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Amiloride-sensitive sodium channel subunit beta (Beta-NaCH) (Epithelial Na( ) channel subunit beta) (Beta-ENaC) (ENaCB) (Nonvoltage-gated sodium channel 1 subunit beta) (SCNEB)

 SCNNB_HUMAN             Reviewed;         640 AA.
P51168; C5HTZ2; O60891; Q96KG2; Q9UJ32; Q9UMU5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 180.
RecName: Full=Amiloride-sensitive sodium channel subunit beta;
AltName: Full=Beta-NaCH;
AltName: Full=Epithelial Na(+) channel subunit beta;
Short=Beta-ENaC;
Short=ENaCB;
AltName: Full=Nonvoltage-gated sodium channel 1 subunit beta;
AltName: Full=SCNEB;
Name=SCNN1B;
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 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Lung;
PubMed=7490094; DOI=10.1006/geno.1995.1188;
Voilley N., Bassilana F., Mignon C., Merscher S., Mattei M.-G.,
Carle G.F., Lazdunski M., Barbry P.;
"Cloning, chromosomal localization, and physical linkage of the beta
and gamma subunits (SCNN1B and SCNN1G) of the human epithelial
amiloride-sensitive sodium channel.";
Genomics 28:560-565(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-336, FUNCTION,
GLYCOSYLATION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=7762608;
McDonald F.J., Snyder P.M., Price M.P., Welsh M.J.;
"Cloning and expression of the beta- and gamma-subunits of the human
epithelial sodium channel.";
Am. J. Physiol. 268:C1157-C1163(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Epithelium;
PubMed=9813171; DOI=10.1006/bbrc.1998.9625;
Saxena A., Hanukoglu I., Strautnieks S.S., Thompson R.J.,
Gardiner R.M., Hanukoglu A.;
"Gene structure of the human amiloride-sensitive epithelial sodium
channel beta subunit.";
Biochem. Biophys. Res. Commun. 252:208-213(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12107247; DOI=10.1210/jc.87.7.3344;
Saxena A., Hanukoglu I., Saxena D., Thompson R.J., Gardiner R.M.,
Hanukoglu A.;
"Novel mutations responsible for autosomal recessive multisystem
pseudohypoaldosteronism and sequence variants in epithelial sodium
channel alpha-, beta-, and gamma-subunit genes.";
J. Clin. Endocrinol. Metab. 87:3344-3350(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Lung, and Testis;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-259.
PubMed=10493829; DOI=10.1006/geno.1999.5927;
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
Harris P.C., Venter J.C., Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from
human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-56 (ISOFORM 2).
TISSUE=Kidney;
Thomas C.P., Auerbach S.D., Loftus R.W., Li X., Itani O.A.;
"Separate promoters of the human epithelial sodium channel beta
subunit direct expression of alternate transcripts that encode N-
terminal protein variants.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 515-640.
PubMed=7954808; DOI=10.1016/0092-8674(94)90250-X;
Shimkets R.A., Warnock D.G., Bositis C.M., Nelson-Williams C.,
Hansson J.H., Schambelan M., Gill J.R., Ulick S., Milora R.V.,
Findling J.W., Canessa C.M., Rossier B.C., Lifton R.P.;
"Liddle's syndrome: heritable human hypertension caused by mutations
in the beta subunit of the epithelial sodium channel.";
Cell 79:407-414(1994).
[10]
DEFINITION OF DIFFERENT FORMS OF PSEUDOHYPOALDOSTERONISM TYPE 1.
PubMed=1939532; DOI=10.1210/jcem-73-5-936;
Hanukoglu A.;
"Type I pseudohypoaldosteronism includes two clinically and
genetically distinct entities with either renal or multiple target
organ defects.";
J. Clin. Endocrinol. Metab. 73:936-944(1991).
[11]
SUBUNIT.
PubMed=7499195; DOI=10.1074/jbc.270.46.27411;
Waldmann R., Champigny G., Bassilana F., Voilley N., Lazdunski M.;
"Molecular cloning and functional expression of a novel amiloride-
sensitive Na+ channel.";
J. Biol. Chem. 270:27411-27414(1995).
[12]
INTERACTION WITH WWP1 AND WWP2.
