EDNRB_HORSE
ID EDNRB_HORSE Reviewed; 443 AA.
AC O62709; O77508;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 117.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT OLWS LYS-126.
RC TISSUE=Liver;
RX PubMed=9580670; DOI=10.1093/hmg/7.6.1047;
RA Yang G.C., Croaker D., Zhang A.L., Manglick P., Cartmill T., Cass D.;
RT "A dinucleotide mutation in the endothelin-B receptor gene is associated
RT with lethal white foal syndrome (LWFS); a horse variant of Hirschsprung
RT disease.";
RL Hum. Mol. Genet. 7:1047-1052(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-443, AND VARIANT OLWS LYS-126.
RX PubMed=9530628; DOI=10.1007/s003359900754;
RA Santschi E.M., Purdy A.K., Valberg S.J., Vrotsos P.D., Kaese H.,
RA Mickelson J.R.;
RT "Endothelin receptor B polymorphism associated with lethal white foal
RT syndrome in horses.";
RL Mamm. Genome 9:306-309(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 -!- DISEASE: Note=Defects in EDNRB are a cause of overo lethal white
CC syndrome (OLWS) also known as lethal white foal syndrome (LWFS). It is
CC an inherited syndrome of foals born to American paint horse parents of
CC the overo coat-pattern lineage. Affected foals are totally or almost
CC totally white and die within days from complications due to intestinal
CC aganglionosis. {ECO:0000269|PubMed:9530628,
CC ECO:0000269|PubMed:9580670}.
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; AF019072; AAC25983.1; -; mRNA.
DR EMBL; AF038900; AAC23486.1; -; mRNA.
DR RefSeq; NP_001075306.2; NM_001081837.2.
DR AlphaFoldDB; O62709; -.
DR SMR; O62709; -.
DR STRING; 9796.ENSECAP00000037052; -.
DR PaxDb; O62709; -.
DR PRIDE; O62709; -.
DR GeneID; 100033875; -.
DR KEGG; ecb:100033875; -.
DR CTD; 1910; -.
DR InParanoid; O62709; -.
DR OrthoDB; 876925at2759; -.
DR Proteomes; UP000002281; Unplaced.
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:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
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:InterPro.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IBA:GO_Central.
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; Disease variant; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..443
FT /note="Endothelin receptor type B"
FT /id="PRO_0000012728"
FT TOPO_DOM 27..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..127
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..164
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..198
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..244
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..297
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..351
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..390
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 51..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT MOD_RES 440
FT /note="Phosphotyrosine"
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 MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT LIPID 403
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 404
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 406
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 175..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 126
FT /note="I -> K (in OLWS)"
FT /evidence="ECO:0000269|PubMed:9530628,
FT ECO:0000269|PubMed:9580670"
FT CONFLICT 11
FT /note="V -> A (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..44
FT /note="FE -> SG (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..66
FT /note="PRL -> QRS (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="A -> E (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="E -> D (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="E -> M (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="E -> D (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="W -> S (in Ref. 2; AAC23486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50006 MW; 74381DDFCF9A9AF4 CRC64;
MQPLPTLCGR VLVALILACG VAGVQGEERR FPPARATPPL LGFEEIMTPP TKTSWPTGSN
ASVPRLSAPP QMPKAGRTAG AQRRTLPPPP CERTIEIKET FKYINTVVSC LVFVLGIIGN
STLLRIIYKN KCMRNGPNIL IASLALGDLL HIIIDIPINV YKLLAEDWPF GVEMCKLVPF
IQKASVGITV LSLCALSIDR YRAVASWSRI KGIGVPKWTA VEIVLIWVVS VVLAVPEAVG
FDMITADYKG SYLRICLLHP TQKTAFMQFY KNAKDWWLFS FYFCLPLAIT AFFYTLETCE
MLRKKSGMQI ALNDHLKQRR EVAKTVFCLV LVFALCWLPL HLSRILKHTL YDQNDPHRCE
LLSFLLVLEY IGINMASLNS CINPIALYLV SKRFKNCFKW CLCCWCQSFE EKQSLEDKQS
CLKFKANDHG YDNFRSSNKY SSS
