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Database: UniProt
Entry: A5A8K3_RABIT
LinkDB: A5A8K3_RABIT
Original site: A5A8K3_RABIT 
ID   A5A8K3_RABIT            Unreviewed;       427 AA.
AC   A5A8K3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Endothelin-1 receptor {ECO:0000256|ARBA:ARBA00013809};
DE   AltName: Full=Endothelin receptor type A {ECO:0000256|ARBA:ARBA00030983};
GN   Name=ednrA {ECO:0000313|EMBL:BAF62262.1};
GN   Synonyms=EDNRA {ECO:0000313|Ensembl:ENSOCUP00000001082.2};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|EMBL:BAF62262.1};
RN   [1] {ECO:0000313|EMBL:BAF62262.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yomogida S.;
RT   "rabbit endothelin receptor type A, mRNA.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000001082.2, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000001082.2,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [3] {ECO:0000313|Ensembl:ENSOCUP00000001082.2}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001082.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025187}.
CC   -!- SUBUNIT: Interacts with HDAC7 and KAT5.
CC       {ECO:0000256|ARBA:ARBA00011811}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU000688}.
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DR   EMBL; AAGW02045813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02045814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02045815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB303551; BAF62262.1; -; mRNA.
DR   RefSeq; NP_001099144.1; NM_001105674.1.
DR   RefSeq; XP_008265496.1; XM_008267274.2.
DR   STRING; 9986.ENSOCUP00000001082; -.
DR   ChEMBL; CHEMBL1795104; -.
DR   PaxDb; 9986-ENSOCUP00000001082; -.
DR   Ensembl; ENSOCUT00000001249.4; ENSOCUP00000001082.2; ENSOCUG00000001250.4.
DR   GeneID; 100126073; -.
DR   KEGG; ocu:100126073; -.
DR   CTD; 1909; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263512; -.
DR   HOGENOM; CLU_009579_28_0_1; -.
DR   OMA; YNERDPG; -.
DR   OrthoDB; 2905228at2759; -.
DR   TreeFam; TF331292; -.
DR   Proteomes; UP000001811; Chromosome 15.
DR   Bgee; ENSOCUG00000001250; Expressed in heart and 14 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004962; F:endothelin receptor activity; IEA:Ensembl.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR   GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0003228; P:atrial cardiac muscle tissue development; IEA:Ensembl.
DR   GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR   GO; GO:0060385; P:axonogenesis involved in innervation; IEA:Ensembl.
DR   GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0003207; P:cardiac chamber formation; IEA:Ensembl.
DR   GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
DR   GO; GO:0044751; P:cellular response to human chorionic gonadotropin stimulus; IEA:Ensembl.
DR   GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
DR   GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
DR   GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR   GO; GO:0086101; P:endothelin receptor signaling pathway involved in heart process; IEA:Ensembl.
DR   GO; GO:0048484; P:enteric nervous system development; IEA:InterPro.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR   GO; GO:0060324; P:face development; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0072011; P:glomerular endothelium development; IEA:Ensembl.
DR   GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR   GO; GO:0030202; P:heparin metabolic process; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR   GO; GO:1903537; P:meiotic cell cycle process involved in oocyte maturation; IEA:Ensembl.
DR   GO; GO:0097152; P:mesenchymal cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0014034; P:neural crest cell fate commitment; IEA:Ensembl.
DR   GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR   GO; GO:0016322; P:neuron remodeling; IEA:Ensembl.
DR   GO; GO:0003357; P:noradrenergic neuron differentiation; IEA:Ensembl.
DR   GO; GO:0042415; P:norepinephrine metabolic process; IEA:Ensembl.
DR   GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IEA:Ensembl.
DR   GO; GO:1903210; P:podocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0072112; P:podocyte differentiation; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0010737; P:protein kinase A signaling; IEA:Ensembl.
DR   GO; GO:0071806; P:protein transmembrane transport; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0010827; P:regulation of glucose transmembrane transport; IEA:Ensembl.
DR   GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR   GO; GO:1905871; P:regulation of protein localization to cell leading edge; IEA:Ensembl.
DR   GO; GO:0097018; P:renal albumin absorption; IEA:Ensembl.
DR   GO; GO:0070294; P:renal sodium ion absorption; IEA:Ensembl.
DR   GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR   GO; GO:1905144; P:response to acetylcholine; IEA:Ensembl.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IEA:Ensembl.
DR   GO; GO:0055078; P:sodium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0048485; P:sympathetic nervous system development; IEA:Ensembl.
DR   GO; GO:0097492; P:sympathetic neuron axon guidance; IEA:Ensembl.
DR   GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
DR   GO; GO:0097084; P:vascular associated smooth muscle cell development; IEA:Ensembl.
DR   CDD; cd15975; 7tmA_ET-AR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000499; Endthln_rcpt.
DR   InterPro; IPR002175; ETA_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR46099:SF2; ENDOTHELIN-1 RECEPTOR; 1.
DR   PANTHER; PTHR46099; G_PROTEIN_RECEP_F1_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00570; ENDOTHELINAR.
DR   PRINTS; PR00366; ENDOTHELINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU000688};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..427
FT                   /note="Endothelin-1 receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015086476"
FT   TRANSMEM        81..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..369
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   REGION          406..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   427 AA;  48852 MW;  5C289E5BFBB945A8 CRC64;
     METFCLRASF WLVLIGCVIS DNPERYSTNL SNHMDEFTTF HGPELNLLVT THRPTNLVLP
     SNGSRHNYCP QQTKITSAFK YINTVISCTI FIVGMVGNAT LLRIIYQNKC MRNGPNALIA
     SLALGDLIYV VIDLPINVFK LLAGRWPFDH NDFGVFLCKL FPFLQKSSVG ITVLNLCALS
     VDRYRAVASW SRVQGIGIPL ITAIEIVSIW ILSFILAIPE AIGFVMVPFE YRGEQHKTCM
     LNATSKFMEF YQDVKDWWLF GFYFCMPLVC TAIFYTLMTC EMLNRRNGSL RIALSEHLKQ
     RREVAKTVFC LVVIFALCWF PLHLSRILKK TVYDEMDKNR CELLSFLLLM DYIGINLATM
     NSCINPIALY FVSKKFKNCF QSCLCCCCHQ SKSLMTSVPM NGTSIQWKNH DQNNHNTERS
     SHKDSIN
//
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