ID EDNRB_HUMAN Reviewed; 442 AA. AC P24530; A2A2Z8; A8K3T4; O15343; Q59GB1; Q5W0G9; Q8NHM6; Q8NHM7; Q8NHM8; AC Q8NHM9; Q9UD23; Q9UQK3; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 27-MAR-2024, entry version 244. DE RecName: Full=Endothelin receptor type B {ECO:0000305}; DE Short=ET-B; DE Short=ET-BR; DE AltName: Full=Endothelin receptor non-selective type; DE Flags: Precursor; GN Name=EDNRB {ECO:0000312|HGNC:HGNC:3180}; Synonyms=ETRB; 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 A). RX PubMed=1710450; DOI=10.1016/0006-291x(91)91944-8; RA Nakamuta M., Takayanagi R., Sakai Y., Sakamoto S., Hagiwara H., Mizuno T., RA Saito Y., Hirose S., Yamamoto M., Nawata H.; RT "Cloning and sequence analysis of a cDNA encoding human non-selective type RT of endothelin receptor."; RL Biochem. Biophys. Res. Commun. 177:34-39(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=1648908; DOI=10.1016/0006-291x(91)91806-n; RA Ogawa Y., Nakao K., Arai H., Nakagawa O., Hosoda K., Suga S., Nakanishi S., RA Imura H.; RT "Molecular cloning of a non-isopeptide-selective human endothelin RT receptor."; RL Biochem. Biophys. Res. Commun. 178:248-255(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=1713452; DOI=10.1016/0006-291x(91)90158-4; RA Sakamoto A., Yanagisawa M., Sakurai T., Takuwa Y., Yanagisawa H., RA Masaki T.; RT "Cloning and functional expression of human cDNA for the ETB endothelin RT receptor."; RL Biochem. Biophys. Res. Commun. 178:656-663(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RC TISSUE=Lung; RX PubMed=1282938; DOI=10.1097/00005344-199204002-00002; RA Haendler B., Hechler U., Schleuning W.-D.; RT "Molecular cloning of human endothelin (ET) receptors ETA and ETB."; RL J. Cardiovasc. Pharmacol. 20:S1-S4(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8429023; DOI=10.1016/s0021-9258(18)53717-0; RA Arai H., Nakao K., Takaya K., Hosoda K., Ogawa Y., Nakanishi S., Imura H.; RT "The human endothelin-B receptor gene. Structural organization and RT chromosomal assignment."; RL J. Biol. Chem. 268:3463-3470(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION. RC TISSUE=Prostate; RX PubMed=7536888; RA Webb M.L., Chao C.-C., Rizzo M., Shapiro R.A., Neubauer M., Liu E.C.K., RA Aversa C.R., Brittain R.J., Treiger B.; RT "Cloning and expression of an endothelin receptor subtype B from human RT prostate that mediates contraction."; RL Mol. Pharmacol. 47:730-737(1995). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RC TISSUE=Placenta; RX PubMed=8810293; DOI=10.1074/jbc.271.41.25300; RA Elshourbagy N.A., Adamou J.E., Gagnon A.W., Wu H.L., Pullen M., Nambi P.; RT "Molecular characterization of a novel human endothelin receptor splice RT variant."; RL J. Biol. Chem. 271:25300-25307(1996). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). RX PubMed=10072757; DOI=10.1016/s0378-1119(99)00014-1; RA Tsutsumi M., Liang G., Jones P.A.; RT "Novel endothelin B receptor transcripts with the potential of generating a RT new receptor."; RL Gene 228:43-49(1999). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). 