EDNRB_MOUSE
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 03-AUG-2022, entry version 166.
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_001136061.2.
DR RefSeq; NP_001263225.1; NM_001276296.1.
DR RefSeq; NP_031930.1; NM_007904.4.
DR RefSeq; XP_006518578.1; XM_006518515.2.
DR AlphaFoldDB; P48302; -.
DR SMR; P48302; -.
DR STRING; 10090.ENSMUSP00000126057; -.
DR BindingDB; P48302; -.
DR ChEMBL; CHEMBL1681617; -.
DR GlyGen; P48302; 1 site.
DR iPTMnet; P48302; -.
DR PhosphoSitePlus; P48302; -.
DR SwissPalm; P48302; -.
DR MaxQB; P48302; -.
DR PaxDb; P48302; -.
DR PRIDE; P48302; -.
DR ProteomicsDB; 277798; -.
DR Antibodypedia; 4509; 475 antibodies from 39 providers.
DR DNASU; 13618; -.
DR Ensembl; ENSMUST00000022718; ENSMUSP00000022718; ENSMUSG00000022122.
DR Ensembl; ENSMUST00000172237; ENSMUSP00000126057; ENSMUSG00000022122.
DR Ensembl; ENSMUST00000227824; ENSMUSP00000154806; ENSMUSG00000022122.
DR GeneID; 13618; -.
DR KEGG; mmu:13618; -.
DR UCSC; uc007uww.3; mouse.
DR CTD; 1910; -.
DR MGI; MGI:102720; Ednrb.
DR VEuPathDB; HostDB:ENSMUSG00000022122; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_28_0_1; -.
DR InParanoid; P48302; -.
DR OMA; GFDMITT; -.
DR OrthoDB; 876925at2759; -.
DR PhylomeDB; P48302; -.
DR TreeFam; TF331292; -.
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 72 CRISPR screens.
DR ChiTaRS; Ednrb; mouse.
DR PRO; PR:P48302; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P48302; protein.
DR Bgee; ENSMUSG00000022122; Expressed in iris and 272 other tissues.
DR Genevisible; P48302; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
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:MGI.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
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:0019934; P:cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; IGI: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:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; IDA:MGI.
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 metabolic process; IGI:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0048246; P:macrophage chemotaxis; ISO:MGI.
DR GO; GO:0030318; P:melanocyte differentiation; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
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:MGI.
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:0097402; P:neuroblast migration; IMP:MGI.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR GO; GO:0060465; P:pharynx development; IDA:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0072112; P:podocyte differentiation; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0035810; P:positive regulation of urine volume; ISO:MGI.
DR GO; GO:0007497; P:posterior midgut development; IMP:MGI.
DR GO; GO:0071806; P:protein transmembrane transport; IDA:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0031620; P:regulation of fever generation; ISO:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0006885; P:regulation of pH; IMP:MGI.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0097018; P:renal albumin absorption; IGI:MGI.
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:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IGI:MGI.
DR GO; GO:0048265; P:response to pain; ISO:MGI.
DR GO; GO:1904383; P:response to sodium phosphate; IMP:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR GO; GO:0055078; P:sodium ion homeostasis; IGI:MGI.
DR GO; GO:0042310; P:vasoconstriction; ISO:MGI.
DR GO; GO:0042311; P:vasodilation; ISO:MGI.
DR GO; GO:0014826; P:vein smooth muscle contraction; ISO:MGI.
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 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..68
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