P24530 (EDNRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endothelin B receptor
Short name=ET-B
Short name=ET-BR

Alternative name(s):
Endothelin receptor non-selective type

Gene names

Name:	EDNRB
Synonyms:	ETRB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	442 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	Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Ref.8
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in placental stem villi vessels, but not in cultured placental villi smooth muscle cells. Ref.19
Post-translational modification	Palmitoylation of Cys-402 was confirmed by the palmitoylation of Cys-402 in a deletion mutant lacking both Cys-403 and Cys-405.
Involvement in disease	Defects in EDNRB are a cause of Waardenburg syndrome type 4A (WS4A) [MIM:277580]; also known as Waardenburg-Shah syndrome. WS4A is characterized by the association of Waardenburg features (depigmentation and deafness) and the absence of enteric ganglia in the distal part of the intestine (Hirschsprung disease). Ref.23 Ref.30 Defects in EDNRB are the cause of Hirschsprung disease type 2 (HSCR2) [MIM:600155]; also known as aganglionic megacolon (MGC). HSCR2 is a congenital disorder characterized by absence of enteric ganglia along a variable length of the intestine. It is the most common cause of congenital intestinal obstruction. Early symptoms range from complete acute neonatal obstruction, characterized by vomiting, abdominal distention and failure to pass stool, to chronic constipation in the older child. Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Defects in EDNRB are the cause of ABCD syndrome (ABCDS) [MIM:600501]. ABCD syndrome is an autosomal recessive syndrome characterized by albinism, black lock at temporal occipital region, bilateral deafness, aganglionosis of the large intestine and total absence of neurocytes and nerve fibers in the small intestine.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRB sub-subfamily.
Sequence caution	The sequence BAD92435.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Deafness Disease mutation Hirschsprung disease Waardenburg syndrome
Domain	Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger Traceable author statement. Source: ProtInc enteric nervous system development Inferred from sequence or structural similarity. Source: BHF-UCL enteric smooth muscle cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL macrophage chemotaxis Inferred from mutant phenotype. Source: BHF-UCL negative regulation of adenylate cyclase activity Traceable author statement. Source: ProtInc negative regulation of cellular protein metabolic process Inferred from mutant phenotype. Source: BHF-UCL negative regulation of neuron maturation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL vein smooth muscle contraction Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	endothelin receptor activity Inferred from direct assay Ref.3. Source: BHF-UCL peptide hormone binding Inferred from direct assay Ref.3. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P24530-1) 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 B (identifier: P24530-2) The sequence of this isoform differs from the canonical sequence as follows:      399-442: SCLCCWCQSF...FRSSNKYSSS → AGPHVGNKLV...MWPERKSNNN
Isoform C (identifier: P24530-3) Also known as: Delta-3; The sequence of this isoform differs from the canonical sequence as follows:      1-1: M → MNKSTCLMAA...RTPSGAGSSM
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	79 – 84	6	SGHRTP → RPPDA in AAD24541. Ref.10

