EDNRB_RABIT
ID EDNRB_RABIT Reviewed; 441 AA.
AC Q9N0W7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 95.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang L., Wu Q., Yang N., Long Q., Wang X.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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; AF245469; AAF60366.1; -; mRNA.
DR RefSeq; NP_001076190.1; NM_001082721.1.
DR AlphaFoldDB; Q9N0W7; -.
DR SMR; Q9N0W7; -.
DR STRING; 9986.ENSOCUP00000015272; -.
DR ChEMBL; CHEMBL2259248; -.
DR PRIDE; Q9N0W7; -.
DR GeneID; 100009477; -.
DR KEGG; ocu:100009477; -.
DR CTD; 1910; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9N0W7; -.
DR OrthoDB; 876925at2759; -.
DR Proteomes; UP000001811; 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: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; IEA:InterPro.
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..441
FT /note="Endothelin receptor type B"
FT /id="PRO_0000012732"
FT TOPO_DOM 27..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..125
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..162
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..196
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..242
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..295
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..349
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..388
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 30..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT MOD_RES 438
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT MOD_RES 439
FT /note="Phosphoserine"
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 LIPID 402
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 404
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 441 AA; 49441 MW; 059BF28017E02A19 CRC64;
MQPPPSLCGL ALLALVLACG MAEVWGEERE MPSAPATPPL LGASEILTPS TKTSWPRDSN
ASLPRSSAPA EIPKEGRTAG APRRTPPPCQ RPTEIKDTFK YINTVVSCLV FVLGIIGNST
LLRIIYKNKC MRNGPNILIA SLALGDLLHI IIDIPINVYK LLAEDWPFGA EMCKLVPFIQ
KASVGITVLS LCALSIDRYR AVASWSRIKG IGVPKWTAVE IVLIWVVSVI LAVPEAIGFN
LVTIDYKGSY LRICLLNPTQ KTAFMQFYKT AKDWWLFSFY FCLPLAITAF FYTLMTCEML
RKKSGMQIAL NDHLKQRREV AKTVFCLVLV FGLCWLALHL SRILKLTLYD QNDPNRCELL
SFLLVLDYIG INMASLNSCI NPIALYLVSK RFKNCFKSCL CCWCQSFEEK QSLEEKQSCL
KFKANDHGYD NFRSSNKYSS S
