EDNRA_HUMAN
ID EDNRA_HUMAN Reviewed; 427 AA.
AC P25101; B2R723; B4E2V6; B7Z9G6; D3DP03; E7ER36; O43441; Q16432; Q16433;
AC Q8TBH2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Endothelin-1 receptor {ECO:0000305};
DE AltName: Full=Endothelin receptor type A {ECO:0000312|HGNC:HGNC:3179};
DE Short=ET-A;
DE Short=ETA-R;
DE Short=hET-AR;
DE Flags: Precursor;
GN Name=EDNRA {ECO:0000312|HGNC:HGNC:3179}; Synonyms=ETA, ETRA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1719979; DOI=10.1016/s0006-291x(05)81332-4;
RA Adachi M., Yang Y.Y., Furuichi Y., Miyamoto C.;
RT "Cloning and characterization of cDNA encoding human A-type endothelin
RT receptor.";
RL Biochem. Biophys. Res. Commun. 180:1265-1272(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1659806; DOI=10.1016/s0006-291x(05)81399-3;
RA Cyr C., Huebner K., Druck T., Kris R.;
RT "Cloning and chromosomal localization of a human endothelin ETA receptor.";
RL Biochem. Biophys. Res. Commun. 181:184-190(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1652463; DOI=10.1016/0014-5793(91)80007-p;
RA Hosoda K., Nakao K., Arai H., Suga S., Ogawa Y., Mukoyama M., Shirakami G.,
RA Saito Y., Nakanishi S., Imura H.;
RT "Cloning and expression of human endothelin-1 receptor cDNA.";
RL FEBS Lett. 287:23-26(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1291713; DOI=10.1253/jcj.56.supplementv_1303;
RA Arai H., Nakao K., Hosoda K., Ogawa Y., Nakagawa O., Komatsu Y., Imura H.;
RT "Molecular cloning of human endothelin receptors and their expression in
RT vascular endothelial cells and smooth muscle cells.";
RL Jpn. Circ. J. 56:1303-1307(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8440682; DOI=10.1016/s0021-9258(18)53554-7;
RA Elshourbagy N.A., Korman D.R., Wu H.L., Sylvester D.R., Lee J.A.,
RA Nuthalaganti P., Bergsma D.J., Kumar C.S., Nambi P.;
RT "Molecular characterization and regulation of the human endothelin
RT receptors.";
RL J. Biol. Chem. 268:3873-3879(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=1326535; DOI=10.1016/s0021-9258(19)37031-0;
RA Hosoda K., Nakao K., Tamura N., Arai H., Ogawa Y., Suga S., Nakanishi S.,
RA Imura H.;
RT "Organization, structure, chromosomal assignment, and expression of the
RT gene encoding the human endothelin-A receptor.";
RL J. Biol. Chem. 267:18797-18804(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1415318; DOI=10.1097/00000441-199210000-00002;
RA Hayzer D.J., Rose P.M., Lynch J.S., Webb M.L., Kienzle B.K., Liu E.C.,
RA Bogosian E.A., Brinson E., Runge M.S.;
RT "Cloning and expression of a human endothelin receptor: subtype A.";
RL Am. J. Med. Sci. 304:231-238(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=8611157; DOI=10.1042/bj3130795;
RA Miyamoto Y., Yoshimasa T., Arai H., Takaya K., Ogawa Y., Itoh H., Nakao K.;
RT "Alternative RNA splicing of the human endothelin-A receptor generates
RT multiple transcripts.";
RL Biochem. J. 313:795-801(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Cerebellum, Testis, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140 (ISOFORMS 1/2/3/4).
RX PubMed=8427579; DOI=10.1006/bbrc.1993.1052;
RA Yang H., Tabuchi H., Furuichi Y., Miyamoto C.;
RT "Molecular characterization of the 5'-flanking region of human genomic ETA
RT gene.";
RL Biochem. Biophys. Res. Commun. 190:332-339(1993).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-427 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=9284755; DOI=10.1210/jcem.82.9.4209;
RA Bourgeois C., Robert B., Rebourcet R., Mondon F., Mignot T.-M.,
RA Duc-Goiran P., Ferre F.;
RT "Endothelin-1 and ETA receptor expression in vascular smooth muscle cells
RT from human placenta: a new ETA receptor messenger ribonucleic acid is
RT generated by alternative splicing of exon 3.";
RL J. Clin. Endocrinol. Metab. 82:3116-3123(1997).
RN [17]
RP INTERACTION WITH HDAC7 AND KAT5.