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 [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-5 AND ASN-305. RG NIEHS SNPs program; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [16] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Skin; 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 [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102; 172-196 AND 200-317. RX PubMed=12628594; DOI=10.1016/s0890-8508(03)00003-3; RA Zaahl M.G., du Plessis L., Warnich L., Kotze M.J., Moore S.W.; RT "Significance of novel endothelin-B receptor gene polymorphisms in RT Hirschsprung's disease: predominance of a novel variant (561C/T) in RT patients with co-existing Down's syndrome."; RL Mol. Cell. Probes 17:49-54(2003). RN [19] RP TISSUE SPECIFICITY. 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 [20] RP PALMITOYLATION AT CYS-402; CYS-403 AND CYS-405, AND MUTAGENESIS OF CYS-402; RP CYS-403 AND CYS-405. RX PubMed=9261180; DOI=10.1074/jbc.272.34.21589; RA Okamoto Y., Ninomiya H., Tanioka M., Sakamoto A., Miwa S., Masaki T.; RT "Palmitoylation of human endothelinB. Its critical role in G protein RT coupling and a differential requirement for the cytoplasmic tail by G RT protein subtypes."; RL J. Biol. Chem. 272:21589-21596(1997). RN [21] RP REVIEW ON VARIANTS. RX PubMed=9359036; RA Hofstra R.M.W., Osinga J., Buys C.H.C.M.; RT "Mutations in Hirschsprung disease: when does a mutation contribute to the RT phenotype."; RL Eur. J. Hum. Genet. 5:180-185(1997). RN [22] RP VARIANT HSCR2 CYS-276. RX PubMed=8001158; DOI=10.1016/0092-8674(94)90016-7; RA Puffenberger E.G., Hosoda K., Washington S.S., Nakao K., Dewit D., RA Yanagisawa M., Chakravarti A.; RT "A missense mutation of the endothelin-B receptor gene in multigenic RT Hirschsprung's disease."; RL Cell 79:1257-1266(1994). RN [23] RP VARIANT WS4A GLY-183. RX PubMed=8634719; DOI=10.1093/hmg/4.12.2407; RA Attie T., Till M., Pelet A., Amiel J., Edery P., Boutrand L., Munnich A., RA Lyonnet S.; RT "Mutation of the endothelin-receptor B gene in Waardenburg-Hirschsprung RT disease."; RL Hum. Mol. Genet. 4:2407-2409(1995). RN [24] RP VARIANT ASN-305. RX PubMed=8852659; DOI=10.1093/hmg/5.3.351; RA Auricchio A., Casari G., Staiano A., Ballabio A.; RT "Endothelin-B receptor mutations in patients with isolated Hirschsprung RT disease from a non-inbred population."; RL Hum. Mol. Genet. 5:351-354(1996). RN [25] RP VARIANTS HSCR2 TRP-319 AND LEU-383, AND VARIANT SER-57. RX PubMed=8852660; DOI=10.1093/hmg/5.3.355; RA Amiel J., Attie T., Jan D., Pelet A., Edery P., Bidaud C., Lacombe D., RA Tam P., Simeoni J., Flori E., Nihoul-Fekete C., Munnich A., Lyonnet S.; RT "Heterozygous endothelin receptor B (EDNRB) mutations in isolated RT Hirschsprung disease."; RL Hum. Mol. Genet. 5:355-357(1996). RN [26] RP VARIANT HSCR2 ILE-374, AND VARIANT SER-57. RX PubMed=8630503; DOI=10.1038/ng0496-445; RA Hofstra R.M.W., Tan-Sindhunata G., Wu Y., Kamsteeg E.-J., Stulp R.P., RA van Ravenswaaij-Arts C., Majoor-Krakauer D., Angrist M., Chakravarti A., RA Meijers C., Buys C.H.C.M.; RT "A homozygous mutation in the endothelin-3 gene associated with a combined RT Waardenburg type 2 and Hirschsprung phenotype (Shah-Waardenburg RT syndrome)."; RL Nat. Genet. 12:445-447(1996). RN [27] RP VARIANT SER-57. RX PubMed=9760196; DOI=10.1007/s004390050797; RA Svensson P.J., Anvret M., Molander M.L., Nordenskjold A.; RT "Phenotypic variation in a family with mutations in two Hirschsprung- RT related genes (RET and endothelin receptor B)."; RL Hum. Genet. 103:145-148(1998). RN [28] RP VARIANT ASN-305. RX PubMed=10874640; RA Brooks A.S., Breuning M.H., Osinga J., vd Smagt J.J., Catsman C.E., RA Buys C.H., Meijers C., Hofstra R.M.; RT "A consanguineous family with Hirschsprung disease, microcephaly, and RT mental retardation (Goldberg-Shprintzen syndrome)."; RL J. Med. Genet. 