P25101 (EDNRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endothelin-1 receptor

Alternative name(s):
Endothelin A receptor
Short name=ET-A
Short name=ETA-R
Short name=hET-AR

Gene names

Name:	EDNRA
Synonyms:	ETA, ETRA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3.
Subunit structure	Interacts with HDAC7 and KAT5. Ref.17
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Isoform 1, isoform 3 and isoform 4 are expressed in a variety of tissues, with highest levels in the aorta and cerebellum, followed by lung, atrium and cerebral cortex, lower levels in the placenta, kidney, adrenal gland, duodenum, colon, ventricle and liver but no expression in umbilical vein endothelial cells. Within the placenta, isoform 1, isoform 2, isoform 3 and isoform 4 are expressed in the villi and stem villi vessels. Ref.8 Ref.16
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRA sub-subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from electronic annotation. Source: Compara activation of adenylate cyclase activity Traceable author statement PubMed 8702836. Source: ProtInc activation of phospholipase C activity Traceable author statement PubMed 8702836. Source: ProtInc aging Inferred from electronic annotation. Source: Compara artery smooth muscle contraction Inferred from mutant phenotype PubMed 8982507. Source: BHF-UCL cell proliferation Non-traceable author statement Ref.16. Source: UniProtKB cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Traceable author statement PubMed 1849646. Source: ProtInc elevation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Inferred from electronic annotation. Source: Compara enteric nervous system development Inferred from electronic annotation. Source: InterPro fibroblast proliferation Inferred from electronic annotation. Source: Compara glomerular filtration Inferred from electronic annotation. Source: Compara glucose transport Inferred from sequence or structural similarity. Source: UniProtKB head development Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara histamine secretion Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara maternal process involved in parturition Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cAMP biosynthetic process Inferred from electronic annotation. Source: Compara neural crest cell development Inferred from electronic annotation. Source: Compara patterning of blood vessels Inferred from electronic annotation. Source: Compara penile erection Inferred from electronic annotation. Source: Compara positive regulation of ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of inflammatory response Inferred from electronic annotation. Source: Compara positive regulation of kidney development Inferred from electronic annotation. Source: Compara positive regulation of neutrophil chemotaxis Inferred from electronic annotation. Source: Compara positive regulation of odontogenesis Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of release of sequestered calcium ion into cytosol Inferred from electronic annotation. Source: Compara protein kinase C-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara regulation of blood pressure Inferred from electronic annotation. Source: InterPro regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara respiratory gaseous exchange Inferred from sequence or structural similarity. Source: UniProtKB response to hypoxia Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to morphine Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara
Cellular_component	T-tubule Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.6. Source: ProtInc nuclear membrane Inferred from electronic annotation. Source: Compara
Molecular_function	endothelin receptor activity Non-traceable author statement Ref.8Ref.16. Source: UniProtKB phosphatidylinositol phospholipase C activity Traceable author statement PubMed 8702836. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P25101-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P25101-2)

Also known as: Delta-3;

The sequence of this isoform differs from the canonical sequence as follows:
     141-161: LLAGRWPFDHNDFGVFLCKLF → VQSSCLLESCSGNWDSFGNCH
     162-427: Missing.

Isoform 3 (identifier: P25101-3)

Also known as: Delta-4;

The sequence of this isoform differs from the canonical sequence as follows:
     183-187: RYRAV → SSTKM
     188-427: Missing.

Isoform 4 (identifier: P25101-4)

Also known as: Delta-3,4;

The sequence of this isoform differs from the canonical sequence as follows:
     141-249: Missing.

