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Amiloride-sensitive sodium channel subunit alpha (Alpha-NaCH) (Epithelial Na( ) channel subunit alpha) (Alpha-ENaC) (ENaCA) (Nonvoltage-gated sodium channel 1 subunit alpha) (SCNEA)

 SCNNA_HUMAN             Reviewed;         669 AA.
P37088; A5X2U9; B4E2Q5; C5HTZ0; O43271; Q6GSQ6; Q9UM64;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
25-OCT-2017, entry version 185.
RecName: Full=Amiloride-sensitive sodium channel subunit alpha;
AltName: Full=Alpha-NaCH;
AltName: Full=Epithelial Na(+) channel subunit alpha;
Short=Alpha-ENaC;
Short=ENaCA;
AltName: Full=Nonvoltage-gated sodium channel 1 subunit alpha;
AltName: Full=SCNEA;
Name=SCNN1A; Synonyms=SCNN1;
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), AND FUNCTION.
TISSUE=Lung;
PubMed=8278374; DOI=10.1073/pnas.91.1.247;
Voilley N., Lingueglia E., Champigny G., Mattei M.-G., Waldmann R.,
Lazdunski M., Barbry P.;
"The lung amiloride-sensitive Na+ channel: biophysical properties,
pharmacology, ontogenesis, and molecular cloning.";
Proc. Natl. Acad. Sci. U.S.A. 91:247-251(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Kidney;
PubMed=8023962;
McDonald F.J., Snyder P.M., McCray P.B. Jr., Welsh M.J.;
"Cloning, expression, and tissue distribution of a human amiloride-
sensitive Na+ channel.";
Am. J. Physiol. 266:L728-L734(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9654208; DOI=10.1007/s004390050743;
Ludwig M., Bolkenius U., Wickert L., Marynen P., Bidlingmaier F.;
"Structural organisation of the gene encoding the alpha-subunit of the
human amiloride-sensitive epithelial sodium channel.";
Hum. Genet. 102:576-581(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10447117; DOI=10.1203/00006450-199908000-00014;
Chow Y.H., Wang Y., Plumb J., O'Brodovich H., Hu J.;
"Hormonal regulation and genomic organization of the human amiloride-
sensitive epithelial sodium channel alpha subunit gene.";
Pediatr. Res. 46:208-214(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-663.
TISSUE=Nasal epithelium;
PubMed=17766193; DOI=10.1016/j.jcf.2007.07.012;
Bangel N., Dahlhoff C., Sobczak K., Weber W.M., Kusche-Vihrog K.;
"Upregulated expression of ENaC in human CF nasal epithelium.";
J. Cyst. Fibros. 7:197-205(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-663.
TISSUE=Colon, and Lung;
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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50, AND ALTERNATIVE SPLICING
(ISOFORMS 1 AND 2).
TISSUE=Kidney;
PubMed=9612219;
Thomas C.P., Auerbach S.D., Stokes J.B., Volk K.A.;
"5' heterogeneity in epithelial sodium channel alpha-subunit mRNA
leads to distinct NH2-terminal variant proteins.";
Am. J. Physiol. 274:C1312-C1323(1998).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50 (ISOFORMS 1 AND 2), AND
INDUCTION.
TISSUE=Placenta;
PubMed=11266509; DOI=10.1210/mend.15.4.0620;
Mick V.E., Itani O.A., Loftus R.W., Husted R.F., Schmidt T.J.,
Thomas C.P.;
"The alpha-subunit of the epithelial sodium channel is an aldosterone-
induced transcript in mammalian collecting ducts, and this
transcriptional response is mediated via distinct cis-elements in the
5'-flanking region of the gene.";
Mol. Endocrinol. 15:575-588(2001).
[13]
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).
[14]
ALTERNATIVE SPLICING (ISOFORMS 1; 3; 4 AND 5), AND TISSUE SPECIFICITY.
PubMed=9575806;
Tucker J.K., Tamba K., Lee Y.-J., Shen L.-L., Warnock D.G., Oh Y.;
"Cloning and functional studies of splice variants of the alpha-
subunit of the amiloride-sensitive Na+ channel.";
Am. J. Physiol. 274:C1081-C1089(1998).
[15]
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).