36:485-489(1999). RN [29] RP CHARACTERIZATION OF VARIANTS HSCR2 TRP-319 AND LEU-383, AND RP CHARACTERIZATION OF VARIANT SER-57. RX PubMed=11471546; DOI=10.1007/bf03401945; RA Fuchs S., Amiel J., Claudel S., Lyonnet S., Corvol P., Pinet F.; RT "Functional characterization of three mutations of the endothelin B RT receptor gene in patients with Hirschsprung's disease: evidence for RT selective loss of Gi coupling."; RL Mol. Med. 7:115-124(2001). RN [30] RP INVOLVEMENT IN ABCD SYNDROME. RX PubMed=11891690; DOI=10.1002/ajmg.10172; RA Verheij J.B., Kunze J., Osinga J., van Essen A.J., Hofstra R.M.; RT "ABCD syndrome is caused by a homozygous mutation in the EDNRB gene."; RL Am. J. Med. Genet. 108:223-225(2002). RN [31] RP VARIANT WS4A LEU-292. RX PubMed=12189494; DOI=10.1007/s00439-002-0765-8; RA Pingault V., Girard M., Bondurand N., Dorkins H., Van Maldergem L., RA Mowat D., Shimotake T., Verma I., Baumann C., Goossens M.; RT "SOX10 mutations in chronic intestinal pseudo-obstruction suggest a complex RT physiopathological mechanism."; RL Hum. Genet. 111:198-206(2002). RN [32] RP VARIANTS PHE-17; PRO-17; TYR-137; ARG-156 AND 226-TRP--SER-442 DEL, RP INVOLVEMENT IN WAARDENBURG SYNDROME 2, SUBCELLULAR LOCATION, RP CHARACTERIZATION OF VARIANTS PHE-17; PRO-17; TYR-137; ARG-156 AND RP 226-TRP--SER-442 DEL, AND CHARACTERIZATION OF VARIANTS HSCR2 ILE-374 AND RP LEU-383. RX PubMed=28236341; DOI=10.1002/humu.23206; RA Issa S., Bondurand N., Faubert E., Poisson S., Lecerf L., Nitschke P., RA Deggouj N., Loundon N., Jonard L., David A., Sznajer Y., Blanchet P., RA Marlin S., Pingault V.; RT "EDNRB mutations cause Waardenburg syndrome type II in the heterozygous RT state."; RL Hum. Mutat. 38:581-593(2017). CC -!- FUNCTION: Non-specific receptor for endothelin 1, 2, and 3. Mediates CC its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC {ECO:0000269|PubMed:7536888}. CC -!- INTERACTION: CC P24530; P05305: EDN1; NbExp=2; IntAct=EBI-6624656, EBI-715181; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28236341}; CC Multi-pass membrane protein. Note=internalized after activation by CC endothelins. {ECO:0000269|PubMed:28236341}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=P24530-1; Sequence=Displayed; CC Name=B; CC IsoId=P24530-2; Sequence=VSP_001879; CC Name=C; Synonyms=Delta-3; CC IsoId=P24530-3; Sequence=VSP_001878; CC -!- TISSUE SPECIFICITY: Expressed in placental stem villi vessels, but not CC in cultured placental villi smooth muscle cells. CC {ECO:0000269|PubMed:9284755}. CC -!- PTM: Palmitoylation of Cys-402 was confirmed by the palmitoylation of CC Cys-402 in a deletion mutant lacking both Cys-403 and Cys-405. CC {ECO:0000269|PubMed:9261180}. CC -!- DISEASE: Waardenburg syndrome 4A (WS4A) [MIM:277580]: A disorder CC characterized by the association of Waardenburg features CC (depigmentation and deafness) with the absence of enteric ganglia in CC the distal part of the intestine (Hirschsprung disease). CC {ECO:0000269|PubMed:12189494, ECO:0000269|PubMed:8634719}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Hirschsprung disease 2 (HSCR2) [MIM:600155]: A disorder of CC neural crest development characterized by absence of enteric ganglia CC along a variable length of the intestine. It is