PubMed=9169421; DOI=10.1074/jbc.272.23.14611;
Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B.,
Kay B.K., Fowlkes D.M.;
"Identification of novel human WW domain-containing proteins by
cloning of ligand targets.";
J. Biol. Chem. 272:14611-14616(1997).
[13]
INTERACTION WITH NEDD4 AND NEDD4L.
PubMed=11244092; DOI=10.1074/jbc.C000906200;
Harvey K.F., Dinudom A., Cook D.I., Kumar S.;
"The Nedd4-like protein KIAA0439 is a potential regulator of the
epithelial sodium channel.";
J. Biol. Chem. 276:8597-8601(2001).
[14]
INTERACTION WITH NEDD4 AND WWP2.
PubMed=12167593; DOI=10.1152/ajprenal.00080.2002;
McDonald F.J., Western A.H., McNeil J.D., Thomas B.C., Olson D.R.,
Snyder P.M.;
"Ubiquitin-protein ligase WWP2 binds to and downregulates the
epithelial Na(+) channel.";
Am. J. Physiol. 283:F431-F436(2002).
[15]
SUBUNIT.
PubMed=16423824; DOI=10.1074/jbc.M512293200;
Ji H.L., Su X.F., Kedar S., Li J., Barbry P., Smith P.R., Matalon S.,
Benos D.J.;
"Delta-subunit confers novel biophysical features to alpha beta gamma-
human epithelial sodium channel (ENaC) via a physical interaction.";
J. Biol. Chem. 281:8233-8241(2006).
[16]
GENOTYPE-PHENOTYPE RELATIONSHIPS IN PHA1B, AND LONG-TERM EFFECTS OF
MUTATIONS ON PHA1B.
PubMed=18634878; DOI=10.1016/j.jsbmb.2008.06.013;
Hanukoglu A., Edelheit O., Shriki Y., Gizewska M., Dascal N.,
Hanukoglu I.;
"Renin-aldosterone response, urinary Na/K ratio and growth in
pseudohypoaldosteronism patients with mutations in epithelial sodium
channel (ENaC) subunit genes.";
J. Steroid Biochem. Mol. Biol. 111:268-274(2008).
[17]
INVOLVEMENT IN PSEUDOHYPOALDOSTERONISM TYPE 1.
PubMed=20064610; DOI=10.1016/j.jsbmb.2010.01.002;
Edelheit O., Hanukoglu I., Shriki Y., Tfilin M., Dascal N., Gillis D.,
Hanukoglu A.;
"Truncated beta epithelial sodium channel (ENaC) subunits responsible
for multi-system pseudohypoaldosteronism support partial activity of
ENaC.";
J. Steroid Biochem. Mol. Biol. 119:84-88(2010).
[18]
TISSUE SPECIFICITY.
PubMed=22207244; DOI=10.1007/s00418-011-0904-1;
Enuka Y., Hanukoglu I., Edelheit O., Vaknine H., Hanukoglu A.;
"Epithelial sodium channels (ENaC) are uniformly distributed on motile
cilia in the oviduct and the respiratory airways.";
Histochem. Cell Biol. 137:339-353(2012).
[19]
INTERACTION WITH PCSK9.
PubMed=22493497; DOI=10.1074/jbc.M112.363382;
Sharotri V., Collier D.M., Olson D.R., Zhou R., Snyder P.M.;
"Regulation of epithelial sodium channel trafficking by proprotein
convertase subtilisin/kexin type 9 (PCSK9).";
J. Biol. Chem. 287:19266-19274(2012).
[20]
INTERACTION WITH BPIFA1, AND GLYCOSYLATION.
PubMed=24124190; DOI=10.1152/ajplung.00103.2013;
Hobbs C.A., Blanchard M.G., Alijevic O., Tan C.D., Kellenberger S.,
Bencharit S., Cao R., Kesimer M., Walton W.G., Henderson A.G.,
Redinbo M.R., Stutts M.J., Tarran R.;
"Identification of the SPLUNC1 ENaC-inhibitory domain yields novel
strategies to treat sodium hyperabsorption in cystic fibrosis airway
epithelial cultures.";
Am. J. Physiol. 305:L990-L1001(2013).