[16]
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).
[17]
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).
[18]
PROTEOLYTIC PROCESSING.
PubMed=18650438; DOI=10.1074/jbc.M803931200;
Carattino M.D., Hughey R.P., Kleyman T.R.;
"Proteolytic processing of the epithelial sodium channel gamma subunit
has a dominant role in channel activation.";
J. Biol. Chem. 283:25290-25295(2008).
[19]
GENOTYPE-PHENOTYPE RELATIONSHIPS IN PHA1B, LONG-TERM EFFECTS OF
MUTATIONS ON PHA1B, VARIANT PHA1B CYS-327, AND CHARACTERIZATION OF
VARIANT PHA1B CYS-327.
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).
[20]
SUBCELLULAR LOCATION, AND 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).
[21]
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).
[22]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[23]
INTERACTION WITH NEDD4.
PubMed=23665454; DOI=10.1016/j.bbapap.2013.04.031;
Bobby R., Medini K., Neudecker P., Lee T.V., Brimble M.A.,
McDonald F.J., Lott J.S., Dingley A.J.;
"Structure and dynamics of human Nedd4-1 WW3 in complex with the
alphaENaC PY motif.";
Biochim. Biophys. Acta 1834:1632-1641(2013).
[24]
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).
[25]
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).
[26]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=28130590; DOI=10.1007/s00418-016-1535-3;
Hanukoglu I., Boggula V.R., Vaknine H., Sharma S., Kleyman T.,
Hanukoglu A.;
"Expression of epithelial sodium channel (ENaC) and CFTR in the human
epidermis and epidermal appendages.";
Histochem. Cell Biol. 147:733-748(2017).
[27]
VARIANTS THR-334; PHE-618 AND ALA-663.
PubMed=10523338; DOI=10.1161/01.HYP.34.4.631;
Ambrosius W.T., Bloem L.J., Zhou L., Rebhun J.F., Snyder P.M.,
Wagner M.A., Guo C., Pratt J.H.;
"Genetic variants in the epithelial sodium channel in relation to
aldosterone and potassium excretion and risk for hypertension.";
Hypertension 34:631-637(1999).
[28]
ERRATUM.
Ambrosius W.T., Bloem L.J., Zhou L., Rebhun J.F., Snyder P.M.,
Wagner M.A., Guo C., Pratt J.H.;
Hypertension 41:1E-1E(2003).
[29]
INTERACTION WITH NEDD4 AND NEDD4L.
PubMed=11696533; DOI=10.1074/jbc.C100623200;
Snyder P.M., Olson D.R., Thomas B.C.;
"Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated
inhibition of the epithelial Na+ channel.";
J. Biol. Chem. 277:5-8(2002).
[30]
VARIANT ALA-663.
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).
[31]
VARIANT PHA1B LEU-562, AND VARIANT ARG-493.
PubMed=10586178; DOI=10.1016/S0022-3476(99)70094-6;
Schaedel C., Marthinsen L., Kristoffersson A.-C., Kornfalt R.,
Nilsson K.O., Orlenius B., Holmberg L.;
"Lung symptoms in pseudohypoaldosteronism type 1 are associated with
deficiency of the alpha-subunit of the epithelial sodium channel.";
J. Pediatr. 135:739-745(1999).
[32]
VARIANT ALA-663.
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).
[33]
VARIANT ALA-663, AND ASSOCIATION OF VARIANT ARG-493 WITH RISK FOR
ISCHEMIC CEREBROVASCULAR EVENTS.
PubMed=15734793; DOI=10.1373/clinchem.2004.046276;
Hsieh K., Lalouschek W., Schillinger M., Endler G., Reisinger M.,
Janisiw M., Lang W., Cheng S., Wagner O., Mannhalter C.;
"Impact of alphaENaC polymorphisms on the risk of ischemic
cerebrovascular events: a multicenter case-control study.";
Clin. Chem. 51:952-956(2005).
[34]
VARIANT PHA1B CYS-327.
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).
[35]
VARIANT TRP-181.
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).
[36]
VARIANTS BESC2 LEU-61 AND ILE-114, VARIANTS TRP-181; THR-334; ARG-493
AND ALA-663, CHARACTERIZATION OF VARIANTS BESC2 LEU-61 AND ILE-114,
AND CHARACTERIZATION OF VARIANTS TRP-181; THR-334 AND ARG-493.