the most common cause CC of congenital intestinal obstruction. Early symptoms range from CC complete acute neonatal obstruction, characterized by vomiting, CC abdominal distention and failure to pass stool, to chronic constipation CC in the older child. {ECO:0000269|PubMed:11471546, CC ECO:0000269|PubMed:28236341, ECO:0000269|PubMed:8001158, CC ECO:0000269|PubMed:8630503, ECO:0000269|PubMed:8852660}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: ABCD syndrome (ABCDS) [MIM:600501]: An autosomal recessive CC syndrome characterized by albinism, black lock at temporal occipital CC region, bilateral deafness, aganglionosis of the large intestine and CC total absence of neurocytes and nerve fibers in the small intestine. CC {ECO:0000269|PubMed:11891690}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Note=Heterozygous mutations in EDNRB may be responsible for CC Waardenburg syndrome 2, an autosomal dominant disorder characterized by CC sensorineural deafness and pigmentary disturbances. CC {ECO:0000269|PubMed:28236341}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Endothelin receptor subfamily. EDNRB sub-subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92435.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ednrb/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M74921; AAA58465.1; -; mRNA. DR EMBL; D90402; BAA14398.1; -; mRNA. DR EMBL; S44866; AAB19411.1; -; mRNA. DR EMBL; S57283; AAB25531.1; -; mRNA. DR EMBL; D13168; BAA02445.1; -; Genomic_DNA. DR EMBL; L06623; AAA52342.1; -; mRNA. DR EMBL; X99250; CAA67623.1; -; mRNA. DR EMBL; AF114165; AAD24541.1; -; mRNA. DR EMBL; AY275463; AAP32295.1; -; mRNA. DR EMBL; AB209198; BAD92435.1; ALT_INIT; mRNA. DR EMBL; AK290699; BAF83388.1; -; mRNA. DR EMBL; AY547312; AAS38516.1; -; Genomic_DNA. DR EMBL; AL139002; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471093; EAW80573.1; -; Genomic_DNA. DR EMBL; CH471093; EAW80575.1; -; Genomic_DNA. DR EMBL; BC014472; AAH14472.1; -; mRNA. DR EMBL; AJ458188; CAD30645.1; -; Genomic_DNA. DR EMBL; AJ458189; CAD30646.1; -; Genomic_DNA. DR EMBL; AJ458190; CAD30647.1; -; Genomic_DNA. DR EMBL; AJ458191; CAD30648.1; -; Genomic_DNA. DR CCDS; CCDS45059.1; -. [P24530-2] DR CCDS; CCDS55902.1; -. [P24530-3] DR CCDS; CCDS9461.1; -. [P24530-1] DR PIR; A46609; JQ1042. DR RefSeq; NP_000106.1; NM_000115.4. [P24530-1] DR RefSeq; NP_001116131.1; NM_001122659.2. [P24530-1] DR RefSeq; NP_001188326.1; NM_001201397.1. [P24530-3] DR RefSeq; NP_003982.1; NM_003991.3. [P24530-2] DR PDB; 5GLH; X-ray; 2.80 A; A=66-303, A=313-395. DR PDB; 5GLI; X-ray; 2.50 A; A=66-303, A=313-395. DR PDB; 5X93; X-ray; 2.20 A; A=66-303, A=311-407. DR PDB; 5XPR; X-ray; 3.60 A; A=66-303, A=311-407. DR PDB; 6IGK; X-ray; 2.00 A; A=66-407. DR PDB; 6IGL; X-ray; 2.70 A; A=66-407. DR PDB; 6LRY; X-ray; 3.00 A; A=66-407. DR PDB; 8HBD; EM; 2.99 A; R=27-424. DR PDB; 8HCX; EM; 3.50 A; C=27-424. DR PDBsum; 5GLH; -. DR PDBsum; 5GLI; -. DR PDBsum; 5X93; -. DR PDBsum; 5XPR; -. DR PDBsum; 6IGK; -. DR PDBsum; 6IGL; -. DR PDBsum; 6LRY; -. DR PDBsum; 8HBD; -. DR PDBsum; 8HCX; -. DR AlphaFoldDB; P24530; -. DR EMDB; EMD-34619; -. DR SMR; P24530; -. DR BioGRID; 108232; 35. DR IntAct; P24530; 25. DR MINT; P24530; -. DR STRING; 9606.ENSP00000366416; -. DR BindingDB; P24530; -. DR ChEMBL; CHEMBL1785; -. DR DrugBank; DB06403; Ambrisentan. DR DrugBank; DB00559; Bosentan. DR DrugBank; DB06460; Enrasentan. DR