[21]
REVIEW.
PubMed=23547933;
Alvarez de la Rosa D., Navarro-Gonzalez J.F., Giraldez T.;
"ENaC modulators and renal disease.";
Curr. Mol. Pharmacol. 6:35-43(2013).
[22]
INTERACTION WITH BPIFA1.
PubMed=24043776; DOI=10.1073/pnas.1311999110;
Garland A.L., Walton W.G., Coakley R.D., Tan C.D., Gilmore R.C.,
Hobbs C.A., Tripathy A., Clunes L.A., Bencharit S., Stutts M.J.,
Betts L., Redinbo M.R., Tarran R.;
"Molecular basis for pH-dependent mucosal dehydration in cystic
fibrosis airways.";
Proc. Natl. Acad. Sci. U.S.A. 110:15973-15978(2013).
[23]
PHYLOGENETIC ANALYSIS, AND NOMENCLATURE.
PubMed=26772908; DOI=10.1016/j.gene.2015.12.061;
Hanukoglu I., Hanukoglu A.;
"Epithelial sodium channel (ENaC) family: Phylogeny, structure-
function, tissue distribution, and associated inherited diseases.";
Gene 579:95-132(2016).
[24]
VARIANT LIDLS LEU-616.
PubMed=7550319; DOI=10.1038/ng0995-76;
Hansson J.H., Nelson-Williams C., Suzuki H., Schild L., Shimkets R.A.,
Lu Y., Canessa C.M., Iwasaki T., Rossier B.C., Lifton R.P.;
"Hypertension caused by a truncated epithelial sodium channel gamma
subunit: genetic heterogeneity of Liddle syndrome.";
Nat. Genet. 11:76-82(1995).
[25]
VARIANT LIDLS LEU-616.
PubMed=8524790; DOI=10.1073/pnas.92.25.11495;
Hansson J.H., Schild L., Lu Y., Wilson T.A., Gautschi I.,
Shimkets R.A., Nelson-Williams C., Rossier B.C., Lifton R.P.;
"A de novo missense mutation of the beta subunit of the epithelial
sodium channel causes hypertension and Liddle syndrome, identifying a
proline-rich segment critical for regulation of channel activity.";
Proc. Natl. Acad. Sci. U.S.A. 92:11495-11499(1995).
[26]
VARIANT LIDLS HIS-620, AND CHARACTERIZATION OF VARIANT LIDLS HIS-620.
PubMed=8601645; DOI=10.1172/JCI118606;
Tamura H., Schild L., Enomoto N., Matsui N., Marumo F., Rossier B.C.;
"Liddle disease caused by a missense mutation of beta subunit of the
epithelial sodium channel gene.";
J. Clin. Invest. 97:1780-1784(1996).
[27]
VARIANT PHA1B SER-37.
PubMed=8589714; DOI=10.1038/ng0396-248;
Chang S.S., Grunder S., Hanukoglu A., Roesler A., Mathew P.M.,
Hanukoglu I., Schild L., Lu Y., Shimkets R.A., Nelson-Williams C.,
Rossier B.C., Lifton R.P.;
"Mutations in subunits of the epithelial sodium channel cause salt
wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1.";
Nat. Genet. 12:248-253(1996).
[28]
VARIANTS MET-434; VAL-442; SER-589; MET-594; HIS-597; CYS-624 AND
GLY-632.
PubMed=9674649; DOI=10.1161/01.HYP.32.1.129;
Persu A., Barbry P., Bassilana F., Houot A.-M., Mengual R.,
Lazdunski M., Corvol P., Jeunemaitre X.;
"Genetic analysis of the beta subunit of the epithelial Na+ channel in
essential hypertension.";
Hypertension 32:129-137(1998).
[29]
VARIANT LIDLS SER-617.
PubMed=9626162; DOI=10.1210/jcem.83.6.5030;
Inoue J., Iwaoka T., Tokunaga H., Takamune K., Naomi S., Araki M.,
Takahama K., Yamaguchi K., Tomita K.;
"A family with Liddle's syndrome caused by a new missense mutation in
the beta subunit of the epithelial sodium channel.";
J. Clin. Endocrinol. Metab. 83:2210-2213(1998).
[30]
VARIANTS LIDLS LEU-616 AND SER-616.