RX PubMed=11262386; DOI=10.1074/jbc.c000909200;
RA Lee H.-J., Chun M., Kandror K.V.;
RT "Tip60 and HDAC7 interact with the endothelin receptor a and may be
RT involved in downstream signaling.";
RL J. Biol. Chem. 276:16597-16600(2001).
RN [18]
RP INVOLVEMENT IN MFDA, AND VARIANTS MFDA PHE-129 AND LYS-303.
RX PubMed=25772936; DOI=10.1016/j.ajhg.2015.01.015;
RA Gordon C.T., Weaver K.N., Zechi-Ceide R.M., Madsen E.C., Tavares A.L.,
RA Oufadem M., Kurihara Y., Adameyko I., Picard A., Breton S., Pierrot S.,
RA Biosse-Duplan M., Voisin N., Masson C., Bole-Feysot C., Nitschke P.,
RA Delrue M.A., Lacombe D., Guion-Almeida M.L., Moura P.P., Garib D.G.,
RA Munnich A., Ernfors P., Hufnagel R.B., Hopkin R.J., Kurihara H., Saal H.M.,
RA Weaver D.D., Katsanis N., Lyonnet S., Golzio C., Clouthier D.E., Amiel J.;
RT "Mutations in the endothelin receptor type A cause mandibulofacial
RT dysostosis with alopecia.";
RL Am. J. Hum. Genet. 96:519-531(2015).
RN [19]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-136.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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.
CC -!- SUBUNIT: Interacts with HDAC7 and KAT5. {ECO:0000269|PubMed:11262386}.
CC -!- INTERACTION:
CC P25101; P49407: ARRB1; NbExp=3; IntAct=EBI-6624559, EBI-743313;
CC P25101; P32121: ARRB2; NbExp=2; IntAct=EBI-6624559, EBI-714559;
CC P25101; P05305: EDN1; NbExp=2; IntAct=EBI-6624559, EBI-715181;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P25101-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta-3;
CC IsoId=P25101-2; Sequence=VSP_011059, VSP_011060;
CC Name=3; Synonyms=Delta-4;
CC IsoId=P25101-3; Sequence=VSP_011062, VSP_011063;
CC Name=4; Synonyms=Delta-3,4;
CC IsoId=P25101-4; Sequence=VSP_011061;
CC Name=5;
CC IsoId=P25101-5; Sequence=VSP_045578;
CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are expressed in
CC a variety of tissues, with highest levels in the aorta and cerebellum,
CC followed by lung, atrium and cerebral cortex, lower levels in the
CC placenta, kidney, adrenal gland, duodenum, colon, ventricle and liver
CC but no expression in umbilical vein endothelial cells. Within the
CC placenta, isoform 1, isoform 2, isoform 3 and isoform 4 are expressed
CC in the villi and stem villi vessels. {ECO:0000269|PubMed:8611157,
CC ECO:0000269|PubMed:9284755}.
CC -!- DISEASE: Mandibulofacial dysostosis with alopecia (MFDA) [MIM:616367]:
CC A form of mandibulofacial dysostosis, a disorder characterized by malar
CC and mandibular hypoplasia, typically associated with abnormalities of
CC the ears and eyelids. MFDA features include maxillary dysmorphism with
CC dysplastic zygomatic arch, hypoplastic mandible, scalp alopecia, scant
CC eyebrows and eyelashes, severe hypoplasia or aplasia of eyelids, small
CC cupped dysplastic ears, conductive hearing loss, cleft palate, dental
CC anomalies, micrognathia, and limited jaw mobility.
CC {ECO:0000269|PubMed:25772936}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Endothelin receptor subfamily. EDNRA sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ednra/";
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DR EMBL; S63938; AAB20278.1; -; mRNA.
DR EMBL; S67127; AAB20407.1; -; mRNA.
DR EMBL; X61950; CAA43953.1; -; mRNA.
DR EMBL; D90348; BAA14359.1; -; mRNA.
DR EMBL; S57498; AAB25530.2; -; mRNA.
DR EMBL; L06622; AAA58447.1; -; mRNA.
DR EMBL; D11151; BAA01920.1; -; Genomic_DNA.
DR EMBL; S45956; AAB23644.1; -; mRNA.
DR EMBL; S81539; AAB36325.1; -; mRNA.
DR EMBL; S81542; AAB36326.1; -; mRNA.
DR EMBL; S81545; AAB36327.1; -; mRNA.
DR EMBL; AY275462; AAP32294.1; -; mRNA.
DR EMBL; AY422989; AAQ87880.1; -; Genomic_DNA.
DR EMBL; AK304451; BAG65268.1; -; mRNA.