DrugBank; DB06138; IRL-1620. DR DrugBank; DB08932; Macitentan. DR DrugBank; DB06268; Sitaxentan. DR DrugBank; DB06558; Tezosentan. DR DrugCentral; P24530; -. DR GuidetoPHARMACOLOGY; 220; -. DR GlyCosmos; P24530; 1 site, No reported glycans. DR GlyGen; P24530; 1 site. DR iPTMnet; P24530; -. DR PhosphoSitePlus; P24530; -. DR SwissPalm; P24530; -. DR BioMuta; EDNRB; -. DR DMDM; 119622; -. DR EPD; P24530; -. DR jPOST; P24530; -. DR MassIVE; P24530; -. DR MaxQB; P24530; -. DR PaxDb; 9606-ENSP00000366416; -. DR PeptideAtlas; P24530; -. DR ProteomicsDB; 54211; -. [P24530-1] DR ProteomicsDB; 54212; -. [P24530-2] DR ProteomicsDB; 54213; -. [P24530-3] DR ABCD; P24530; 3 sequenced antibodies. DR Antibodypedia; 4509; 535 antibodies from 39 providers. DR DNASU; 1910; -. DR Ensembl; ENST00000377211.8; ENSP00000366416.4; ENSG00000136160.17. [P24530-3] DR Ensembl; ENST00000475537.2; ENSP00000487082.2; ENSG00000136160.17. [P24530-1] DR Ensembl; ENST00000626030.1; ENSP00000486202.1; ENSG00000136160.17. [P24530-2] DR Ensembl; ENST00000646605.1; ENSP00000494278.1; ENSG00000136160.17. [P24530-1] DR Ensembl; ENST00000646607.2; ENSP00000493527.1; ENSG00000136160.17. [P24530-1] DR Ensembl; ENST00000646948.1; ENSP00000493895.1; ENSG00000136160.17. [P24530-1] DR GeneID; 1910; -. DR KEGG; hsa:1910; -. DR MANE-Select; ENST00000646607.2; ENSP00000493527.1; NM_001122659.3; NP_001116131.1. DR UCSC; uc001vko.3; human. [P24530-1] DR AGR; HGNC:3180; -. DR CTD; 1910; -. DR DisGeNET; 1910; -. DR GeneCards; EDNRB; -. DR HGNC; HGNC:3180; EDNRB. DR HPA; ENSG00000136160; Tissue enhanced (placenta). DR MalaCards; EDNRB; -. DR MIM; 131244; gene. DR MIM; 142623; phenotype. DR MIM; 277580; phenotype. DR MIM; 600155; phenotype. DR MIM; 600501; phenotype. DR neXtProt; NX_P24530; -. DR OpenTargets; ENSG00000136160; -. DR Orphanet; 388; Hirschsprung disease. DR Orphanet; 895; Waardenburg syndrome type 2. DR Orphanet; 897; Waardenburg-Shah syndrome. DR PharmGKB; PA27618; -. DR VEuPathDB; HostDB:ENSG00000136160; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01100000263512; -. DR HOGENOM; CLU_009579_28_0_1; -. DR InParanoid; P24530; -. DR OMA; YDQSDPN; -. DR OrthoDB; 2905228at2759; -. DR PhylomeDB; P24530; -. DR TreeFam; TF331292; -. DR PathwayCommons; P24530; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR SignaLink; P24530; -. DR SIGNOR; P24530; -. DR BioGRID-ORCS; 1910; 11 hits in 1158 CRISPR screens. DR ChiTaRS; EDNRB; human. DR GeneWiki; Endothelin_receptor_type_B; -. DR GenomeRNAi; 1910; -. DR Pharos; P24530; Tclin. DR PRO; PR:P24530; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P24530; Protein. DR Bgee; ENSG00000136160; Expressed in parotid gland and 196 other cell types or tissues. DR ExpressionAtlas; P24530; baseline and differential. DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0004962; F:endothelin receptor activity; IDA:BHF-UCL. DR GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL. DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl. DR GO; GO:0032341; P:aldosterone metabolic process; IEA:Ensembl. DR GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl. DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl. DR GO; GO:0160093; P:chordate pharynx development; IEA:Ensembl. DR GO; GO:0048066; P:developmental pigmentation; IBA:GO_Central. DR GO; GO:0086100; P:endothelin receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0048484; P:enteric