PubMed=9794716; DOI=10.1097/00004872-199816080-00008;
Uehara Y., Sasaguri M., Kinoshita A., Tsuji E., Kiyose H.,
Taniguchi H., Noda K., Ideishi M., Inoue J., Tomita K., Arakawa K.;
"Genetic analysis of the epithelial sodium channel in Liddle's
syndrome.";
J. Hypertens. 16:1131-1135(1998).
[31]
VARIANT PRO-336.
PubMed=10404817; DOI=10.1210/jcem.84.7.5857;
Arai K., Zachman K., Shibasaki T., Chrousos G.P.;
"Polymorphisms of amiloride-sensitive sodium channel subunits in five
sporadic cases of pseudohypoaldosteronism: do they have pathologic
potential?";
J. Clin. Endocrinol. Metab. 84:2434-2437(1999).
[32]
VARIANT GLN-563, AND ASSOCIATION WITH HYPERTENSION.
PubMed=12714866; DOI=10.1097/00004872-200305000-00016;
Rayner B.L., Owen E.P., King J.A., Soule S.G., Vreede H., Opie L.H.,
Marais D., Davidson J.S.;
"A new mutation, R563Q, of the beta subunit of the epithelial sodium
channel associated with low-renin, low-aldosterone hypertension.";
J. Hypertens. 21:921-926(2003).
[33]
INVOLVEMENT IN PSEUDOHYPOALDOSTERONISM TYPE 1.
PubMed=15853823; DOI=10.1111/j.1365-2265.2005.02255.x;
Edelheit O., Hanukoglu I., Gizewska M., Kandemir N.,
Tenenbaum-Rakover Y., Yurdakoek M., Zajaczek S., Hanukoglu A.;
"Novel mutations in epithelial sodium channel (ENaC) subunit genes and
phenotypic expression of multisystem pseudohypoaldosteronism.";
Clin. Endocrinol. (Oxf.) 62:547-553(2005).
[34]
VARIANTS BESC1 CYS-82; LEU-267; SER-294 AND LYS-539, AND
CHARACTERIZATION OF VARIANTS BESC1 LEU-267; SER-294 AND LYS-539.
PubMed=16207733; DOI=10.1093/hmg/ddi374;
Sheridan M.B., Fong P., Groman J.D., Conrad C., Flume P., Diaz R.,
Harris C., Knowles M., Cutting G.R.;
"Mutations in the beta-subunit of the epithelial Na+ channel in
patients with a cystic fibrosis-like syndrome.";
Hum. Mol. Genet. 14:3493-3498(2005).
[35]
VARIANT LIDLS ARG-618.
PubMed=15483078; DOI=10.1210/jc.2004-1027;
Furuhashi M., Kitamura K., Adachi M., Miyoshi T., Wakida N., Ura N.,
Shikano Y., Shinshi Y., Sakamoto K., Hayashi M., Satoh N.,
Nishitani T., Tomita K., Shimamoto K.;
"Liddle's syndrome caused by a novel mutation in the proline-rich PY
motif of the epithelial sodium channel beta-subunit.";
J. Clin. Endocrinol. Metab. 90:340-344(2005).
[36]
VARIANTS [LARGE SCALE ANALYSIS] VAL-311; VAL-314 AND VAL-387.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[37]
VARIANTS BESC1 CYS-82; SER-288 AND THR-369.
PubMed=18507830; DOI=10.1186/1465-9921-9-46;
Fajac I., Viel M., Sublemontier S., Hubert D., Bienvenu T.;
"Could a defective epithelial sodium channel lead to bronchiectasis.";
Respir. Res. 9:46-46(2008).
[38]
VARIANT BESC1 MET-348, AND VARIANT VAL-442.
PubMed=19017867; DOI=10.1378/chest.08-2246;
Mutesa L., Azad A.K., Verhaeghe C., Segers K., Vanbellinghen J.F.,
Ngendahayo L., Rusingiza E.K., Mutwa P.R., Rulisa S., Koulischer L.,
Cassiman J.J., Cuppens H., Bours V.;
"Genetic analysis of Rwandan patients with cystic fibrosis-like
symptoms: identification of novel cystic fibrosis transmembrane
conductance regulator and epithelial sodium channel gene variants.";
Chest 135:1233-1242(2009).
