EDNRB_HUMAN
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 03-AUG-2022, entry version 235.
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/";
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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 PDBsum; 5GLH; -.
DR PDBsum; 5GLI; -.
DR PDBsum; 5X93; -.
DR PDBsum; 5XPR; -.
DR PDBsum; 6IGK; -.
DR PDBsum; 6IGL; -.
DR PDBsum; 6LRY; -.
DR AlphaFoldDB; P24530; -.
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 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; P24530; -.
DR PeptideAtlas; P24530; -.
DR PRIDE; 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; 475 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 CTD; 1910; -.
DR DisGeNET; 1910; -.
DR GeneCards; EDNRB; -.
DR HGNC; HGNC:3180; EDNRB.
DR HPA; ENSG00000136160; Tissue enhanced (brain, 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; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_28_0_1; -.
DR InParanoid; P24530; -.
DR OMA; GFDMITT; -.
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 1074 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 194 other tissues.
DR ExpressionAtlas; P24530; baseline and differential.
DR Genevisible; P24530; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
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:0007568; P:aging; 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: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:0007249; P:I-kappaB kinase/NF-kappaB signaling; 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:0060465; P:pharynx 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: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:0035815; P:positive regulation of renal sodium excretion; 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:0051930; P:regulation of sensory perception of pain; 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:0019233; P:sensory perception of pain; 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 InterPro; IPR000499; Endthln_rcpt.
DR InterPro; IPR001112; ETB_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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 (probable disease-associated variant found in
FT patients with Waardenburg syndrome 2; loss of cell membrane
FT location; new cytoplasmic location)"
FT /evidence="ECO:0000269|PubMed:28236341"
FT /id="VAR_078312"
FT VARIANT 57
FT /note="G -> S (associated with increased susceptibility for
FT Hirschsprung 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 (probable disease-associated variant found in
FT patients with Waardenburg syndrome 2; decreased calcium
FT release upon endothelin 3 exposure; loss of downstream
FT pathway activation upon endothelin 3 exposure; no effect on
FT cell 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 (probable disease-associated variant found in
FT patients with Waardenburg syndrome 2; loss of cell membrane
FT location; new 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 (probable disease-associated variant found
FT in patients with Waardenburg syndrome 2; loss of cell
FT membrane location; new 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