PubMed=19462466; DOI=10.1002/humu.21011;
Azad A.K., Rauh R., Vermeulen F., Jaspers M., Korbmacher J.,
Boissier B., Bassinet L., Fichou Y., des Georges M., Stanke F.,
De Boeck K., Dupont L., Balascakova M., Hjelte L., Lebecque P.,
Radojkovic D., Castellani C., Schwartz M., Stuhrmann M., Schwarz M.,
Skalicka V., de Monestrol I., Girodon E., Ferec C., Claustres M.,
Tuemmler B., Cassiman J.-J., Korbmacher C., Cuppens H.;
"Mutations in the amiloride-sensitive epithelial sodium channel in
patients with cystic fibrosis-like disease.";
Hum. Mutat. 30:1093-1103(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 eccrine sweat glands. Also plays a role in
taste perception. {ECO:0000269|PubMed:24124190,
ECO:0000269|PubMed:8278374}.
-!- ENZYME REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
{ECO:0000250|UniProtKB:Q61180}.
-!- 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
(By similarity). Interacts with NEDD4 (via WW domains)
(PubMed:11244092, PubMed:11696533, PubMed:12167593,
PubMed:23665454). Interacts with NEDD4L (via WW domains)
(PubMed:11244092, PubMed:11696533). Interacts with WWP1 (via WW
domains) (PubMed:9169421). Interacts with WWP2 (via WW domains)
(PubMed:12167593, PubMed:9169421). Interacts with the full-length
immature form of PCSK9 (pro-PCSK9) (PubMed:22493497).
{ECO:0000250|UniProtKB:Q61180, ECO:0000269|PubMed:11244092,
ECO:0000269|PubMed:11696533, ECO:0000269|PubMed:12167593,
ECO:0000269|PubMed:22493497, ECO:0000269|PubMed:23665454,
ECO:0000269|PubMed:9169421}.
-!- INTERACTION:
P51170:SCNN1G; NbExp=3; IntAct=EBI-7845444, EBI-2547354;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:22207244, ECO:0000269|PubMed:28130590}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P37089}. Cell
projection, cilium {ECO:0000269|PubMed:22207244}. Cytoplasmic
granule {ECO:0000269|PubMed:28130590}. Cytoplasm
{ECO:0000269|PubMed:28130590}. Note=In the oviduct and bronchus,
located on cilia in multi-ciliated cells. In endometrial non-
ciliated epithelial cells, restricted to apical surfaces. In
epidermis, located nearly uniformly in the cytoplasm in a granular
distribution (PubMed:28130590). In sebaceous glands, observed only
in the cytoplasmic space in between the lipid vesicles
(PubMed:28130590). In eccrine sweat glands, mainly located at the
apical surface of the cells facing the lumen (PubMed:28130590). In
skin, in arrector pili muscle cells and in adipocytes, located in
the cytoplasm and colocalized with actin fibers (PubMed:28130590).
{ECO:0000269|PubMed:22207244, ECO:0000269|PubMed:24124190,
ECO:0000269|PubMed:28130590}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Alpha ENAC1;
IsoId=P37088-1; Sequence=Displayed;
Name=2; Synonyms=Alpha ENAC2;
IsoId=P37088-2; Sequence=VSP_007719;
Name=3; Synonyms=Alpha ENACx;
IsoId=P37088-3; Sequence=VSP_007720, VSP_007721;
Note=Does not give rise to amiloride-sensitive ion current. May
be produced at very low levels due to a premature stop codon in
the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4; Synonyms=Alpha ENAC-19;
IsoId=P37088-4; Sequence=VSP_007722;
Note=Amiloride-sensitive ion current is nearly abolished.;
Name=5; Synonyms=Alpha ENAC+22;
IsoId=P37088-5; Sequence=VSP_007723;
Note=Does not give rise to amiloride-sensitive ion current.;
Name=6;
IsoId=P37088-6; Sequence=VSP_043667;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the female reproductive tract,
from the fimbrial end of the fallopian tube to the endometrium (at
protein level) (PubMed:22207244). Expressed in kidney (at protein
level). In the respiratory tract, expressed in the bronchial
epithelium (at protein level). Highly expressed in lung. Detected
at intermediate levels in pancreas and liver, and at low levels in
heart and placenta (PubMed:22207244). in skin, expressed in
keratinocytes, melanocytes and Merkel cells of the epidermal sub-
layers, stratum basale, stratum spinosum and stratum granulosum
(at protein level) (PubMed:28130590). Expressed in the outer root
sheath of the hair follicles (at protein level) (PubMed:28130590).