-!- FUNCTION: Sodium permeable non-voltage-sensitive ion channel
inhibited by the diuretic amiloride. Mediates the electrodiffusion
of the luminal sodium (and water, which follows osmotically)
through the apical membrane of epithelial cells. Plays an
essential role in electrolyte and blood pressure homeostasis, but
also in airway surface liquid homeostasis, which is important for
proper clearance of mucus. Controls the reabsorption of sodium in
kidney, colon, lung and sweat glands. Also plays a role in taste
perception. {ECO:0000269|PubMed:7762608,
ECO:0000303|PubMed:7490094}.
-!- ENZYME REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
{ECO:0000250|UniProtKB:Q9WU38}.
-!- SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B
and a gamma/SCNN1G subunit. An additional delta/SCNN1D subunit
exists only in some organisms and can replace the alpha/SCNN1A
subunit to form an alternative channel with specific properties
(PubMed:7499195, PubMed:16423824). Interacts with NEDD4 (via WW
domains) (PubMed:11244092, PubMed:12167593). Interacts with NEDD4L
(via WW domains) (PubMed:11244092). Interacts with WWP1 (via WW
domains) (PubMed:9169421). Interacts with WWP2 (via WW domains)
(PubMed:9169421, PubMed:12167593). Interacts with the full-length
immature form of PCSK9 (pro-PCSK9) (PubMed:22493497). Interacts
(N-glycosylated) with BPIFA1; the interaction is direct and
inhibits the proteolytic processing of SCNN1A and SCNN1G and the
activation of ENaC (PubMed:24124190, PubMed:24043776).
{ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:12167593,
ECO:0000269|PubMed:16423824, ECO:0000269|PubMed:22493497,
ECO:0000269|PubMed:24043776, ECO:0000269|PubMed:24124190,
ECO:0000269|PubMed:7499195, ECO:0000269|PubMed:9169421}.
-!- INTERACTION:
P46934:NEDD4; NbExp=4; IntAct=EBI-2547187, EBI-726944;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000305|PubMed:7490094}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial
cells. {ECO:0000305|PubMed:7490094}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P51168-1; Sequence=Displayed;
Name=2;
IsoId=P51168-2; Sequence=VSP_007724;
-!- TISSUE SPECIFICITY: Detected in placenta, lung and kidney
(PubMed:7762608). Expressed in kidney (at protein level)
(PubMed:22207244). {ECO:0000269|PubMed:22207244,
ECO:0000269|PubMed:7762608}.
-!- PTM: Phosphorylated on serine and threonine residues. Aldosterone
and insulin increase the basal level of phosphorylation.
{ECO:0000250|UniProtKB:P37090}.
-!- PTM: N-glycosylated. N-glycosylation is required for interaction
with BPIFA1. {ECO:0000269|PubMed:24124190,
ECO:0000269|PubMed:7762608}.
-!- DISEASE: Pseudohypoaldosteronism 1, autosomal recessive (PHA1B)
[MIM:264350]: A rare salt wasting disease resulting from target
organ unresponsiveness to mineralocorticoids. PHA1B is a severe
form involving multiple organ systems, and characterized by an
often fulminant presentation in the neonatal period with
dehydration, hyponatremia, hyperkalemia, metabolic acidosis,
failure to thrive and weight loss. {ECO:0000269|PubMed:8589714}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. The degree of channel function
impairment differentially affects the renin-aldosterone system and
urinary Na/K ratios, resulting in distinct genotype-phenotype
relationships in PHA1 patients. Loss-of-function mutations are
associated with a severe clinical course and age-dependent
hyperactivation of the renin-aldosterone system. This feature is
not observed in patients with missense mutations that reduce but
do not eliminate channel function. Markedly reduced channel
activity results in impaired linear growth and delayed puberty
(PubMed:18634878). {ECO:0000269|PubMed:18634878}.
