of fever generation; ISO:GO_Central.
DR   GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR   GO; GO:0006885; P:regulation of pH; IMP:MGI.
DR   GO; GO:0097018; P:renal albumin absorption; IEA:UniProtKB-ARBA.
DR   GO; GO:0035812; P:renal sodium excretion; IMP:MGI.
DR   GO; GO:0070294; P:renal sodium ion absorption; IMP:MGI.
DR   GO; GO:0002001; P:renin secretion into blood stream; IMP:MGI.
DR   GO; GO:1990839; P:response to endothelin; ISO:GO_Central.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:GO_Central.
DR   GO; GO:0048265; P:response to pain; ISO:GO_Central.
DR   GO; GO:1904383; P:response to sodium phosphate; IMP:MGI.
DR   GO; GO:0055078; P:sodium ion homeostasis; IGI:MGI.
DR   GO; GO:0042310; P:vasoconstriction; ISO:GO_Central.
DR   GO; GO:0042311; P:vasodilation; ISO:GO_Central.
DR   GO; GO:0014826; P:vein smooth muscle contraction; ISO:GO_Central.
DR   CDD; cd15976; 7tmA_ET-BR; 1.
DR   FunFam; 1.20.1070.10:FF:000076; Endothelin receptor type B; 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; IPR051193; GPCR_endothelin_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_0000012730"
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          50..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..65
FT                   /note="Polar residues"
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        60
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;  49561 MW;  ED28A676F854B3D1 CRC64;
     MQSPASRCGR ALVALLLACG FLGVWGEKRG FPPAQATLSL LGTKEVMTPP TKTSWTRGSN
     SSLMRSSAPA EVTKGGRGAG VPPRSFPPPC QRNIEISKTF KYINTIVSCL VFVLGIIGNS
     TLLRIIYKNK CMRNGPNILI ASLALGDLLH IIIDIPINTY KLLAEDWPFG AEMCKLVPFI
     QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF
     DMITSDYKGK PLRVCMLNPF QKTAFMQFYK TAKDWWLFSF YFCLPLAITA VFYTLMTCEM
     LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTLY DQSNPHRCEL
     LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQTFEE KQSLEEKQSC
     LKFKANDHGY DNFRSSNKYS SS
//