Isoform 5 (identifier: P25101-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-225: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 427	407	Endothelin-1 receptor		PRO_0000012721
Regions
	Topological domain	21 – 80	60	Extracellular Potential
	Transmembrane	81 – 102	22	Helical; Name=1; Potential
	Topological domain	103 – 112	10	Cytoplasmic Potential
	Transmembrane	113 – 132	20	Helical; Name=2; Potential
	Topological domain	133 – 159	27	Extracellular Potential
	Transmembrane	160 – 181	22	Helical; Name=3; Potential
	Topological domain	182 – 205	24	Cytoplasmic Potential
	Transmembrane	206 – 229	24	Helical; Name=4; Potential
	Topological domain	230 – 256	27	Extracellular Potential
	Transmembrane	257 – 278	22	Helical; Name=5; Potential
	Topological domain	279 – 306	28	Cytoplasmic Potential
	Transmembrane	307 – 328	22	Helical; Name=6; Potential
	Topological domain	329 – 347	19	Extracellular Potential
	Transmembrane	348 – 372	25	Helical; Name=7; Potential
	Topological domain	373 – 427	55	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	29	1	N-linked (GlcNAc...) Potential
	Glycosylation	62	1	N-linked (GlcNAc...) Potential
	Disulfide bond	158 ↔ 239		By similarity
Natural variations
	Alternative sequence	1 – 225	225	Missing in isoform 5.		VSP_045578
	Alternative sequence	141 – 249	109	Missing in isoform 4.		VSP_011061
	Alternative sequence	141 – 161	21	LLAGR…LCKLF → VQSSCLLESCSGNWDSFGNC H in isoform 2.		VSP_011059
	Alternative sequence	162 – 427	266	Missing in isoform 2.		VSP_011060
	Alternative sequence	183 – 187	5	RYRAV → SSTKM in isoform 3.		VSP_011062
	Alternative sequence	188 – 427	240	Missing in isoform 3.		VSP_011063
	Natural variant	136	1	I → L in a breast cancer sample; somatic mutation. Ref.18		VAR_035758
Experimental info
	Sequence conflict	110	1	C → Y in AAB23644. Ref.7
	Sequence conflict	115	1	P → H in AAH22511. Ref.14
	Sequence conflict	207	1	V → A in AAA58447. Ref.5
	Sequence conflict	232	1	R → K in BAH14302. Ref.11
	Sequence conflict	234	1	E → G in AAA58447. Ref.5
	Sequence conflict	280	1	C → G in AAA58447. Ref.5
	Sequence conflict	300	1	Q → H in BAG65268. Ref.11
	Sequence conflict	322	1	L → V in AAH22511. Ref.14
	Sequence conflict	345	1	S → G in BAG65268. Ref.11
	Sequence conflict	409	1	N → D in AAH22511. Ref.14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 207272D4A231404F	FASTA	427	48,722
	10 20 30 40 50 60 METLCLRASF WLALVGCVIS DNPERYSTNL SNHVDDFTTF RGTELSFLVT THQPTNLVLP 70 80 90 100 110 120 SNGSMHNYCP QQTKITSAFK YINTVISCTI FIVGMVGNAT LLRIIYQNKC MRNGPNALIA 130 140 150 160 170 180 SLALGDLIYV VIDLPINVFK LLAGRWPFDH NDFGVFLCKL FPFLQKSSVG ITVLNLCALS 190 200 210 220 230 240 VDRYRAVASW SRVQGIGIPL VTAIEIVSIW ILSFILAIPE AIGFVMVPFE YRGEQHKTCM 250 260 270 280 290 300 LNATSKFMEF YQDVKDWWLF GFYFCMPLVC TAIFYTLMTC EMLNRRNGSL RIALSEHLKQ 310 320 330 340 350 360 RREVAKTVFC LVVIFALCWF PLHLSRILKK TVYNEMDKNR CELLSFLLLM DYIGINLATM 370 380 390 400 410 420 NSCINPIALY FVSKKFKNCF QSCLCCCCYQ SKSLMTSVPM NGTSIQWKNH DQNNHNTDRS SHKDSMN
	Isoform 2 (Delta-3) [UniParc]. Checksum: B6227E27C1B05915	FASTA	161	17,820
	10 20 30 40 50 60 METLCLRASF WLALVGCVIS DNPERYSTNL SNHVDDFTTF RGTELSFLVT THQPTNLVLP 70 80 90 100 110 120 SNGSMHNYCP QQTKITSAFK YINTVISCTI FIVGMVGNAT LLRIIYQNKC MRNGPNALIA 130 140 150 160 SLALGDLIYV VIDLPINVFK VQSSCLLESC SGNWDSFGNC H
	Isoform 3 (Delta-4) [UniParc]. Checksum: 60E5564BDE6D7A96	FASTA	187	20,763
	10 20 30 40 50 60 METLCLRASF WLALVGCVIS DNPERYSTNL SNHVDDFTTF RGTELSFLVT THQPTNLVLP 70 80 90 100 110 120 SNGSMHNYCP QQTKITSAFK YINTVISCTI FIVGMVGNAT LLRIIYQNKC MRNGPNALIA 130 140 150 160 170 180 SLALGDLIYV VIDLPINVFK LLAGRWPFDH NDFGVFLCKL FPFLQKSSVG ITVLNLCALS VDSSTKM
	Isoform 4 (Delta-3,4) [UniParc]. Checksum: 0423FAA16DB6A9BF	FASTA	318	36,489