-!- DISEASE: Liddle syndrome (LIDLS) [MIM:177200]: An autosomal
dominant disorder characterized by hypertension, hypokalemic
alkalosis, and suppression of plasma renin activity and
aldosterone secretion. {ECO:0000269|PubMed:15483078,
ECO:0000269|PubMed:7550319, ECO:0000269|PubMed:8524790,
ECO:0000269|PubMed:8601645, ECO:0000269|PubMed:9626162,
ECO:0000269|PubMed:9794716}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Bronchiectasis with or without elevated sweat chloride 1
(BESC1) [MIM:211400]: A debilitating respiratory disease
characterized by chronic, abnormal dilatation of the bronchi and
other cystic fibrosis-like symptoms in the absence of known causes
of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary
dyskinesia, common variable immunodeficiency, foreign body
obstruction). Clinical features include sub-normal lung function,
sinopulmonary infections, chronic productive cough, excessive
sputum production, and elevated sweat chloride in some cases.
{ECO:0000269|PubMed:16207733, ECO:0000269|PubMed:18507830,
ECO:0000269|PubMed:19017867}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. SCNN1B subfamily. {ECO:0000305}.
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EMBL; X87159; CAA60632.1; -; mRNA.
EMBL; L36593; AAA75459.1; -; mRNA.
EMBL; AJ005383; CAA06508.2; -; Genomic_DNA.
EMBL; AJ005384; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005385; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005386; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005387; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005388; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005389; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005390; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005391; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005392; CAA06508.2; JOINED; Genomic_DNA.
EMBL; AJ005393; CAA06508.2; JOINED; Genomic_DNA.
EMBL; FJ515831; ACS13723.1; -; Genomic_DNA.
EMBL; BC036352; AAH36352.2; -; mRNA.
EMBL; AC130452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF260226; AAK49394.1; -; mRNA.
EMBL; U16023; AAA67036.1; -; Genomic_DNA.
CCDS; CCDS10609.1; -. [P51168-1]
PIR; I51915; I51915.
RefSeq; NP_000327.2; NM_000336.2. [P51168-1]
UniGene; Hs.414614; -.
ProteinModelPortal; P51168; -.
BioGrid; 112242; 18.
CORUM; P51168; -.
ELM; P51168; -.
IntAct; P51168; 4.
MINT; MINT-198733; -.
STRING; 9606.ENSP00000345751; -.
ChEMBL; CHEMBL2107836; -.
DrugBank; DB00594; Amiloride.
DrugBank; DB00384; Triamterene.
GuidetoPHARMACOLOGY; 739; -.
TCDB; 1.A.6.1.1; the epithelial na(+) channel (enac) family.
iPTMnet; P51168; -.
PhosphoSitePlus; P51168; -.
BioMuta; SCNN1B; -.
DMDM; 8928561; -.
PaxDb; P51168; -.
PeptideAtlas; P51168; -.
PRIDE; P51168; -.
DNASU; 6338; -.
Ensembl; ENST00000307331; ENSP00000302874; ENSG00000168447. [P51168-2]
Ensembl; ENST00000343070; ENSP00000345751; ENSG00000168447. [P51168-1]
GeneID; 6338; -.
KEGG; hsa:6338; -.
UCSC; uc002dln.3; human. [P51168-1]
CTD; 6338; -.
DisGeNET; 6338; -.
EuPathDB; HostDB:ENSG00000168447.10; -.
GeneCards; SCNN1B; -.
H-InvDB; HIX0026943; -.
HGNC; HGNC:10600; SCNN1B.
HPA; HPA015612; -.
MalaCards; SCNN1B; -.
MIM; 177200; phenotype.
MIM; 211400; phenotype.
MIM; 264350; phenotype.
MIM; 600760; gene.
neXtProt; NX_P51168; -.
OpenTargets; ENSG00000168447; -.
Orphanet; 171876; Generalized pseudohypoaldosteronism type 1.
Orphanet; 60033; Idiopathic bronchiectasis.
Orphanet; 526; Liddle syndrome.
PharmGKB; PA306; -.
eggNOG; KOG4294; Eukaryota.
eggNOG; ENOG410ZNFK; LUCA.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000236286; -.
HOVERGEN; HBG058435; -.
InParanoid; P51168; -.
KO; K04825; -.
