EDNRB_CANLF
ID EDNRB_CANLF Reviewed; 442 AA.
AC P56497; Q5KSU8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 115.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tsukui T., Yasuda N., Maeda S., Koyanagi M., Hashimoto R., Masuda K.,
RA Ohno K., Sakaguchi M., Tsujimoto H., Iwabuchi S.;
RT "Expression analysis of endothelin receptor type B gene in canine atopic
RT dermatitis.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-426.
RA Zemke D., Yuzbasiyan-Gurkan V.;
RL Submitted (JUL-1998) 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.
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; AB183285; BAD83850.1; -; mRNA.
DR EMBL; AF034530; AAC26970.1; -; mRNA.
DR RefSeq; NP_001010943.2; NM_001010943.2.
DR AlphaFoldDB; P56497; -.
DR SMR; P56497; -.
DR STRING; 9615.ENSCAFP00000007760; -.
DR GeneID; 403862; -.
DR KEGG; cfa:403862; -.
DR CTD; 1910; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P56497; -.
DR OrthoDB; 876925at2759; -.
DR Proteomes; UP000002254; 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 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_0000012727"
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 69..88
FT /note="Disordered"
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 59
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; 49722 MW; 3E9EE7AE581D7E15 CRC64;
MQPPPSLCGR ALVALVLACG LSRIWGEERG FPPDRATPLL QTAEIMTPPT KTLWPKGSNA
SLARSLAPAE VPKGDRTAGS PPRTISPPPC EGSIEIKETF KYINTVVSCL VFVLGIIGNS
TLLRIIYKNK CMRNGPNILI ASLALGDLLH IIIDIPITVY KLLAEDWPFG VEMCKLVPFI
QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAVGF
DMITIDYKGR YLRICLLHPT QKTAFMQFYK TAKDWWLFSF YFCLPLAITA FFYTLMTCEM
LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTIY DQNDPNRCEL
LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQSFEE KQSLEEKQSC
LKFKANDHGY DNFRSSNKYS SS