nervous system development; ISS:BHF-UCL. DR GO; GO:0035645; P:enteric smooth muscle cell differentiation; ISS:BHF-UCL. DR GO; GO:0042045; P:epithelial fluid transport; IEA:Ensembl. DR GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0030202; P:heparin metabolic process; IEA:Ensembl. DR GO; GO:0048246; P:macrophage chemotaxis; IMP:BHF-UCL. DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl. DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0014043; P:negative regulation of neuron maturation; ISS:BHF-UCL. DR GO; GO:0051248; P:negative regulation of protein metabolic process; IMP:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl. DR GO; GO:0097402; P:neuroblast migration; IEA:Ensembl. DR GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0072112; P:podocyte differentiation; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0060406; P:positive regulation of penile erection; IEA:Ensembl. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl. DR GO; GO:0007497; P:posterior midgut development; IEA:Ensembl. DR GO; GO:0071806; P:protein transmembrane transport; IEA:Ensembl. DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0031620; P:regulation of fever generation; IEA:Ensembl. DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl. DR GO; GO:0006885; P:regulation of pH; IEA:Ensembl. DR GO; GO:0097018; P:renal albumin absorption; IEA:Ensembl. DR GO; GO:0035812; P:renal sodium excretion; IEA:Ensembl. DR GO; GO:0070294; P:renal sodium ion absorption; IEA:Ensembl. DR GO; GO:0002001; P:renin secretion into blood stream; IEA:Ensembl. DR GO; GO:1990839; P:response to endothelin; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0048265; P:response to pain; IEA:Ensembl. DR GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl. DR GO; GO:0042310; P:vasoconstriction; IMP:BHF-UCL. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR GO; GO:0014826; P:vein smooth muscle contraction; IMP:BHF-UCL. DR CDD; cd15976; 7tmA_ET-BR; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000499; Endthln_rcpt. DR InterPro; IPR001112; ETB_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR46099:SF3; ENDOTHELIN RECEPTOR TYPE B; 1. DR PANTHER; PTHR46099; G_PROTEIN_RECEP_F1_2 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00571; ENDOTHELINBR. DR PRINTS; PR00366; ENDOTHELINR. DR PRINTS; PR00237; GPCRRHODOPSN. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P24530; HS. PE 1: Evidence at protein level; KW 3D-structure; Albinism; Alternative splicing; Cell membrane; Deafness; KW Disease variant; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Hirschsprung disease; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Receptor; Reference proteome; Signal; Transducer; Transmembrane; KW Transmembrane helix; Waardenburg syndrome. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..442 FT /note="Endothelin receptor type B" FT /id="PRO_0000012729" FT TOPO_DOM 27..101 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 102..126 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 127..137 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 138..163 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 164..175 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 176..197 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 198..218 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 219..243 