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Endothelin receptor type B (ET-B) (ET-BR) (Endothelin receptor non-selective type)

 EDNRB_HUMAN             Reviewed;         442 AA.
P24530; A2A2Z8; A8K3T4; O15343; Q59GB1; Q5W0G9; Q8NHM6; Q8NHM7;
Q8NHM8; Q8NHM9; Q9UD23; Q9UQK3;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
12-SEP-2018, entry version 211.
RecName: Full=Endothelin receptor type B {ECO:0000305};
Short=ET-B;
Short=ET-BR;
AltName: Full=Endothelin receptor non-selective type;
Flags: Precursor;
Name=EDNRB {ECO:0000312|HGNC:HGNC:3180}; Synonyms=ETRB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=1710450; DOI=10.1016/0006-291X(91)91944-8;
Nakamuta M., Takayanagi R., Sakai Y., Sakamoto S., Hagiwara H.,
Mizuno T., Saito Y., Hirose S., Yamamoto M., Nawata H.;
"Cloning and sequence analysis of a cDNA encoding human non-selective
type of endothelin receptor.";
Biochem. Biophys. Res. Commun. 177:34-39(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=1648908; DOI=10.1016/0006-291X(91)91806-N;
Ogawa Y., Nakao K., Arai H., Nakagawa O., Hosoda K., Suga S.,
Nakanishi S., Imura H.;
"Molecular cloning of a non-isopeptide-selective human endothelin
receptor.";
Biochem. Biophys. Res. Commun. 178:248-255(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=1713452; DOI=10.1016/0006-291X(91)90158-4;
Sakamoto A., Yanagisawa M., Sakurai T., Takuwa Y., Yanagisawa H.,
Masaki T.;
"Cloning and functional expression of human cDNA for the ETB
endothelin receptor.";
Biochem. Biophys. Res. Commun. 178:656-663(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Lung;
PubMed=1282938;
Haendler B., Hechler U., Schleuning W.-D.;
"Molecular cloning of human endothelin (ET) receptors ETA and ETB.";
J. Cardiovasc. Pharmacol. 20:S1-S4(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=1291713;
Arai H., Nakao K., Hosoda K., Ogawa Y., Nakagawa O., Komatsu Y.,
Imura H.;
"Molecular cloning of human endothelin receptors and their expression
in vascular endothelial cells and smooth muscle cells.";
Jpn. Circ. J. 56:1303-1307(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8429023;
Arai H., Nakao K., Takaya K., Hosoda K., Ogawa Y., Nakanishi S.,
Imura H.;
"The human endothelin-B receptor gene. Structural organization and
chromosomal assignment.";
J. Biol. Chem. 268:3463-3470(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=8440682;
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.;
"Molecular characterization and regulation of the human endothelin
receptors.";
J. Biol. Chem. 268:3873-3879(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
TISSUE=Prostate;
PubMed=7536888;
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.;
"Cloning and expression of an endothelin receptor subtype B from human
prostate that mediates contraction.";
Mol. Pharmacol. 47:730-737(1995).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Placenta;
PubMed=8810293; DOI=10.1074/jbc.271.41.25300;
Elshourbagy N.A., Adamou J.E., Gagnon A.W., Wu H.L., Pullen M.,
Nambi P.;
"Molecular characterization of a novel human endothelin receptor
splice variant.";
J. Biol. Chem. 271:25300-25307(1996).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
PubMed=10072757; DOI=10.1016/S0378-1119(99)00014-1;
Tsutsumi M., Liang G., Jones P.A.;
"Novel endothelin B receptor transcripts with the potential of
generating a new receptor.";
Gene 228:43-49(1999).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Placenta;
Warren C.N., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Brain;
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.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-5 AND ASN-305.
NIEHS SNPs program;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
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.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[17]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102; 172-196 AND 200-317.
PubMed=12628594; DOI=10.1016/S0890-8508(03)00003-3;
Zaahl M.G., du Plessis L., Warnich L., Kotze M.J., Moore S.W.;
"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.";
Mol. Cell. Probes 17:49-54(2003).