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 442	416	Endothelin B receptor		PRO_0000012729
Regions
	Topological domain	27 – 101	75	Extracellular Potential
	Transmembrane	102 – 126	25	Helical; Name=1; Potential
	Topological domain	127 – 137	11	Cytoplasmic Potential
	Transmembrane	138 – 163	26	Helical; Name=2; Potential
	Topological domain	164 – 175	12	Extracellular Potential
	Transmembrane	176 – 197	22	Helical; Name=3; Potential
	Topological domain	198 – 218	21	Cytoplasmic Potential
	Transmembrane	219 – 243	25	Helical; Name=4; Potential
	Topological domain	244 – 271	28	Extracellular Potential
	Transmembrane	272 – 296	25	Helical; Name=5; Potential
	Topological domain	297 – 324	28	Cytoplasmic Potential
	Transmembrane	325 – 350	26	Helical; Name=6; Potential
	Topological domain	351 – 362	12	Extracellular Potential
	Transmembrane	363 – 389	27	Helical; Name=7; Potential
	Topological domain	390 – 442	53	Cytoplasmic Potential
Amino acid modifications
	Lipidation	402	1	S-palmitoyl cysteine Ref.20
	Lipidation	403	1	S-palmitoyl cysteine Potential
	Lipidation	405	1	S-palmitoyl cysteine Potential
	Glycosylation	59	1	N-linked (GlcNAc...) Potential
	Disulfide bond	174 ↔ 255		By similarity
Natural variations
	Alternative sequence	1	1	M → MNKSTCLMAAETPSKRWRLH CLAFSQRFVRAGPACSSREA CSSPRAGWNPAGFRLPGRWS PFVALHLVCQIREALKLRSG HRTPSGAGSSM in isoform C.		VSP_001878
	Alternative sequence	399 – 442	44	SCLCC…KYSSS → AGPHVGNKLVMLFSVNIECD GTVNQNPTMWPERKSNNN in isoform B.		VSP_001879
	Natural variant	5	1	P → T. Ref.14 Corresponds to variant rs12720160 [ dbSNP | Ensembl ].		VAR_019285
	Natural variant	7	1	L → Q. Corresponds to variant rs5345 [ dbSNP | Ensembl ].		VAR_014675
	Natural variant	17	1	L → F. Corresponds to variant rs5346 [ dbSNP | Ensembl ].		VAR_014676
	Natural variant	57	1	G → S in HSCR2; sporadic; sex-dependent gene dosage effect; neuronal intestinal dysplasia; could be a polymorphism. Ref.25 Ref.26 Ref.27 Ref.28 Corresponds to variant rs1801710 [ dbSNP | Ensembl ].		VAR_003469
	Natural variant	76	1	R → M. Corresponds to variant rs2228271 [ dbSNP | Ensembl ].		VAR_024255
	Natural variant	112	1	F → V. Corresponds to variant rs5347 [ dbSNP | Ensembl ].		VAR_014677
	Natural variant	183	1	A → G in WS4A. Ref.23		VAR_003470
	Natural variant	244	1	T → M. Corresponds to variant rs5350 [ dbSNP | Ensembl ].		VAR_014678
	Natural variant	276	1	W → C in HSCR2. Ref.22		VAR_003471
	Natural variant	292	1	F → L in WS4A. Ref.30		VAR_015294
	Natural variant	305	1	S → N in HSCR2; familial. Ref.14 Ref.24 Corresponds to variant rs5352 [ dbSNP | Ensembl ].		VAR_003472
	Natural variant	319	1	R → W in HSCR2; sporadic. Ref.25 Ref.28		VAR_003473
	Natural variant	374	1	M → I in HSCR2. Ref.26		VAR_003474
	Natural variant	383	1	P → L in HSCR2; familial. Ref.25 Ref.28		VAR_003475
Experimental info
	Mutagenesis	402	1	C → S: Abolishes palmitoylation; when associated with S-403 and S-405. Ref.20
	Mutagenesis	403	1	C → S: Abolishes palmitoylation; when associated with S-402 and S-405. Ref.20
	Mutagenesis	405	1	C → S: Abolishes palmitoylation; when associated with S-402 and S-403. Ref.20
	Sequence conflict	10	1	R → P in AAB19411. Ref.3
	Sequence conflict	16	1	V → L Ref.8
	Sequence conflict	22 – 24	3	SRI → LGV Ref.8
	Sequence conflict	35	1	R → K Ref.8
	Sequence conflict	45	1	I → M in BAD92435. Ref.12
	Sequence conflict	58	1	S → P in BAF83388. Ref.13
	Sequence conflict	140	1	I → V Ref.8
	Sequence conflict	385	1	A → V in BAF83388. Ref.13