Detected in both peripheral and central cells of the sebaceous
gland (at protein level) (PubMed:28130590). Expressed by eccrine
sweat glands (at protein level) (PubMed:28130590). In skin, also
expressed by arrector pili muscle cells and intradermal adipocytes
(PubMed:28130590). Isoform 1 and isoform 2 predominate in all
tissues. Expression of isoform 3, isoform 4 and isoform 5 is very
low or not detectable, except in lung and heart (PubMed:9575806).
{ECO:0000269|PubMed:22207244, ECO:0000269|PubMed:28130590,
ECO:0000269|PubMed:9575806}.
-!- INDUCTION: By aldosterone. {ECO:0000269|PubMed:11266509}.
-!- PTM: Ubiquitinated; this targets individual subunits for
endocytosis and proteasome-mediated degradation.
{ECO:0000250|UniProtKB:P37089}.
-!- PTM: ENaC cleavage by furin, and subsequently by prostasin
(PRSS8), leads to a stepwise increase in the open probability of
the channel as a result of release of the alpha and gamma subunit
inhibitory tracts, respectively. Interaction of ENaC subunit
SCNN1B with BPIFA1 protects ENaC against proteolytic activation.
{ECO:0000269|PubMed:18650438}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P37089}.
-!- 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:10586178,
ECO:0000269|PubMed:15853823, ECO:0000269|PubMed:18634878}.
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: Bronchiectasis with or without elevated sweat chloride 2
(BESC2) [MIM:613021]: 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:19462466}. 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. SCNN1A subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH06526.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X76180; CAA53773.1; -; mRNA.
EMBL; L29007; AAA21813.1; -; Genomic_DNA.
EMBL; Z92978; CAB07505.1; -; Genomic_DNA.
EMBL; Z92979; CAB07505.1; JOINED; Genomic_DNA.
EMBL; Z92980; CAB07505.1; JOINED; Genomic_DNA.
EMBL; Z92981; CAB07505.1; JOINED; Genomic_DNA.
EMBL; AF060913; AAD28355.1; -; Genomic_DNA.
EMBL; AF060910; AAD28355.1; JOINED; Genomic_DNA.
EMBL; AF060911; AAD28355.1; JOINED; Genomic_DNA.
EMBL; AF060912; AAD28355.1; JOINED; Genomic_DNA.
EMBL; DQ402522; ABD72218.1; -; mRNA.
EMBL; AK304379; BAG65217.1; -; mRNA.
EMBL; FJ515830; ACS13721.1; -; Genomic_DNA.
EMBL; AC005840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471116; EAW88804.1; -; Genomic_DNA.
EMBL; BC006526; AAH06526.2; ALT_INIT; mRNA.
EMBL; BC062613; AAH62613.1; -; mRNA.
EMBL; U81961; AAC31773.1; -; Genomic_DNA.
EMBL; U81961; AAC31774.1; -; Genomic_DNA.
CCDS; CCDS53738.1; -. [P37088-2]
CCDS; CCDS53739.1; -. [P37088-6]
CCDS; CCDS8543.1; -. [P37088-1]
PIR; A49585; A49585.
RefSeq; NP_001029.1; NM_001038.5. [P37088-1]
RefSeq; NP_001153047.1; NM_001159575.1. [P37088-6]
RefSeq; NP_001153048.1; NM_001159576.1. [P37088-2]
UniGene; Hs.591047; -.
PDB; 2M3O; NMR; -; P=638-648.
PDBsum; 2M3O; -.
ProteinModelPortal; P37088; -.
SMR; P37088; -.
BioGrid; 112241; 23.
CORUM; P37088; -.
ELM; P37088; -.
