EDNRA_CANLF
ID EDNRA_CANLF Reviewed; 426 AA.
AC Q5KSU9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 88.
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 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 A gene in canine atopic
RT dermatitis.";
RL Submitted (MAR-2005) 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; AB183284; BAD83849.2; -; mRNA.
DR RefSeq; NP_001026802.1; NM_001031632.1.
DR AlphaFoldDB; Q5KSU9; -.
DR SMR; Q5KSU9; -.
DR STRING; 9615.ENSCAFP00000011497; -.
DR PaxDb; Q5KSU9; -.
DR PRIDE; Q5KSU9; -.
DR GeneID; 450187; -.
DR KEGG; cfa:450187; -.
DR CTD; 1909; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q5KSU9; -.
DR Proteomes; UP000002254; 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..426
FT /note="Endothelin-1 receptor"
FT /id="PRO_0000012720"
FT TOPO_DOM 21..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..101
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..131
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..180
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..228
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..277
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..327
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..371
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28088"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 426 AA; 48566 MW; F6D3AD47C39B9064 CRC64;
METFCLKVTF WVALVGYVIG DHPESYSTNL STPVDFTTFH GTELSFLVTT HRPTNLALPS
NGSMHSYCPQ QTKITSAFKY INTVISCTIF IVGMVGNATL LRIIYQNKCM RNGPNALIAS
LALGDLIYVV IDLPINVFKL LAGRWPFDHN DFGVFLCKLF PFLQKSSVGI TVLNLCALSV
DRYRAVASWS RVQGIGIPLI TAIEIVSIWI LSFILAIPEA IGFVMVPFEY KGEQHKTCML
NATSKFMEFY QDVKDWWLFG FYFCMPLVCT AIFYTLMTCE MLNRRNGSLR IALSEHLKQR
REVAKTVFCL VVIFALCWFP LHLSRILKKT VYDEMDKNRC ELLSFLRLMD YIGINLATMN
SCINPIALYF VSKKFKNCFQ SCLCCCCYQS KSLMTSVPMN GTSIQWKNHE QNNHNTERSS
HKDSIN