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified March 1, 1992. Version 1. Checksum: CD4F96CF92C7C51E	FASTA	442	49,644
	10 20 30 40 50 60 MQPPPSLCGR ALVALVLACG LSRIWGEERG FPPDRATPLL QTAEIMTPPT KTLWPKGSNA 70 80 90 100 110 120 SLARSLAPAE VPKGDRTAGS PPRTISPPPC QGPIEIKETF KYINTVVSCL VFVLGIIGNS 130 140 150 160 170 180 TLLRIIYKNK CMRNGPNILI ASLALGDLLH IVIDIPINVY KLLAEDWPFG AEMCKLVPFI 190 200 210 220 230 240 QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF 250 260 270 280 290 300 DIITMDYKGS YLRICLLHPV QKTAFMQFYK TAKDWWLFSF YFCLPLAITA FFYTLMTCEM 310 320 330 340 350 360 LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTLY NQNDPNRCEL 370 380 390 400 410 420 LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQSFEE KQSLEEKQSC 430 440 LKFKANDHGY DNFRSSNKYS SS
	Isoform B [UniParc]. Checksum: A10BD0DD646F981E	FASTA	436	48,710
	10 20 30 40 50 60 MQPPPSLCGR ALVALVLACG LSRIWGEERG FPPDRATPLL QTAEIMTPPT KTLWPKGSNA 70 80 90 100 110 120 SLARSLAPAE VPKGDRTAGS PPRTISPPPC QGPIEIKETF KYINTVVSCL VFVLGIIGNS 130 140 150 160 170 180 TLLRIIYKNK CMRNGPNILI ASLALGDLLH IVIDIPINVY KLLAEDWPFG AEMCKLVPFI 190 200 210 220 230 240 QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF 250 260 270 280 290 300 DIITMDYKGS YLRICLLHPV QKTAFMQFYK TAKDWWLFSF YFCLPLAITA FFYTLMTCEM 310 320 330 340 350 360 LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTLY NQNDPNRCEL 370 380 390 400 410 420 LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKAG PHVGNKLVML FSVNIECDGT 430 VNQNPTMWPE RKSNNN
	Isoform C (Delta-3) [UniParc]. Checksum: 9734B81C0064F533	FASTA	532	59,480
	10 20 30 40 50 60 MNKSTCLMAA ETPSKRWRLH CLAFSQRFVR AGPACSSREA CSSPRAGWNP AGFRLPGRWS 70 80 90 100 110 120 PFVALHLVCQ IREALKLRSG HRTPSGAGSS MQPPPSLCGR ALVALVLACG LSRIWGEERG 130 140 150 160 170 180 FPPDRATPLL QTAEIMTPPT KTLWPKGSNA SLARSLAPAE VPKGDRTAGS PPRTISPPPC 190 200 210 220 230 240 QGPIEIKETF KYINTVVSCL VFVLGIIGNS TLLRIIYKNK CMRNGPNILI ASLALGDLLH 250 260 270 280 290 300 IVIDIPINVY KLLAEDWPFG AEMCKLVPFI QKASVGITVL SLCALSIDRY RAVASWSRIK 310 320 330 340 350 360 GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF DIITMDYKGS YLRICLLHPV QKTAFMQFYK 370 380 390 400 410 420 TAKDWWLFSF YFCLPLAITA FFYTLMTCEM LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL 430 440 450 460 470 480 VFALCWLPLH LSRILKLTLY NQNDPNRCEL LSFLLVLDYI GINMASLNSC INPIALYLVS 490 500 510 520 530 KRFKNCFKSC LCCWCQSFEE KQSLEEKQSC LKFKANDHGY DNFRSSNKYS SS