IntAct; P37088; 3.
MINT; MINT-198663; -.
STRING; 9606.ENSP00000353292; -.
BindingDB; P37088; -.
ChEMBL; CHEMBL1791; -.
DrugBank; DB00594; Amiloride.
DrugBank; DB00384; Triamterene.
GuidetoPHARMACOLOGY; 738; -.
TCDB; 1.A.6.1.1; the epithelial na(+) channel (enac) family.
iPTMnet; P37088; -.
PhosphoSitePlus; P37088; -.
BioMuta; SCNN1A; -.
DMDM; 585966; -.
EPD; P37088; -.
PaxDb; P37088; -.
PeptideAtlas; P37088; -.
PRIDE; P37088; -.
Ensembl; ENST00000228916; ENSP00000228916; ENSG00000111319. [P37088-1]
Ensembl; ENST00000360168; ENSP00000353292; ENSG00000111319. [P37088-2]
Ensembl; ENST00000543768; ENSP00000438739; ENSG00000111319. [P37088-6]
GeneID; 6337; -.
KEGG; hsa:6337; -.
UCSC; uc001qnw.3; human. [P37088-1]
CTD; 6337; -.
DisGeNET; 6337; -.
EuPathDB; HostDB:ENSG00000111319.12; -.
GeneCards; SCNN1A; -.
HGNC; HGNC:10599; SCNN1A.
HPA; HPA012743; -.
MalaCards; SCNN1A; -.
MIM; 264350; phenotype.
MIM; 600228; gene.
MIM; 613021; phenotype.
neXtProt; NX_P37088; -.
OpenTargets; ENSG00000111319; -.
Orphanet; 171876; Generalized pseudohypoaldosteronism type 1.
Orphanet; 60033; Idiopathic bronchiectasis.
PharmGKB; PA305; -.
eggNOG; KOG4294; Eukaryota.
eggNOG; ENOG410ZNFK; LUCA.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000236286; -.
HOVERGEN; HBG058435; -.
InParanoid; P37088; -.
KO; K04824; -.
OMA; VEYCDYR; -.
OrthoDB; EOG091G0KW6; -.
PhylomeDB; P37088; -.
TreeFam; TF330663; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
SIGNOR; P37088; -.
ChiTaRS; SCNN1A; human.
GeneWiki; SCNN1A; -.
GenomeRNAi; 6337; -.
PRO; PR:P37088; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111319; -.
CleanEx; HS_SCNN1A; -.
ExpressionAtlas; P37088; baseline and differential.
Genevisible; P37088; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0031514; C:motile cilium; 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; IEA:InterPro.
GO; GO:0050699; F:WW domain binding; IPI:BHF-UCL.
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.
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;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Disease mutation; Glycoprotein;
Ion channel; Ion transport; Membrane; Polymorphism;
Reference proteome; Sensory transduction; Sodium; Sodium channel;
Sodium transport; Taste; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 669 Amiloride-sensitive sodium channel
subunit alpha.
/FTId=PRO_0000181261.
TOPO_DOM 1 85 Cytoplasmic.
{ECO:0000250|UniProtKB:P37089}.
TRANSMEM 86 106 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 107 562 Extracellular.
{ECO:0000250|UniProtKB:P37089}.
TRANSMEM 563 583 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 584 669 Cytoplasmic.
{ECO:0000250|UniProtKB:P37089}.
VAR_SEQ 1 1 M -> MGMARGSLTRVPGVMGEGTQGPELSLDPDPCSPQST
PGLMKGNKLEEQDPRPLQPIPGLM (in isoform 2).
{ECO:0000305}.
/FTId=VSP_007719.
VAR_SEQ 1 1 M -> MSSIKGNKLEEQDPRPLQPIPGLM (in isoform
6). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_043667.
VAR_SEQ 229 245 CNQNKSDCFYQTYSSGV -> ELLSLPPPDVWKLLYFG
(in isoform 3). {ECO:0000305}.
/FTId=VSP_007720.
VAR_SEQ 246 669 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_007721.
VAR_SEQ 327 345 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_007722.
VAR_SEQ 454 454 G -> GQVRSLTPVIPALWEAEAGGSRG (in isoform
5). {ECO:0000305}.