OMA; CNDTQYK; -.
OrthoDB; EOG091G0KW6; -.
PhylomeDB; P51168; -.
TreeFam; TF330663; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
SIGNOR; P51168; -.
GeneWiki; SCNN1B; -.
GenomeRNAi; 6338; -.
PRO; PR:P51168; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000168447; -.
CleanEx; HS_SCNN1B; -.
ExpressionAtlas; P51168; baseline and differential.
Genevisible; P51168; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0034706; C:sodium channel complex; IDA:UniProtKB.
GO; GO:0015280; F:ligand-gated sodium channel activity; TAS:ProtInc.
GO; GO:0050699; F:WW domain binding; IPI:BHF-UCL.
GO; GO:0007588; P:excretion; TAS:ProtInc.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0050891; P:multicellular organismal water homeostasis; IDA:UniProtKB.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
GO; GO:0055078; P:sodium ion homeostasis; IDA:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006814; P:sodium ion transport; TAS:ProtInc.
InterPro; IPR001873; ENaC.
InterPro; IPR004724; ENaC_chordates.
InterPro; IPR020903; ENaC_CS.
PANTHER; PTHR11690; PTHR11690; 1.
Pfam; PF00858; ASC; 1.
PRINTS; PR01078; AMINACHANNEL.
TIGRFAMs; TIGR00859; ENaC; 1.
PROSITE; PS01206; ASC; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Cytoplasmic vesicle; Disease mutation; Glycoprotein; Ion channel;
Ion transport; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Sensory transduction; Sodium; Sodium channel;
Sodium transport; Taste; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 640 Amiloride-sensitive sodium channel
subunit beta.
/FTId=PRO_0000181268.
TOPO_DOM 1 50 Cytoplasmic.
{ECO:0000250|UniProtKB:P37089}.
TRANSMEM 51 71 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 72 532 Extracellular.
{ECO:0000250|UniProtKB:P37089}.
TRANSMEM 533 553 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 554 640 Cytoplasmic.
{ECO:0000250|UniProtKB:P37089}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WU38}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WU38}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 1 M -> MLLHINPAYLFKLLHGFPPWIMPTDGNLGDKNFQMG
KPGHREGATM (in isoform 2).
{ECO:0000303|Ref.8}.
/FTId=VSP_007724.
VARIANT 37 37 G -> S (in PHA1B; dbSNP:rs137852706).
{ECO:0000269|PubMed:8589714}.
/FTId=VAR_007127.
VARIANT 82 82 S -> C (in BESC1; dbSNP:rs35731153).
{ECO:0000269|PubMed:16207733,
ECO:0000269|PubMed:18507830}.
/FTId=VAR_062401.
VARIANT 267 267 P -> L (in BESC1; decreased channel
activity; dbSNP:rs137852709).
{ECO:0000269|PubMed:16207733}.
/FTId=VAR_062402.
VARIANT 288 288 N -> S (in BESC1; dbSNP:rs137852712).
{ECO:0000269|PubMed:18507830}.
/FTId=VAR_062403.
VARIANT 294 294 G -> S (in BESC1; increased channel
activity; dbSNP:rs72654338).
{ECO:0000269|PubMed:16207733}.
/FTId=VAR_062404.
VARIANT 311 311 A -> V (in a colorectal cancer sample;
somatic mutation; dbSNP:rs777888930).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036480.
VARIANT 314 314 A -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036481.
VARIANT 336 336 A -> P. {ECO:0000269|PubMed:10404817,
ECO:0000269|PubMed:7762608}.
/FTId=VAR_015836.
VARIANT 348 348 V -> M (in BESC1; dbSNP:rs61759921).
{ECO:0000269|PubMed:19017867}.
/FTId=VAR_062405.
VARIANT 369 369 P -> T (in BESC1; dbSNP:rs137852711).
{ECO:0000269|PubMed:18507830}.
/FTId=VAR_062406.
VARIANT 387 387 L -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036482.
VARIANT 434 434 V -> M (in dbSNP:rs201330438).
{ECO:0000269|PubMed:9674649}.
/FTId=VAR_015837.
VARIANT 442 442 G -> V (in dbSNP:rs1799980).