	10 20 30 40 50 60 METLCLRASF WLALVGCVIS DNPERYSTNL SNHVDDFTTF RGTELSFLVT THQPTNLVLP 70 80 90 100 110 120 SNGSMHNYCP QQTKITSAFK YINTVISCTI FIVGMVGNAT LLRIIYQNKC MRNGPNALIA 130 140 150 160 170 180 SLALGDLIYV VIDLPINVFK FYQDVKDWWL FGFYFCMPLV CTAIFYTLMT CEMLNRRNGS 190 200 210 220 230 240 LRIALSEHLK QRREVAKTVF CLVVIFALCW FPLHLSRILK KTVYNEMDKN RCELLSFLLL 250 260 270 280 290 300 MDYIGINLAT MNSCINPIAL YFVSKKFKNC FQSCLCCCCY QSKSLMTSVP MNGTSIQWKN 310 HDQNNHNTDR SSHKDSMN
	Isoform 5 [UniParc]. Checksum: 01C9764279D905CD	FASTA	202	23,803
	10 20 30 40 50 60 MVPFEYRGEQ HKTCMLNATS KFMEFYQDVK DWWLFGFYFC MPLVCTAIFY TLMTCEMLNR 70 80 90 100 110 120 RNGSLRIALS EHLKQRREVA KTVFCLVVIF ALCWFPLHLS RILKKTVYNE MDKNRCELLS 130 140 150 160 170 180 FLLLMDYIGI NLATMNSCIN PIALYFVSKK FKNCFQSCLC CCCYQSKSLM TSVPMNGTSI 190 200 QWKNHDQNNH NTDRSSHKDS MN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of cDNA encoding human A-type endothelin receptor." Adachi M., Yang Y.Y., Furuichi Y., Miyamoto C. Biochem. Biophys. Res. Commun. 180:1265-1272(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1). Tissue: Placenta.
[2]	"Cloning and chromosomal localization of a human endothelin ETA receptor." Cyr C., Huebner K., Druck T., Kris R. Biochem. Biophys. Res. Commun. 181:184-190(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1). Tissue: Placenta.
[3]	"Cloning and expression of human endothelin-1 receptor cDNA." Hosoda K., Nakao K., Arai H., Suga S., Ogawa Y., Mukoyama M., Shirakami G., Saito Y., Nakanishi S., Imura H. FEBS Lett. 287:23-26(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[4]	"Molecular cloning of human endothelin receptors and their expression in vascular endothelial cells and smooth muscle cells." Arai H., Nakao K., Hosoda K., Ogawa Y., Nakagawa O., Komatsu Y., Imura H. Jpn. Circ. J. 56:1303-1307(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[5]	"Molecular characterization and regulation of the human endothelin receptors." Elshourbagy N.A., Korman D.R., Wu H.L., Sylvester D.R., Lee J.A., Nuthalaganti P., Bergsma D.J., Kumar C.S., Nambi P. J. Biol. Chem. 268:3873-3879(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]	"Organization, structure, chromosomal assignment, and expression of the gene encoding the human endothelin-A receptor." Hosoda K., Nakao K., Tamura N., Arai H., Ogawa Y., Suga S., Nakanishi S., Imura H. J. Biol. Chem. 267:18797-18804(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[7]	"Cloning and expression of a human endothelin receptor: subtype A." Hayzer D.J., Rose P.M., Lynch J.S., Webb M.L., Kienzle B.K., Liu E.C., Bogosian E.A., Brinson E., Runge M.S. Am. J. Med. Sci. 304:231-238(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Placenta.
[8]	"Alternative RNA splicing of the human endothelin-A receptor generates multiple transcripts." Miyamoto Y., Yoshimasa T., Arai H., Takaya K., Ogawa Y., Itoh H., Nakao K. Biochem. J. 313:795-801(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), TISSUE SPECIFICITY. Tissue: Lung.
[9]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Warren C.N., Aronstam R.S., Sharma S.V. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[10]	NIEHS SNPs program Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5). Tissue: Cerebellum, Testis and Trachea.
[12]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[15]	"Molecular characterization of the 5'-flanking region of human genomic ETA gene." Yang H., Tabuchi H., Furuichi Y., Miyamoto C. Biochem. Biophys. Res. Commun. 190:332-339(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140 (ISOFORMS 1/2/3/4).