[19]
TISSUE SPECIFICITY.
PubMed=9284755; DOI=10.1210/jcem.82.9.4209;
Bourgeois C., Robert B., Rebourcet R., Mondon F., Mignot T.-M.,
Duc-Goiran P., Ferre F.;
"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.";
J. Clin. Endocrinol. Metab. 82:3116-3123(1997).
[20]
PALMITOYLATION AT CYS-402; CYS-403 AND CYS-405, AND MUTAGENESIS OF
CYS-402; CYS-403 AND CYS-405.
PubMed=9261180; DOI=10.1074/jbc.272.34.21589;
Okamoto Y., Ninomiya H., Tanioka M., Sakamoto A., Miwa S., Masaki T.;
"Palmitoylation of human endothelinB. Its critical role in G protein
coupling and a differential requirement for the cytoplasmic tail by G
protein subtypes.";
J. Biol. Chem. 272:21589-21596(1997).
[21]
REVIEW ON VARIANTS.
PubMed=9359036;
Hofstra R.M.W., Osinga J., Buys C.H.C.M.;
"Mutations in Hirschsprung disease: when does a mutation contribute to
the phenotype.";
Eur. J. Hum. Genet. 5:180-185(1997).
[22]
VARIANT HSCR2 CYS-276.
PubMed=8001158; DOI=10.1016/0092-8674(94)90016-7;
Puffenberger E.G., Hosoda K., Washington S.S., Nakao K., Dewit D.,
Yanagisawa M., Chakravarti A.;
"A missense mutation of the endothelin-B receptor gene in multigenic
Hirschsprung's disease.";
Cell 79:1257-1266(1994).
[23]
VARIANT WS4A GLY-183.
PubMed=8634719; DOI=10.1093/hmg/4.12.2407;
Attie T., Till M., Pelet A., Amiel J., Edery P., Boutrand L.,
Munnich A., Lyonnet S.;
"Mutation of the endothelin-receptor B gene in Waardenburg-
Hirschsprung disease.";
Hum. Mol. Genet. 4:2407-2409(1995).
[24]
VARIANT ASN-305.
PubMed=8852659; DOI=10.1093/hmg/5.3.351;
Auricchio A., Casari G., Staiano A., Ballabio A.;
"Endothelin-B receptor mutations in patients with isolated
Hirschsprung disease from a non-inbred population.";
Hum. Mol. Genet. 5:351-354(1996).
[25]
VARIANTS HSCR2 TRP-319 AND LEU-383, AND VARIANT SER-57.
PubMed=8852660; DOI=10.1093/hmg/5.3.355;
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.;
"Heterozygous endothelin receptor B (EDNRB) mutations in isolated
Hirschsprung disease.";
Hum. Mol. Genet. 5:355-357(1996).
[26]
VARIANT HSCR2 ILE-374, AND VARIANT SER-57.
PubMed=8630503; DOI=10.1038/ng0496-445;
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.;
"A homozygous mutation in the endothelin-3 gene associated with a
combined Waardenburg type 2 and Hirschsprung phenotype (Shah-
Waardenburg syndrome).";
Nat. Genet. 12:445-447(1996).
[27]
VARIANT SER-57.
PubMed=9760196; DOI=10.1007/s004390050797;
Svensson P.J., Anvret M., Molander M.L., Nordenskjold A.;
"Phenotypic variation in a family with mutations in two Hirschsprung-
related genes (RET and endothelin receptor B).";
Hum. Genet. 103:145-148(1998).
[28]
VARIANT ASN-305.
PubMed=10874640;
Brooks A.S., Breuning M.H., Osinga J., vd Smagt J.J., Catsman C.E.,
Buys C.H., Meijers C., Hofstra R.M.;
"A consanguineous family with Hirschsprung disease, microcephaly, and
mental retardation (Goldberg-Shprintzen syndrome).";
J. Med. Genet. 36:485-489(1999).
[29]
CHARACTERIZATION OF VARIANTS HSCR2 TRP-319 AND LEU-383, AND
CHARACTERIZATION OF VARIANT SER-57.