DR EMBL; AK312812; BAG35670.1; -; mRNA.
DR EMBL; AK315931; BAH14302.1; -; mRNA.
DR EMBL; AC093908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX05019.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05021.1; -; Genomic_DNA.
DR EMBL; BC022511; AAH22511.1; -; mRNA.
DR EMBL; S55772; AAB25212.1; -; Genomic_DNA.
DR EMBL; AF014826; AAB94859.1; -; mRNA.
DR CCDS; CCDS3769.1; -. [P25101-1]
DR CCDS; CCDS54810.1; -. [P25101-4]
DR PIR; A44158; A44158.
DR RefSeq; NP_001159527.1; NM_001166055.1. [P25101-4]
DR RefSeq; NP_001243212.1; NM_001256283.1.
DR RefSeq; NP_001948.1; NM_001957.3. [P25101-1]
DR AlphaFoldDB; P25101; -.
DR SMR; P25101; -.
DR BioGRID; 108231; 62.
DR CORUM; P25101; -.
DR DIP; DIP-48718N; -.
DR IntAct; P25101; 13.
DR STRING; 9606.ENSP00000315011; -.
DR BindingDB; P25101; -.
DR ChEMBL; CHEMBL252; -.
DR DrugBank; DB04674; 2-HYDROXY-3,5-DIIODOBENZOIC ACID.
DR DrugBank; DB00945; Acetylsalicylic acid.
DR DrugBank; DB05367; Actelion-1.
DR DrugBank; DB06403; Ambrisentan.
DR DrugBank; DB06199; Atrasentan.
DR DrugBank; DB00559; Bosentan.
DR DrugBank; DB06677; Clazosentan.
DR DrugBank; DB04883; Darusentan.
DR DrugBank; DB06460; Enrasentan.
DR DrugBank; DB08932; Macitentan.
DR DrugBank; DB06268; Sitaxentan.
DR DrugBank; DB12548; Sparsentan.
DR DrugBank; DB05290; SPP 301.
DR DrugBank; DB06558; Tezosentan.
DR DrugCentral; P25101; -.
DR GuidetoPHARMACOLOGY; 219; -.
DR GlyGen; P25101; 2 sites.
DR iPTMnet; P25101; -.
DR PhosphoSitePlus; P25101; -.
DR SwissPalm; P25101; -.
DR BioMuta; EDNRA; -.
DR DMDM; 119606; -.
DR jPOST; P25101; -.
DR MassIVE; P25101; -.
DR PaxDb; P25101; -.
DR PeptideAtlas; P25101; -.
DR PRIDE; P25101; -.
DR ProteomicsDB; 17708; -.
DR ProteomicsDB; 54256; -. [P25101-1]
DR ProteomicsDB; 54258; -. [P25101-3]
DR ProteomicsDB; 54259; -. [P25101-4]
DR Antibodypedia; 2942; 356 antibodies from 34 providers.
DR DNASU; 1909; -.
DR Ensembl; ENST00000324300.10; ENSP00000315011.5; ENSG00000151617.17. [P25101-1]
DR Ensembl; ENST00000358556.8; ENSP00000351359.4; ENSG00000151617.17. [P25101-4]
DR Ensembl; ENST00000506066.1; ENSP00000425281.1; ENSG00000151617.17. [P25101-4]
DR Ensembl; ENST00000510697.5; ENSP00000427259.1; ENSG00000151617.17. [P25101-3]
DR Ensembl; ENST00000511804.5; ENSP00000425354.1; ENSG00000151617.17. [P25101-5]
DR Ensembl; ENST00000648866.1; ENSP00000496976.1; ENSG00000151617.17. [P25101-5]
DR Ensembl; ENST00000651419.1; ENSP00000498969.1; ENSG00000151617.17. [P25101-1]
DR GeneID; 1909; -.
DR KEGG; hsa:1909; -.
DR MANE-Select; ENST00000651419.1; ENSP00000498969.1; NM_001957.4; NP_001948.1.
DR UCSC; uc003iky.4; human. [P25101-1]
DR CTD; 1909; -.
DR DisGeNET; 1909; -.
DR GeneCards; EDNRA; -.
DR HGNC; HGNC:3179; EDNRA.
DR HPA; ENSG00000151617; Tissue enhanced (seminal).
DR MalaCards; EDNRA; -.
DR MIM; 131243; gene.
DR MIM; 616367; phenotype.
DR neXtProt; NX_P25101; -.
DR OpenTargets; ENSG00000151617; -.
DR Orphanet; 586; Cystic fibrosis.
DR Orphanet; 443995; Mandibulofacial dysostosis with alopecia.