[16]	"Endothelin-1 and ETA receptor expression in vascular smooth muscle cells from human placenta: a new ETA receptor messenger ribonucleic acid is generated by alternative splicing of exon 3." Bourgeois C., Robert B., Rebourcet R., Mondon F., Mignot T.-M., Duc-Goiran P., Ferre F. J. Clin. Endocrinol. Metab. 82:3116-3123(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-427 (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Placenta.
[17]	"Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling." Lee H.-J., Chun M., Kandror K.V. J. Biol. Chem. 276:16597-16600(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC7 AND KAT5.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-136.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	S63938 mRNA. Translation: AAB20278.1. S67127 mRNA. Translation: AAB20407.1. X61950 mRNA. Translation: CAA43953.1. D90348 mRNA. Translation: BAA14359.1. S57498 mRNA. Translation: AAB25530.2. L06622 mRNA. Translation: AAA58447.1. D11151 Genomic DNA. Translation: BAA01920.1. S45956 mRNA. Translation: AAB23644.1. S81539 mRNA. Translation: AAB36325.1. S81542 mRNA. Translation: AAB36326.1. S81545 mRNA. Translation: AAB36327.1. AY275462 mRNA. Translation: AAP32294.1. AY422989 Genomic DNA. Translation: AAQ87880.1. AK304451 mRNA. Translation: BAG65268.1. AK312812 mRNA. Translation: BAG35670.1. AK315931 mRNA. Translation: BAH14302.1. AC093908 Genomic DNA. No translation available. CH471056 Genomic DNA. Translation: EAX05019.1. CH471056 Genomic DNA. Translation: EAX05021.1. BC022511 mRNA. Translation: AAH22511.1. S55772 Genomic DNA. Translation: AAB25212.1. AF014826 mRNA. Translation: AAB94859.1.
IPI	IPI00434353. IPI00434354. IPI00434355. IPI00434356. IPI00966192.
PIR	A44158.
RefSeq	NP_001159527.1. NM_001166055.1. NP_001243212.1. NM_001256283.1. NP_001948.1. NM_001957.3.
UniGene	Hs.183713.
3D structure databases
ProteinModelPortal	P25101.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48718N.
STRING	9606.ENSP00000315011.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P25101.
Polymorphism databases
DMDM	119606.
Proteomic databases
PaxDb	P25101.
PRIDE	P25101.
Protocols and materials databases
DNASU	1909.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324300; ENSP00000315011; ENSG00000151617. ENST00000339690; ENSP00000341556; ENSG00000151617. ENST00000358556; ENSP00000351359; ENSG00000151617. ENST00000506066; ENSP00000425281; ENSG00000151617. ENST00000510697; ENSP00000427259; ENSG00000151617. ENST00000511804; ENSP00000425354; ENSG00000151617.
GeneID	1909.
KEGG	hsa:1909.
UCSC	uc003iky.3. human. uc010ipe.1. human. uc010ipg.2. human.
Organism-specific databases
CTD	1909.
GeneCards	GC04P148401.
HGNC	HGNC:3179. EDNRA.
HPA	CAB018957. HPA013774. HPA014087.
MIM	131243. gene.
neXtProt	NX_P25101.
PharmGKB	PA27617.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG278704.
HOVERGEN	HBG051443.
InParanoid	P25101.
KO	K04197.
OMA	DNPESYS.
OrthoDB	EOG4W3SMZ.
PhylomeDB	P25101.
Enzyme and pathway databases
Pathway_Interaction_DB	endothelinpathway. Endothelins.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P25101.
Bgee	P25101.
CleanEx	HS_EDNRA.
Genevestigator	P25101.
GermOnline	ENSG00000151617. Homo sapiens.
Family and domain databases
InterPro	IPR000499. Endthln_rcpt. IPR002175. ETA_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00570. ENDOTHELINAR. PR00366. ENDOTHELINR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P25101.
ChEMBL	CHEMBL252.
DrugBank	DB00559. Bosentan.
GenomeRNAi	1909.
NextBio	35477375.
SOURCE	Search...

Entry information

Entry name

EDNRA_HUMAN

Accession

Primary (citable) accession number: P25101
Secondary accession number(s): B2R723 , B4E2V6, B7Z9G6, D3DP03, E7ER36, O43441, Q16432, Q16433, Q8TBH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.