PubMed=11471546;
Fuchs S., Amiel J., Claudel S., Lyonnet S., Corvol P., Pinet F.;
"Functional characterization of three mutations of the endothelin B
receptor gene in patients with Hirschsprung's disease: evidence for
selective loss of Gi coupling.";
Mol. Med. 7:115-124(2001).
[30]
INVOLVEMENT IN ABCD SYNDROME.
PubMed=11891690; DOI=10.1002/ajmg.10172;
Verheij J.B., Kunze J., Osinga J., van Essen A.J., Hofstra R.M.;
"ABCD syndrome is caused by a homozygous mutation in the EDNRB gene.";
Am. J. Med. Genet. 108:223-225(2002).
[31]
VARIANT WS4A LEU-292.
PubMed=12189494; DOI=10.1007/s00439-002-0765-8;
Pingault V., Girard M., Bondurand N., Dorkins H., Van Maldergem L.,
Mowat D., Shimotake T., Verma I., Baumann C., Goossens M.;
"SOX10 mutations in chronic intestinal pseudo-obstruction suggest a
complex physiopathological mechanism.";
Hum. Genet. 111:198-206(2002).
[32]
VARIANTS PHE-17; PRO-17; TYR-137; ARG-156 AND 226-TRP--SER-442 DEL,
INVOLVEMENT IN WAARDENBURG SYNDROME 2, SUBCELLULAR LOCATION,
CHARACTERIZATION OF VARIANTS PHE-17; PRO-17; TYR-137; ARG-156 AND
226-TRP--SER-442 DEL, AND CHARACTERIZATION OF VARIANTS HSCR2 ILE-374
AND LEU-383.
PubMed=28236341; DOI=10.1002/humu.23206;
Issa S., Bondurand N., Faubert E., Poisson S., Lecerf L., Nitschke P.,
Deggouj N., Loundon N., Jonard L., David A., Sznajer Y., Blanchet P.,
Marlin S., Pingault V.;
"EDNRB mutations cause Waardenburg syndrome type II in the
heterozygous state.";
Hum. Mutat. 38:581-593(2017).
-!- 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.
{ECO:0000269|PubMed:7536888}.
-!- INTERACTION:
P05305:EDN1; NbExp=2; IntAct=EBI-6624656, EBI-715181;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28236341};
Multi-pass membrane protein. Note=internalized after activation by
endothelins. {ECO:0000269|PubMed:28236341}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A;
IsoId=P24530-1; Sequence=Displayed;
Name=B;
IsoId=P24530-2; Sequence=VSP_001879;
Name=C; Synonyms=Delta-3;
IsoId=P24530-3; Sequence=VSP_001878;
Note=Ref.10 (AAD24541) sequence is in conflict in positions:
79:SGHRTP->RPPDA. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in placental stem villi vessels, but
not in cultured placental villi smooth muscle cells.
{ECO:0000269|PubMed:9284755}.
-!- PTM: Palmitoylation of Cys-402 was confirmed by the palmitoylation
of Cys-402 in a deletion mutant lacking both Cys-403 and Cys-405.
{ECO:0000269|PubMed:9261180}.
-!- DISEASE: Waardenburg syndrome 4A (WS4A) [MIM:277580]: A disorder
characterized by the association of Waardenburg features
(depigmentation and deafness) with the absence of enteric ganglia
in the distal part of the intestine (Hirschsprung disease).
{ECO:0000269|PubMed:12189494, ECO:0000269|PubMed:8634719}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Hirschsprung disease 2 (HSCR2) [MIM:600155]: A disorder
of neural crest development 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.
{ECO:0000269|PubMed:11471546, ECO:0000269|PubMed:28236341,
ECO:0000269|PubMed:8001158, ECO:0000269|PubMed:8630503,
ECO:0000269|PubMed:8852660}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: ABCD syndrome (ABCDS) [MIM:600501]: 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. {ECO:0000269|PubMed:11891690}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Heterozygous mutations in EDNRB may be responsible
for Waardenburg syndrome 2, an autosomal dominant disorder
characterized by sensorineural deafness and pigmentary
disturbances. {ECO:0000269|PubMed:28236341}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Endothelin receptor subfamily. EDNRB sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=BAD92435.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ednrb/";
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EMBL; M74921; AAA58465.1; -; mRNA.