References

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[1]	"Cloning and sequence analysis of a cDNA encoding human non-selective type of endothelin receptor." Nakamuta M., Takayanagi R., Sakai Y., Sakamoto S., Hagiwara H., Mizuno T., Saito Y., Hirose S., Yamamoto M., Nawata H. Biochem. Biophys. Res. Commun. 177:34-39(1991) [PubMed: 1710450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]	"Molecular cloning of a non-isopeptide-selective human endothelin receptor." Ogawa Y., Nakao K., Arai H., Nakagawa O., Hosoda K., Suga S., Nakanishi S., Imura H. Biochem. Biophys. Res. Commun. 178:248-255(1991) [PubMed: 1648908] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[3]	"Cloning and functional expression of human cDNA for the ETB endothelin receptor." Sakamoto A., Yanagisawa M., Sakurai T., Takuwa Y., Yanagisawa H., Masaki T. Biochem. Biophys. Res. Commun. 178:656-663(1991) [PubMed: 1713452] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[4]	"Molecular cloning of human endothelin (ET) receptors ETA and ETB." Haendler B., Hechler U., Schleuning W.-D. J. Cardiovasc. Pharmacol. 20:S1-S4(1992) [PubMed: 1282938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). Tissue: Lung.
[5]	"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: 1291713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[6]	"The human endothelin-B receptor gene. Structural organization and chromosomal assignment." Arai H., Nakao K., Takaya K., Hosoda K., Ogawa Y., Nakanishi S., Imura H. J. Biol. Chem. 268:3463-3470(1993) [PubMed: 8429023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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: 8440682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[8]	"Cloning and expression of an endothelin receptor subtype B from human prostate that mediates contraction." Webb M.L., Chao C.-C., Rizzo M., Shapiro R.A., Neubauer M., Liu E.C.K., Aversa C.R., Brittain R.J., Treiger B. Mol. Pharmacol. 47:730-737(1995) [PubMed: 7536888] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION. Tissue: Prostate.
[9]	"Molecular characterization of a novel human endothelin receptor splice variant." Elshourbagy N.A., Adamou J.E., Gagnon A.W., Wu H.L., Pullen M., Nambi P. J. Biol. Chem. 271:25300-25307(1996) [PubMed: 8810293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). Tissue: Placenta.
[10]	"Novel endothelin B receptor transcripts with the potential of generating a new receptor." Tsutsumi M., Liang G., Jones P.A. Gene 228:43-49(1999) [PubMed: 10072757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
[11]	"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 A). Tissue: Placenta.
[12]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Tissue: Brain.
[13]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[14]	NIEHS SNPs program Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-5 AND ASN-305.
[15]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[16]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[17]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Tissue: Skin.
[18]	"Significance of novel endothelin-B receptor gene polymorphisms in Hirschsprung's disease: predominance of a novel variant (561C/T) in patients with co-existing Down's syndrome." Zaahl M.G., du Plessis L., Warnich L., Kotze M.J., Moore S.W. Mol. Cell. Probes 17:49-54(2003) [PubMed: 12628594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102; 172-196 AND 200-317.
[19]	"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: 9284755] [Abstract] Cited for: TISSUE SPECIFICITY.
[20]	"Palmitoylation of human endothelinB. Its critical role in G protein coupling and a differential requirement for the cytoplasmic tail by G protein subtypes." Okamoto Y., Ninomiya H., Tanioka M., Sakamoto A., Miwa S., Masaki T. J. Biol. Chem. 272:21589-21596(1997) [PubMed: 9261180] [Abstract] Cited for: PALMITOYLATION AT CYS-402; CYS-403 AND CYS-405, MUTAGENESIS OF CYS-402; CYS-403 AND CYS-405.
[21]	"Mutations in Hirschsprung disease: when does a mutation contribute to the phenotype." Hofstra R.M.W., Osinga J., Buys C.H.C.M. Eur. J. Hum. Genet. 5:180-185(1997) [PubMed: 9359036] [Abstract] Cited for: REVIEW ON VARIANTS.
[22]	"A missense mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease." Puffenberger E.G., Hosoda K., Washington S.S., Nakao K., Dewit D., Yanagisawa M., Chakravarti A. Cell 79:1257-1266(1994) [PubMed: 8001158] [Abstract] Cited for: VARIANT HSCR2 CYS-276.
[23]	"Mutation of the endothelin-receptor B gene in Waardenburg-Hirschsprung disease." Attie T., Till M., Pelet A., Amiel J., Edery P., Boutrand L., Munnich A., Lyonnet S. Hum. Mol. Genet. 4:2407-2409(1995) [PubMed: 8634719] [Abstract] Cited for: VARIANT WS4A GLY-183.
[24]	"Endothelin-B receptor mutations in patients with isolated Hirschsprung disease from a non-inbred population." Auricchio A., Casari G., Staiano A., Ballabio A. Hum. Mol. Genet. 5:351-354(1996) [PubMed: 8852659] [Abstract] Cited for: VARIANT HSCR2 ASN-305.