DR PharmGKB; PA27617; -.
DR VEuPathDB; HostDB:ENSG00000151617; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_096205_1_0_1; -.
DR InParanoid; P25101; -.
DR OMA; QFLCKFL; -.
DR OrthoDB; 876925at2759; -.
DR PhylomeDB; P25101; -.
DR TreeFam; TF331292; -.
DR PathwayCommons; P25101; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P25101; -.
DR SIGNOR; P25101; -.
DR BioGRID-ORCS; 1909; 7 hits in 1070 CRISPR screens.
DR ChiTaRS; EDNRA; human.
DR GeneWiki; Endothelin_receptor_type_A; -.
DR GenomeRNAi; 1909; -.
DR Pharos; P25101; Tclin.
DR PRO; PR:P25101; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P25101; protein.
DR Bgee; ENSG00000151617; Expressed in cauda epididymis and 185 other tissues.
DR Genevisible; P25101; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004962; F:endothelin receptor activity; IBA:GO_Central.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; TAS:ProtInc.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0007202; P:activation of phospholipase C activity; TAS:ProtInc.
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; IMP:BHF-UCL.
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:0008283; P:cell population proliferation; TAS:ProtInc.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
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:0048066; P:developmental pigmentation; IBA:GO_Central.
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:0086100; P:endothelin receptor signaling pathway; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; NAS:UniProtKB.
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:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; 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:0010259; P:multicellular organism aging; 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:2001259; P:positive regulation of cation channel activity; IDA:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR GO; GO:0010737; P:protein kinase A signaling; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; 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; ISS:UniProtKB.
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:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006939; P:smooth muscle contraction; TAS:ProtInc.
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 GO; GO:0042310; P:vasoconstriction; IMP:BHF-UCL.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Hypotrichosis; Membrane;
KW 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_0000012721"
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 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"
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"
FT VAR_SEQ 1..225
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045578"
FT VAR_SEQ 141..249
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8611157"
FT /id="VSP_011061"
FT VAR_SEQ 141..161
FT /note="LLAGRWPFDHNDFGVFLCKLF -> VQSSCLLESCSGNWDSFGNCH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9284755"
FT /id="VSP_011059"
FT VAR_SEQ 162..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9284755"
FT /id="VSP_011060"
FT VAR_SEQ 183..187
FT /note="RYRAV -> SSTKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8611157"
FT /id="VSP_011062"
FT VAR_SEQ 188..427
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8611157"
FT /id="VSP_011063"
FT VARIANT 129
FT /note="Y -> F (in MFDA; dbSNP:rs786205230)"
FT /evidence="ECO:0000269|PubMed:25772936"
FT /id="VAR_073788"
FT VARIANT 136
FT /note="I -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035758"
FT VARIANT 303
FT /note="E -> K (in MFDA; dbSNP:rs876657388)"
FT /evidence="ECO:0000269|PubMed:25772936"
FT /id="VAR_073789"
FT CONFLICT 110
FT /note="C -> Y (in Ref. 7; AAB23644)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="P -> H (in Ref. 14; AAH22511)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="V -> A (in Ref. 5; AAA58447)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="R -> K (in Ref. 11; BAH14302)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="E -> G (in Ref. 5; AAA58447)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="C -> G (in Ref. 5; AAA58447)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="Q -> H (in Ref. 11; BAG65268)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="L -> V (in Ref. 14; AAH22511)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="S -> G (in Ref. 11; BAG65268)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="N -> D (in Ref. 14; AAH22511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 48722 MW; 207272D4A231404F CRC64;
METLCLRASF WLALVGCVIS DNPERYSTNL SNHVDDFTTF RGTELSFLVT THQPTNLVLP
SNGSMHNYCP QQTKITSAFK YINTVISCTI FIVGMVGNAT LLRIIYQNKC MRNGPNALIA
SLALGDLIYV VIDLPINVFK LLAGRWPFDH NDFGVFLCKL FPFLQKSSVG ITVLNLCALS
VDRYRAVASW SRVQGIGIPL VTAIEIVSIW ILSFILAIPE AIGFVMVPFE YRGEQHKTCM
LNATSKFMEF YQDVKDWWLF GFYFCMPLVC TAIFYTLMTC EMLNRRNGSL RIALSEHLKQ
RREVAKTVFC LVVIFALCWF PLHLSRILKK TVYNEMDKNR CELLSFLLLM DYIGINLATM
NSCINPIALY FVSKKFKNCF QSCLCCCCYQ SKSLMTSVPM NGTSIQWKNH DQNNHNTDRS
SHKDSMN