EMBL; D90402; BAA14398.1; -; mRNA.
EMBL; S44866; AAB19411.1; -; mRNA.
EMBL; S57283; AAB25531.1; -; mRNA.
EMBL; D13168; BAA02445.1; -; Genomic_DNA.
EMBL; L06623; AAA52342.1; -; mRNA.
EMBL; X99250; CAA67623.1; -; mRNA.
EMBL; AF114165; AAD24541.1; -; mRNA.
EMBL; AY275463; AAP32295.1; -; mRNA.
EMBL; AB209198; BAD92435.1; ALT_INIT; mRNA.
EMBL; AK290699; BAF83388.1; -; mRNA.
EMBL; AY547312; AAS38516.1; -; Genomic_DNA.
EMBL; AL139002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471093; EAW80573.1; -; Genomic_DNA.
EMBL; CH471093; EAW80575.1; -; Genomic_DNA.
EMBL; BC014472; AAH14472.1; -; mRNA.
EMBL; AJ458188; CAD30645.1; -; Genomic_DNA.
EMBL; AJ458189; CAD30646.1; -; Genomic_DNA.
EMBL; AJ458190; CAD30647.1; -; Genomic_DNA.
EMBL; AJ458191; CAD30648.1; -; Genomic_DNA.
CCDS; CCDS45059.1; -. [P24530-2]
CCDS; CCDS55902.1; -. [P24530-3]
CCDS; CCDS9461.1; -. [P24530-1]
PIR; A46609; JQ1042.
RefSeq; NP_000106.1; NM_000115.4. [P24530-1]
RefSeq; NP_001116131.1; NM_001122659.2. [P24530-1]
RefSeq; NP_001188326.1; NM_001201397.1. [P24530-3]
RefSeq; NP_003982.1; NM_003991.3. [P24530-2]
UniGene; Hs.732046; -.
UniGene; Hs.743195; -.
UniGene; Hs.82002; -.
PDB; 5GLH; X-ray; 2.80 A; A=66-303, A=313-395.
PDB; 5GLI; X-ray; 2.50 A; A=66-303, A=313-395.
PDB; 5X93; X-ray; 2.20 A; A=66-303, A=311-407.
PDB; 5XPR; X-ray; 3.60 A; A=66-303, A=311-407.
PDBsum; 5GLH; -.
PDBsum; 5GLI; -.
PDBsum; 5X93; -.
PDBsum; 5XPR; -.
ProteinModelPortal; P24530; -.
SMR; P24530; -.
BioGrid; 108232; 33.
IntAct; P24530; 1.
STRING; 9606.ENSP00000366416; -.
BindingDB; P24530; -.
ChEMBL; CHEMBL1785; -.
DrugBank; DB06403; Ambrisentan.
DrugBank; DB00559; Bosentan.
DrugBank; DB08932; Macitentan.
DrugBank; DB06268; Sitaxentan.
GuidetoPHARMACOLOGY; 220; -.
iPTMnet; P24530; -.
PhosphoSitePlus; P24530; -.
SwissPalm; P24530; -.
BioMuta; EDNRB; -.
DMDM; 119622; -.
MaxQB; P24530; -.
PaxDb; P24530; -.
PeptideAtlas; P24530; -.
PRIDE; P24530; -.
ProteomicsDB; 54211; -.
ProteomicsDB; 54212; -. [P24530-2]
ProteomicsDB; 54213; -. [P24530-3]
DNASU; 1910; -.
