EDNRB_PIG
ID EDNRB_PIG Reviewed; 443 AA.
AC P35463; Q2WG87;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1312214;
RA Elshourbagy N.A., Lee J.A., Korman D.R., Nuthalaganti P., Sylvester D.R.,
RA Dilella A.G., Sutiphong J.A., Kumar C.S.;
RT "Molecular cloning and characterization of the major endothelin receptor
RT subtype in porcine cerebellum.";
RL Mol. Pharmacol. 41:465-473(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-64.
RC TISSUE=Kidney;
RX PubMed=16441305; DOI=10.1111/j.1365-2052.2005.01404.x;
RA Okumura N., Hayashi T., Sekikawa H., Matsumoto T., Mikawa A., Hamasima N.,
RA Awata T.;
RT "Sequencing, mapping and nucleotide variation of porcine coat color genes
RT EDNRB, MYO5A, KITLG, SLC45A2, RAB27A, SILV and MITF.";
RL Anim. Genet. 37:80-82(2006).
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 -!- 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; AB209953; BAE48719.1; -; mRNA.
DR RefSeq; NP_001033091.1; NM_001038002.1.
DR RefSeq; XP_005668533.1; XM_005668476.2.
DR AlphaFoldDB; P35463; -.
DR SMR; P35463; -.
DR STRING; 9823.ENSSSCP00000010120; -.
DR BindingDB; P35463; -.
DR ChEMBL; CHEMBL3949; -.
DR PaxDb; P35463; -.
DR PRIDE; P35463; -.
DR Ensembl; ENSSSCT00000010390; ENSSSCP00000010120; ENSSSCG00000009477.
DR Ensembl; ENSSSCT00015084214; ENSSSCP00015034133; ENSSSCG00015062748.
DR Ensembl; ENSSSCT00025007250; ENSSSCP00025002976; ENSSSCG00025005370.
DR Ensembl; ENSSSCT00035021243; ENSSSCP00035007683; ENSSSCG00035016595.
DR Ensembl; ENSSSCT00045059994; ENSSSCP00045042119; ENSSSCG00045034860.
DR Ensembl; ENSSSCT00050090066; ENSSSCP00050038678; ENSSSCG00050066108.
DR Ensembl; ENSSSCT00055049549; ENSSSCP00055039603; ENSSSCG00055025001.
DR Ensembl; ENSSSCT00060038177; ENSSSCP00060016229; ENSSSCG00060028213.
DR Ensembl; ENSSSCT00065082193; ENSSSCP00065035791; ENSSSCG00065060011.
DR Ensembl; ENSSSCT00070042107; ENSSSCP00070035384; ENSSSCG00070021181.
DR GeneID; 414911; -.
DR KEGG; ssc:414911; -.
DR CTD; 1910; -.
DR VGNC; VGNC:87550; EDNRB.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_28_0_1; -.
DR InParanoid; P35463; -.
DR OMA; GFDMITT; -.
DR OrthoDB; 876925at2759; -.
DR TreeFam; TF331292; -.
DR Reactome; R-SSC-375276; Peptide ligand-binding receptors.
DR Reactome; R-SSC-416476; G alpha (q) signalling events.
DR PRO; PR:P35463; -.
DR Proteomes; UP000008227; Chromosome 11.
DR Proteomes; UP000314985; Chromosome 11.
DR Bgee; ENSSSCG00000009477; Expressed in cerebellum and 40 other tissues.
DR ExpressionAtlas; P35463; baseline and differential.
DR Genevisible; P35463; SS.
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 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:0000250"
FT CHAIN 27..443
FT /note="Endothelin receptor type B"
FT /id="PRO_0000012731"
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 53..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
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 CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 175..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 64
FT /note="P -> S"
FT /evidence="ECO:0000269|PubMed:16441305"
SQ SEQUENCE 443 AA; 49595 MW; C3B066743990A3C7 CRC64;
MQPLRSLCGR ALVALIFACG VAGVQSEERG FPPAGATPPA LRTGEIVAPP TKTFWPRGSN
ASLPRSSSPP QMPKGGRMAG PPARTLTPPP CEGPIEIKDT FKYINTVVSC LVFVLGIIGN
STLLRIIYKN KCMRNGPNIL IASLALGDLL HIIIDIPINV YKLLAEDWPF GVEMCKLVPF
IQKASVGITV LSLCALSIDR YRAVASWSRI KGIGVPKWTA VEIVLIWVVS VVLAVPEALG
FDMITTDYKG NRLRICLLHP TQKTAFMQFY KTAKDWWLFS FYFCLPLAIT AFFYTLMTCE
MLRKKSGMQI ALNDHLKQRR EVAKTVFCLV LVFALCWLPL HLSRILKLTL YDQNDSNRCE
LLSFLLVLDY IGINMASLNS CINPIALYLV SKRFKNCFKS CLCCWCQSFE EKQSLEEKQS
CLKFKANDHG YDNFRSSNKY SSS
