ID   EDNR3_XENLA             Reviewed;         444 AA.
AC   P32940;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Endothelin-3 receptor;
DE   AltName: Full=Endothelin C receptor;
DE            Short=ET-C;
DE            Short=ET-CR;
DE   Flags: Precursor;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Dermal melanophore;
RX   PubMed=8360195; DOI=10.1016/s0021-9258(17)46743-3;
RA   Karne S., Jayawickreme C.K., Lerner M.R.;
RT   "Cloning and characterization of an endothelin-3 specific receptor (ETC
RT   receptor) from Xenopus laevis dermal melanophores.";
RL   J. Biol. Chem. 268:19126-19133(1993).
CC   -!- FUNCTION: Receptor for endothelin-3. Mediates its action by association
CC       with G proteins that activate a phosphatidylinositol-calcium second
CC       messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Endothelin receptor subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; L20299; AAA49704.1; -; mRNA.
DR   PIR; A48538; A48538.
DR   RefSeq; NP_001079347.1; NM_001085878.1.
DR   AlphaFoldDB; P32940; -.
DR   SMR; P32940; -.
DR   GeneID; 378691; -.
DR   CTD; 1910; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004962; F:endothelin receptor activity; IEA:InterPro.
DR   GO; GO:0048484; P:enteric nervous system development; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
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; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00366; ENDOTHELINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..444
FT                   /note="Endothelin-3 receptor"
FT                   /id="PRO_0000012734"
FT   TOPO_DOM        19..88
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..113
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..161
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..180
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..226
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..254
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..279
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..365
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..444
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          416..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   444 AA;  50172 MW;  80AB7EC36720D783 CRC64;
     MATVILFVAW MACLMVGVCY QEFQTQQNFP DISNPSQELN QEPAHRIVQL DSIQNNGALN
     MSTGNVLNMS PPPPSPCLSR AKIRHAFKYV TTILSCVIFL VGIVGNSTLL RIIYKNKCMR
     NGPNVLIASL ALGDLFYILI AIPIISISFW LSTGHSEYIY QLVHLYRARV YSLSLCALSI
     DRYRAVASWN RIRSIGIPVR KAIELTLIWA VAIIVAVPEA IAFNLVELDF RGQTILVCML
     PMEQTSDFMR FYQEVKVWWL FGFYFCLPLA CTGVFYTLMS CEMLSIKNGM RIALNDHMKQ
     RREVAKTVFC LVVIFALCWL PLHVSSIFVR LSATVKRACI LKNKRSCIMA EIQTGVNYQL
     LMVMNYTGIN MASLNSCIGP VALYFVSRKF KNCFQSCLCC WCHRPTLTIT PMDEKGSGGK
     WKANGHDLDL DRSSSRLSNK YSSS