Ensembl; ENST00000334286; ENSP00000335311; ENSG00000136160. [P24530-1]
Ensembl; ENST00000377211; ENSP00000366416; ENSG00000136160. [P24530-3]
Ensembl; ENST00000475537; ENSP00000487082; ENSG00000136160. [P24530-1]
Ensembl; ENST00000626030; ENSP00000486202; ENSG00000136160. [P24530-2]
Ensembl; ENST00000646605; ENSP00000494278; ENSG00000136160. [P24530-1]
Ensembl; ENST00000646607; ENSP00000493527; ENSG00000136160. [P24530-1]
Ensembl; ENST00000646948; ENSP00000493895; ENSG00000136160. [P24530-1]
GeneID; 1910; -.
KEGG; hsa:1910; -.
UCSC; uc001vko.3; human. [P24530-1]
CTD; 1910; -.
DisGeNET; 1910; -.
EuPathDB; HostDB:ENSG00000136160.14; -.
GeneCards; EDNRB; -.
GeneReviews; EDNRB; -.
HGNC; HGNC:3180; EDNRB.
HPA; CAB017842; -.
HPA; HPA027546; -.
MalaCards; EDNRB; -.
MIM; 131244; gene.
MIM; 142623; phenotype.
MIM; 277580; phenotype.
MIM; 600155; phenotype.
MIM; 600501; phenotype.
neXtProt; NX_P24530; -.
OpenTargets; ENSG00000136160; -.
Orphanet; 388; Hirschsprung disease.
Orphanet; 897; Waardenburg-Shah syndrome.
PharmGKB; PA27618; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000119177; -.
HOVERGEN; HBG051443; -.
InParanoid; P24530; -.
KO; K04198; -.
OMA; TAEIMTP; -.
PhylomeDB; P24530; -.
TreeFam; TF331292; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-416476; G alpha (q) signalling events.
SignaLink; P24530; -.
SIGNOR; P24530; -.
GeneWiki; Endothelin_receptor_type_B; -.
GenomeRNAi; 1910; -.
PRO; PR:P24530; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000136160; Expressed in 217 organ(s), highest expression level in spinal cord.
ExpressionAtlas; P24530; baseline and differential.
Genevisible; P24530; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004962; F:endothelin receptor activity; IDA:BHF-UCL.
GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL.
GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
GO; GO:0086100; P:endothelin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0048484; P:enteric nervous system development; ISS:BHF-UCL.
GO; GO:0035645; P:enteric smooth muscle cell differentiation; ISS:BHF-UCL.
GO; GO:0042045; P:epithelial fluid transport; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0048246; P:macrophage chemotaxis; IMP:BHF-UCL.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IMP:BHF-UCL.
GO; GO:0014043; P:negative regulation of neuron maturation; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0060406; P:positive regulation of penile erection; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl.
GO; GO:0007497; P:posterior midgut development; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0031620; P:regulation of fever generation; IEA:Ensembl.
GO; GO:0006885; P:regulation of pH; IEA:Ensembl.
GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:1990839; P:response to endothelin; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0048265; P:response to pain; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0042310; P:vasoconstriction; IMP:BHF-UCL.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
GO; GO:0014826; P:vein smooth muscle contraction; IMP:BHF-UCL.
InterPro; IPR000499; Endthln_rcpt.
InterPro; IPR001112; ETB_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00571; ENDOTHELINBR.
PRINTS; PR00366; ENDOTHELINR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Albinism; Alternative splicing; Cell membrane;
Complete proteome; Deafness; Disease mutation; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Hirschsprung disease;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix; Waardenburg syndrome.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 442 Endothelin receptor type B.
/FTId=PRO_0000012729.
TOPO_DOM 27 101 Extracellular. {ECO:0000255}.
TRANSMEM 102 126 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 127 137 Cytoplasmic. {ECO:0000255}.
TRANSMEM 138 163 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 164 175 Extracellular. {ECO:0000255}.
TRANSMEM 176 197 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 198 218 Cytoplasmic. {ECO:0000255}.
TRANSMEM 219 243 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 244 271 Extracellular. {ECO:0000255}.
TRANSMEM 272 296 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 297 324 Cytoplasmic. {ECO:0000255}.
TRANSMEM 325 350 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 351 362 Extracellular. {ECO:0000255}.