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 244..271 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 272..296 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 297..324 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 325..350 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 351..362 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 363..389 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 390..442 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 69..88 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28088" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28088" FT MOD_RES 439 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P28088" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28088" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28088" FT MOD_RES 442 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28088" FT LIPID 402 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:9261180" FT LIPID 403 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" FT LIPID 405 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" FT CARBOHYD 59 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 174..255 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VAR_SEQ 1 FT /note="M -> MNKSTCLMAAETPSKRWRLHCLAFSQRFVRAGPACSSREACSSPRAG FT WNPAGFRLPGRWSPFVALHLVCQIREALKLRSGHRTPSGAGSSM (in isoform FT C)" FT /evidence="ECO:0000303|PubMed:10072757" FT /id="VSP_001878" FT VAR_SEQ 399..442 FT /note="SCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS -> AGPH FT VGNKLVMLFSVNIECDGTVNQNPTMWPERKSNNN (in isoform B)" FT /evidence="ECO:0000303|PubMed:8810293" FT /id="VSP_001879" FT VARIANT 5 FT /note="P -> T (in dbSNP:rs12720160)" FT /evidence="ECO:0000269|Ref.14" FT /id="VAR_019285" FT VARIANT 7 FT /note="L -> Q (in dbSNP:rs5345)" FT /id="VAR_014675" FT VARIANT 17 FT /note="L -> F (no effect on cell membrane location; FT dbSNP:rs5346)" FT /evidence="ECO:0000269|PubMed:28236341" FT /id="VAR_014676" FT VARIANT 17 FT /note="L -> P (found in patients with Waardenburg syndrome FT 2; likely pathogenic; loss of cell membrane location; new FT cytoplasmic location)" FT /evidence="ECO:0000269|PubMed:28236341" FT /id="VAR_078312" FT VARIANT 57 FT /note="G -> S (probable risk factor for Hirschsprung FT disease; sex-dependent gene dosage effect; FT dbSNP:rs1801710)" FT /evidence="ECO:0000269|PubMed:11471546, FT ECO:0000269|PubMed:8630503, ECO:0000269|PubMed:8852660, FT ECO:0000269|PubMed:9760196" FT /id="VAR_003469" FT VARIANT 76 FT /note="R -> M (in dbSNP:rs2228271)" FT /id="VAR_024255" FT VARIANT 112 FT /note="F -> V (in dbSNP:rs5347)" FT /id="VAR_014677" FT VARIANT 137 FT /note="N -> Y (found in patients with Waardenburg syndrome FT 2; likely pathogenic; decreased calcium release upon FT endothelin 3 exposure; loss of downstream pathway FT activation upon endothelin 3 exposure; no effect on cell FT membrane location; no effect on internalization upon FT endothelin 3 exposure)" FT /evidence="ECO:0000269|PubMed:28236341" FT /id="VAR_078313" FT VARIANT 156 FT /note="P -> R (found in patients with Waardenburg syndrome FT 2; likely pathogenic; loss of cell membrane location; new FT cytoplasmic location)" FT /evidence="ECO:0000269|PubMed:28236341" FT /id="VAR_078314" FT VARIANT 183 FT /note="A -> G (in WS4A; dbSNP:rs104894388)" FT /evidence="ECO:0000269|PubMed:8634719" FT /id="VAR_003470" FT VARIANT 226..442 FT /note="Missing (found