EDNRA_SHEEP
ID EDNRA_SHEEP Reviewed; 427 AA.
AC Q95L55;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Endothelin-1 receptor {ECO:0000305};
DE AltName: Full=Endothelin receptor type A {ECO:0000250|UniProtKB:P25101};
DE Short=ET-A;
DE Short=ET-AR;
DE Flags: Precursor;
GN Name=EDNRA {ECO:0000250|UniProtKB:P25101};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Linden B.C., Resnik E.R., Cornfield D.N.;
RT "Developmental regulation of pulmonary vascular endothelin A receptor.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for endothelin-1. Mediates its action by association
CC with G proteins that activate a phosphatidylinositol-calcium second
CC messenger system. The rank order of binding affinities for ET-A is: ET1
CC > ET2 >> ET3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HDAC7 and KAT5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Endothelin receptor subfamily. EDNRA sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF416703; AAL08564.1; -; mRNA.
DR RefSeq; NP_001009433.1; NM_001009433.1.
DR AlphaFoldDB; Q95L55; -.
DR SMR; Q95L55; -.
DR STRING; 9940.ENSOARP00000008763; -.
DR GeneID; 443465; -.
DR KEGG; oas:443465; -.
DR CTD; 1909; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 876925at2759; -.
DR Proteomes; UP000002356; Unplaced.
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; IPR002175; ETA_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00570; ENDOTHELINAR.
DR PRINTS; PR00366; ENDOTHELINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Membrane; Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..427
FT /note="Endothelin-1 receptor"
FT /id="PRO_0000012725"
FT TOPO_DOM 21..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..102
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..132
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..181
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..278
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..328
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..372
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 405..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 427 AA; 48510 MW; 1A8BA420E62D5F10 CRC64;
METFWLRVSF WVALVGGVIS DNPESYSTNL SIHVDSVTTF RGTELSFVVT THQPTNLALP
SNGSMHNYCP QQTKITSAFK YINTVISCTI FIVGMVGNAT LLRIIYQNKC MRNGPNALIA
SLALGDLIYV VIDLPINVFK LLAGRWPFEQ NDFGVFLCKL FPFLQKSSVG ITVLNLCALS
VDRYRAVASW SRVQGIGIPL VTAIEIVSIW ILSFILAIPE AIGFVMVPFE YKGAQHRTCM
LNATSKFMEF YQDVKDWWLF GFYFCMPLVC TAIFYTLMTC EMLNRRNGSL RIALSEHLKQ
RREVAKTVFC LVVIFALCWF PLHLSRILKK TVYDEMDTNR CELLSFLLLM DYIGINLATM
NSCINPIALY FVSKKFKNCF QSCLCCCCYQ SKSLMTSVPM NGTSIQWKNP EQNNHNTERS
SHKDSIN