TRANSMEM 363 389 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 390 442 Cytoplasmic. {ECO:0000255}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000250|UniProtKB:P28088}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:P28088}.
MOD_RES 439 439 Phosphotyrosine.
{ECO:0000250|UniProtKB:P28088}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000250|UniProtKB:P28088}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:P28088}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:P28088}.
LIPID 402 402 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9261180}.
LIPID 403 403 S-palmitoyl cysteine. {ECO:0000255}.
LIPID 405 405 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 174 255 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 1 1 M -> MNKSTCLMAAETPSKRWRLHCLAFSQRFVRAGPACS
SREACSSPRAGWNPAGFRLPGRWSPFVALHLVCQIREALKL
RSGHRTPSGAGSSM (in isoform C).
{ECO:0000303|PubMed:10072757}.
/FTId=VSP_001878.
VAR_SEQ 399 442 SCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKY
SSS -> AGPHVGNKLVMLFSVNIECDGTVNQNPTMWPERK
SNNN (in isoform B).
{ECO:0000303|PubMed:8810293}.
/FTId=VSP_001879.
VARIANT 5 5 P -> T (in dbSNP:rs12720160).
{ECO:0000269|Ref.14}.
/FTId=VAR_019285.
VARIANT 7 7 L -> Q (in dbSNP:rs5345).
/FTId=VAR_014675.
VARIANT 17 17 L -> F (polymorphism; no effect on cell
membrane location; dbSNP:rs5346).
{ECO:0000269|PubMed:28236341}.
/FTId=VAR_014676.
VARIANT 17 17 L -> P (probable disease-associated
mutation found in patients with
Waardenburg syndrome 2; loss of cell
membrane location; new cytoplasmic
location). {ECO:0000269|PubMed:28236341}.
/FTId=VAR_078312.
VARIANT 57 57 G -> S (associated with increased
susceptibility for Hirschsprung disease;
sex-dependent gene dosage effect;
dbSNP:rs1801710).
{ECO:0000269|PubMed:11471546,
ECO:0000269|PubMed:8630503,
ECO:0000269|PubMed:8852660,
ECO:0000269|PubMed:9760196}.
/FTId=VAR_003469.
VARIANT 76 76 R -> M (in dbSNP:rs2228271).
/FTId=VAR_024255.
VARIANT 112 112 F -> V (in dbSNP:rs5347).
/FTId=VAR_014677.
VARIANT 137 137 N -> Y (probable disease-associated
mutation found in patients with
Waardenburg syndrome 2; decreased calcium
release upon endothelin 3 exposure; loss
of downstream pathway activation upon
endothelin 3 exposure; no effect on cell
membrane location; no effect on
internalization upon endothelin 3
exposure). {ECO:0000269|PubMed:28236341}.
/FTId=VAR_078313.
VARIANT 156 156 P -> R (probable disease-associated
mutation found in patients with
Waardenburg syndrome 2; loss of cell
membrane location; new cytoplasmic
location). {ECO:0000269|PubMed:28236341}.
/FTId=VAR_078314.
VARIANT 183 183 A -> G (in WS4A; dbSNP:rs104894388).
{ECO:0000269|PubMed:8634719}.
/FTId=VAR_003470.
VARIANT 226 442 Missing (probable disease-associated
mutation found in patients with
Waardenburg syndrome 2; loss of cell
membrane location; new cytoplasmic
location). {ECO:0000269|PubMed:28236341}.
/FTId=VAR_078315.
VARIANT 244 244 T -> M (in dbSNP:rs5350).
/FTId=VAR_014678.
VARIANT 276 276 W -> C (in HSCR2; dbSNP:rs104894387).
{ECO:0000269|PubMed:8001158}.
/FTId=VAR_003471.
VARIANT 292 292 F -> L (in WS4A).
{ECO:0000269|PubMed:12189494}.
/FTId=VAR_015294.
VARIANT 305 305 S -> N (in dbSNP:rs5352).
{ECO:0000269|PubMed:8852659,
ECO:0000269|Ref.14}.