in patients with Waardenburg syndrome FT 2; likely pathogenic; loss of cell membrane location; new FT cytoplasmic location)" FT /evidence="ECO:0000269|PubMed:28236341" FT /id="VAR_078315" FT VARIANT 244 FT /note="T -> M (in dbSNP:rs5350)" FT /id="VAR_014678" FT VARIANT 276 FT /note="W -> C (in HSCR2; dbSNP:rs104894387)" FT /evidence="ECO:0000269|PubMed:8001158" FT /id="VAR_003471" FT VARIANT 292 FT /note="F -> L (in WS4A)" FT /evidence="ECO:0000269|PubMed:12189494" FT /id="VAR_015294" FT VARIANT 305 FT /note="S -> N (in dbSNP:rs5352)" FT /evidence="ECO:0000269|PubMed:8852659, ECO:0000269|Ref.14" FT /id="VAR_003472" FT VARIANT 319 FT /note="R -> W (in HSCR2; sporadic; dbSNP:rs200363611)" FT /evidence="ECO:0000269|PubMed:11471546, FT ECO:0000269|PubMed:8852660" FT /id="VAR_003473" FT VARIANT 374 FT /note="M -> I (in HSCR2; decreased calcium release; no FT effect on cell membrane location)" FT /evidence="ECO:0000269|PubMed:28236341, FT ECO:0000269|PubMed:8630503" FT /id="VAR_003474" FT VARIANT 383 FT /note="P -> L (in HSCR2; familial; loss of cell membrane FT location; new cytoplasmic location)" FT /evidence="ECO:0000269|PubMed:11471546, FT ECO:0000269|PubMed:28236341, ECO:0000269|PubMed:8852660" FT /id="VAR_003475" FT MUTAGEN 402 FT /note="C->S: Abolishes palmitoylation; when associated with FT S-403 and S-405." FT /evidence="ECO:0000269|PubMed:9261180" FT MUTAGEN 403 FT /note="C->S: Abolishes palmitoylation; when associated with FT S-402 and S-405." FT /evidence="ECO:0000269|PubMed:9261180" FT MUTAGEN 405 FT /note="C->S: Abolishes palmitoylation; when associated with FT S-402 and S-403." FT /evidence="ECO:0000269|PubMed:9261180" FT CONFLICT 10 FT /note="R -> P (in Ref. 3; AAB19411)" FT /evidence="ECO:0000305" FT CONFLICT 16 FT /note="V -> L (in Ref. 8)" FT /evidence="ECO:0000305" FT CONFLICT 22..24 FT /note="SRI -> LGV (in Ref. 8)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="R -> K (in Ref. 8)" FT /evidence="ECO:0000305" FT CONFLICT 45 FT /note="I -> M (in Ref. 12; BAD92435)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="S -> P (in Ref. 13; BAF83388)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="I -> V (in Ref. 8)" FT /evidence="ECO:0000305" FT CONFLICT 385 FT /note="A -> V (in Ref. 13; BAF83388)" FT /evidence="ECO:0000305" FT HELIX 98..128 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 135..164 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 170..204 FT /evidence="ECO:0007829|PDB:6IGK" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:6IGK" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:5X93" FT HELIX 216..232 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 234..239 FT /evidence="ECO:0007829|PDB:6IGK" FT STRAND 240..247 FT /evidence="ECO:0007829|PDB:6IGK" FT STRAND 250..257 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 264..281 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 283..310 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 313..349 FT /evidence="ECO:0007829|PDB:6IGK" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:5GLI" FT TURN 355..357 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 358..389 FT /evidence="ECO:0007829|PDB:6IGK" FT HELIX 391..401 FT /evidence="ECO:0007829|PDB:6IGK" FT CONFLICT P24530-3:79..84 FT /note="SGHRTP -> RPPDA (in Ref. 10; AAD24541)" FT /evidence="ECO:0000305" SQ 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 //