[25]	"Heterozygous endothelin receptor B (EDNRB) mutations in isolated Hirschsprung disease." Amiel J., Attie T., Jan D., Pelet A., Edery P., Bidaud C., Lacombe D., Tam P., Simeoni J., Flori E., Nihoul-Fekete C., Munnich A., Lyonnet S. Hum. Mol. Genet. 5:355-357(1996) [PubMed: 8852660] [Abstract] Cited for: VARIANTS HSCR2 SER-57; TRP-319 AND LEU-383.
[26]	"A homozygous mutation in the endothelin-3 gene associated with a combined Waardenburg type 2 and Hirschsprung phenotype (Shah-Waardenburg syndrome)." Hofstra R.M.W., Tan-Sindhunata G., Wu Y., Kamsteeg E.-J., Stulp R.P., van Ravenswaaij-Arts C., Majoor-Krakauer D., Angrist M., Chakravarti A., Meijers C., Buys C.H.C.M. Nat. Genet. 12:445-447(1996) [PubMed: 8630503] [Abstract] Cited for: VARIANT HSCR2 ILE-374, VARIANT SER-57.
[27]	"Phenotypic variation in a family with mutations in two Hirschsprung-related genes (RET and endothelin receptor B)." Svensson P.J., Anvret M., Molander M.L., Nordenskjold A. Hum. Genet. 103:145-148(1998) [PubMed: 9760196] [Abstract] Cited for: VARIANT HSCR2 SER-57.
[28]	"Functional characterization of three mutations of the endothelin B receptor gene in patients with Hirschsprung's disease: evidence for selective loss of Gi coupling." Fuchs S., Amiel J., Claudel S., Lyonnet S., Corvol P., Pinet F. Mol. Med. 7:115-124(2001) [PubMed: 11471546] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS HSCR2 SER-57; TRP-319 AND LEU-383.
[29]	"ABCD syndrome is caused by a homozygous mutation in the EDNRB gene." Verheij J.B., Kunze J., Osinga J., van Essen A.J., Hofstra R.M. Am. J. Med. Genet. 108:223-225(2002) [PubMed: 11891690] [Abstract] Cited for: INVOLVEMENT IN ABCD SYNDROME.
[30]	"SOX10 mutations in chronic intestinal pseudo-obstruction suggest a complex physiopathological mechanism." Pingault V., Girard M., Bondurand N., Dorkins H., Van Maldergem L., Mowat D., Shimotake T., Verma I., Baumann C., Goossens M. Hum. Genet. 111:198-206(2002) [PubMed: 12189494] [Abstract] Cited for: VARIANT WS4A LEU-292.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M74921 mRNA. Translation: AAA58465.1. D90402 mRNA. Translation: BAA14398.1. S44866 mRNA. Translation: AAB19411.1. S57283 mRNA. Translation: AAB25531.1. D13168 Genomic DNA. Translation: BAA02445.1. L06623 mRNA. Translation: AAA52342.1. X99250 mRNA. Translation: CAA67623.1. AF114165 mRNA. Translation: AAD24541.1. AY275463 mRNA. Translation: AAP32295.1. AB209198 mRNA. Translation: BAD92435.1. Different initiation. AK290699 mRNA. Translation: BAF83388.1. AY547312 Genomic DNA. Translation: AAS38516.1. AL139002 Genomic DNA. Translation: CAM16893.1. AL139002 Genomic DNA. Translation: CAH72430.1. CH471093 Genomic DNA. Translation: EAW80573.1. CH471093 Genomic DNA. Translation: EAW80575.1. BC014472 mRNA. Translation: AAH14472.1. AJ458188 Genomic DNA. Translation: CAD30645.1. AJ458189 Genomic DNA. Translation: CAD30646.1. AJ458190 Genomic DNA. Translation: CAD30647.1. AJ458191 Genomic DNA. Translation: CAD30648.1.
IPI	IPI00029123. IPI00218197. IPI00412464.
PIR	JQ1042. A46609.
RefSeq	NP_000106.1. NM_000115.3. NP_001116131.1. NM_001122659.2. NP_001188326.1. NM_001201397.1. NP_003982.1. NM_003991.3.
UniGene	Hs.82002.
3D structure databases
ProteinModelPortal	P24530.
SMR	P24530. Positions 102-410.
ModBase	Search...
Protein-protein interaction databases
STRING	P24530.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P24530.
Polymorphism databases
DMDM	119622.
Proteomic databases
PRIDE	P24530.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000334286; ENSP00000335311; ENSG00000136160. ENST00000377211; ENSP00000366416; ENSG00000136160.
GeneID	1910.
KEGG	hsa:1910.
UCSC	uc001vko.2. human. uc010aez.1. human.
Organism-specific databases
CTD	1910.
GeneCards	GC13M078469.
H-InvDB	HIX0011385.
HGNC	HGNC:3180. EDNRB.
HPA	CAB017842.
MIM	131244. gene. 142623. phenotype. 277580. phenotype. 600155. phenotype. 600501. phenotype.
neXtProt	NX_P24530.
Orphanet	918. ABCD syndrome. 388. Hirschsprung disease. 897. Waardenburg-Shah syndrome.
PharmGKB	PA27618.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07512.
GeneTree	ENSGT00550000074261.
HOVERGEN	HBG051443.
InParanoid	P24530.
OMA	PVQKTAF.
OrthoDB	EOG45HRX3.
Enzyme and pathway databases
Pathway_Interaction_DB	arf6_traffickingpathway. Arf6 trafficking events. endothelinpathway. Endothelins.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P24530.
Bgee	P24530.
Genevestigator	P24530.
GermOnline	ENSG00000136160. Homo sapiens.
Family and domain databases
InterPro	IPR000276. 7TM_GPCR_Rhodpsn. IPR000499. Endthln_rcpt. IPR001112. ETB_rcpt. IPR017452. GPCR_Rhodpsn_supfam. [Graphical view]
KO	K04198.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00571. ENDOTHELINBR. 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
DrugBank	DB00559. Bosentan.
NextBio	7779.
SOURCE	Search...

Entry information

Entry name

EDNRB_HUMAN

Accession

Primary (citable) accession number: P24530
Secondary accession number(s): A2A2Z8 , A8K3T4, O15343, Q59GB1, Q5W0G9, Q8NHM6, Q8NHM7, Q8NHM8, Q8NHM9, Q9UD23, Q9UQK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	January 25, 2012
This is version 144 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.