/FTId=VAR_003472.
VARIANT 319 319 R -> W (in HSCR2; sporadic;
dbSNP:rs200363611).
{ECO:0000269|PubMed:11471546,
ECO:0000269|PubMed:8852660}.
/FTId=VAR_003473.
VARIANT 374 374 M -> I (in HSCR2; decreased calcium
release; no effect on cell membrane
location). {ECO:0000269|PubMed:28236341,
ECO:0000269|PubMed:8630503}.
/FTId=VAR_003474.
VARIANT 383 383 P -> L (in HSCR2; familial; loss of cell
membrane location; new cytoplasmic
location). {ECO:0000269|PubMed:11471546,
ECO:0000269|PubMed:28236341,
ECO:0000269|PubMed:8852660}.
/FTId=VAR_003475.
MUTAGEN 402 402 C->S: Abolishes palmitoylation; when
associated with S-403 and S-405.
{ECO:0000269|PubMed:9261180}.
MUTAGEN 403 403 C->S: Abolishes palmitoylation; when
associated with S-402 and S-405.
{ECO:0000269|PubMed:9261180}.
MUTAGEN 405 405 C->S: Abolishes palmitoylation; when
associated with S-402 and S-403.
{ECO:0000269|PubMed:9261180}.
CONFLICT 10 10 R -> P (in Ref. 3; AAB19411).
{ECO:0000305}.
CONFLICT 16 16 V -> L (in Ref. 8). {ECO:0000305}.
CONFLICT 22 24 SRI -> LGV (in Ref. 8). {ECO:0000305}.
CONFLICT 35 35 R -> K (in Ref. 8). {ECO:0000305}.
CONFLICT 45 45 I -> M (in Ref. 12; BAD92435).
{ECO:0000305}.
CONFLICT 58 58 S -> P (in Ref. 13; BAF83388).
{ECO:0000305}.
CONFLICT 140 140 I -> V (in Ref. 8). {ECO:0000305}.
CONFLICT 385 385 A -> V (in Ref. 13; BAF83388).
{ECO:0000305}.
HELIX 93 128 {ECO:0000244|PDB:5X93}.
HELIX 130 133 {ECO:0000244|PDB:5X93}.
TURN 134 137 {ECO:0000244|PDB:5X93}.
HELIX 138 164 {ECO:0000244|PDB:5X93}.
HELIX 171 203 {ECO:0000244|PDB:5X93}.
STRAND 205 207 {ECO:0000244|PDB:5GLI}.
STRAND 212 214 {ECO:0000244|PDB:5X93}.
HELIX 216 239 {ECO:0000244|PDB:5X93}.
STRAND 240 247 {ECO:0000244|PDB:5X93}.
STRAND 250 257 {ECO:0000244|PDB:5X93}.
HELIX 264 281 {ECO:0000244|PDB:5X93}.
HELIX 283 303 {ECO:0000244|PDB:5X93}.
HELIX 313 349 {ECO:0000244|PDB:5X93}.
STRAND 352 356 {ECO:0000244|PDB:5X93}.
HELIX 357 389 {ECO:0000244|PDB:5X93}.
HELIX 391 401 {ECO:0000244|PDB:5X93}.
SEQUENCE 442 AA; 49644 MW; CD4F96CF92C7C51E CRC64;
MQPPPSLCGR ALVALVLACG LSRIWGEERG FPPDRATPLL QTAEIMTPPT KTLWPKGSNA
SLARSLAPAE VPKGDRTAGS PPRTISPPPC QGPIEIKETF KYINTVVSCL VFVLGIIGNS
TLLRIIYKNK CMRNGPNILI ASLALGDLLH IVIDIPINVY KLLAEDWPFG AEMCKLVPFI
QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF
DIITMDYKGS YLRICLLHPV QKTAFMQFYK TAKDWWLFSF YFCLPLAITA FFYTLMTCEM
LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTLY NQNDPNRCEL
LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQSFEE KQSLEEKQSC
LKFKANDHGY DNFRSSNKYS SS


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