{ECO:0000269|PubMed:19017867,
ECO:0000269|PubMed:9674649}.
/FTId=VAR_014891.
VARIANT 539 539 E -> K (in BESC1; decreased channel
activity; dbSNP:rs137852710).
{ECO:0000269|PubMed:16207733}.
/FTId=VAR_062407.
VARIANT 563 563 R -> Q (associated with hypertension in
South African Black; dbSNP:rs149868979).
{ECO:0000269|PubMed:12714866}.
/FTId=VAR_026519.
VARIANT 589 589 G -> S (in dbSNP:rs61759926).
{ECO:0000269|PubMed:9674649}.
/FTId=VAR_015838.
VARIANT 594 594 T -> M (in dbSNP:rs1799979).
{ECO:0000269|PubMed:9674649}.
/FTId=VAR_014892.
VARIANT 597 597 R -> H (in dbSNP:rs140945152).
{ECO:0000269|PubMed:9674649}.
/FTId=VAR_015839.
VARIANT 616 616 P -> L (in LIDLS; dbSNP:rs387906402).
{ECO:0000269|PubMed:7550319,
ECO:0000269|PubMed:8524790,
ECO:0000269|PubMed:9794716}.
/FTId=VAR_007128.
VARIANT 616 616 P -> S (in LIDLS).
{ECO:0000269|PubMed:9794716}.
/FTId=VAR_007129.
VARIANT 617 617 P -> S (in LIDLS; dbSNP:rs137852708).
{ECO:0000269|PubMed:9626162}.
/FTId=VAR_026520.
VARIANT 618 618 P -> R (in LIDLS; dbSNP:rs137852705).
{ECO:0000269|PubMed:15483078}.
/FTId=VAR_026521.
VARIANT 620 620 Y -> H (in LIDLS; constitutive channel
activation; dbSNP:rs137852707).
{ECO:0000269|PubMed:8601645}.
/FTId=VAR_026522.
VARIANT 624 624 R -> C (in dbSNP:rs372132399).
{ECO:0000269|PubMed:9674649}.
/FTId=VAR_015840.
VARIANT 632 632 E -> G. {ECO:0000269|PubMed:9674649}.
/FTId=VAR_015841.
CONFLICT 41 41 I -> T (in Ref. 6; AAH36352).
{ECO:0000305}.
CONFLICT 314 314 A -> G (in Ref. 1; CAA60632).
{ECO:0000305}.
CONFLICT 498 498 Y -> F (in Ref. 2; AAA75459).
{ECO:0000305}.
SEQUENCE 640 AA; 72659 MW; 5249867F0A960E0C CRC64;
MHVKKYLLKG LHRLQKGPGY TYKELLVWYC DNTNTHGPKR IICEGPKKKA MWFLLTLLFA
ALVCWQWGIF IRTYLSWEVS VSLSVGFKTM DFPAVTICNA SPFKYSKIKH LLKDLDELME
AVLERILAPE LSHANATRNL NFSIWNHTPL VLIDERNPHH PMVLDLFGDN HNGLTSSSAS
EKICNAHGCK MAMRLCSLNR TQCTFRNFTS ATQALTEWYI LQATNIFAQV PQQELVEMSY
PGEQMILACL FGAEPCNYRN FTSIFYPHYG NCYIFNWGMT EKALPSANPG TEFGLKLILD
IGQEDYVPFL ASTAGVRLML HEQRSYPFIR DEGIYAMSGT ETSIGVLVDK LQRMGEPYSP
CTVNGSEVPV QNFYSDYNTT YSIQACLRSC FQDHMIRNCN CGHYLYPLPR GEKYCNNRDF
PDWAHCYSDL QMSVAQRETC IGMCKESCND TQYKMTISMA DWPSEASEDW IFHVLSQERD
QSTNITLSRK GIVKLNIYFQ EFNYRTIEES AANNIVWLLS NLGGQFGFWM GGSVLCLIEF
GEIIIDFVWI TIIKLVALAK SLRQRRAQAS YAGPPPTVAE LVEAHTNFGF QPDTAPRSPN
TGPYPSEQAL PIPGTPPPNY DSLRLQPLDV IESDSEGDAI


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