/FTId=VSP_007723.
VARIANT 61 61 F -> L (in BESC2; hypoactive mutation
resulting in reduction of protein
expression and a significant decrease of
amiloride-sensitive sodium currents;
dbSNP:rs61758859).
{ECO:0000269|PubMed:19462466}.
/FTId=VAR_060793.
VARIANT 114 114 V -> I (in BESC2; hyperactive mutation
resulting in a significant increase of
amiloride-sensitive sodium currents;
dbSNP:rs61759861).
{ECO:0000269|PubMed:19462466}.
/FTId=VAR_060794.
VARIANT 181 181 R -> W (functional polymorphism;
significant increase of amiloride-
sensitive sodium currents;
dbSNP:rs55797039).
{ECO:0000269|PubMed:16207733,
ECO:0000269|PubMed:19462466}.
/FTId=VAR_060795.
VARIANT 327 327 G -> C (in PHA1B; results in a
significant reduction of channel function
as compared to wild-type; significantly
lowers both Li+ and Na+ ion currents).
{ECO:0000269|PubMed:15853823,
ECO:0000269|PubMed:18634878}.
/FTId=VAR_026518.
VARIANT 334 334 A -> T (functional polymorphism;
significant decrease of amiloride-
sensitive sodium currents;
dbSNP:rs11542844).
{ECO:0000269|PubMed:10523338,
ECO:0000269|PubMed:19462466}.
/FTId=VAR_060796.
VARIANT 402 402 P -> H (in dbSNP:rs13306616).
/FTId=VAR_052035.
VARIANT 493 493 W -> R (functional polymorphism; results
in a 4-fold increase of amiloride-
sensitive sodium currents; found in BESC2
patients at higher frequency than in
controls; associated with an increased
risk for ischemic cerebrovascular events;
dbSNP:rs5742912).
{ECO:0000269|PubMed:10586178,
ECO:0000269|PubMed:19462466}.
/FTId=VAR_015833.
VARIANT 562 562 S -> L (in PHA1B; dbSNP:rs137852635).
{ECO:0000269|PubMed:10586178}.
/FTId=VAR_015834.
VARIANT 573 573 V -> I (in dbSNP:rs59142484).
/FTId=VAR_060797.
VARIANT 618 618 C -> F (in dbSNP:rs3741913).
{ECO:0000269|PubMed:10523338}.
/FTId=VAR_022142.
VARIANT 663 663 T -> A (in dbSNP:rs2228576).
{ECO:0000269|PubMed:10404817,
ECO:0000269|PubMed:10523338,
ECO:0000269|PubMed:12107247,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15734793,
ECO:0000269|PubMed:17766193,
ECO:0000269|PubMed:19462466}.
/FTId=VAR_015835.
HELIX 644 647 {ECO:0000244|PDB:2M3O}.
SEQUENCE 669 AA; 75704 MW; 2CCF342E7DF32E72 CRC64;
MEGNKLEEQD SSPPQSTPGL MKGNKREEQG LGPEPAAPQQ PTAEEEALIE FHRSYRELFE
FFCNNTTIHG AIRLVCSQHN RMKTAFWAVL WLCTFGMMYW QFGLLFGEYF SYPVSLNINL
NSDKLVFPAV TICTLNPYRY PEIKEELEEL DRITEQTLFD LYKYSSFTTL VAGSRSRRDL
RGTLPHPLQR LRVPPPPHGA RRARSVASSL RDNNPQVDWK DWKIGFQLCN QNKSDCFYQT
YSSGVDAVRE WYRFHYINIL SRLPETLPSL EEDTLGNFIF ACRFNQVSCN QANYSHFHHP
MYGNCYTFND KNNSNLWMSS MPGINNGLSL MLRAEQNDFI PLLSTVTGAR VMVHGQDEPA
FMDDGGFNLR PGVETSISMR KETLDRLGGD YGDCTKNGSD VPVENLYPSK YTQQVCIHSC
FQESMIKECG CAYIFYPRPQ NVEYCDYRKH SSWGYCYYKL QVDFSSDHLG CFTKCRKPCS
VTSYQLSAGY SRWPSVTSQE WVFQMLSRQN NYTVNNKRNG VAKVNIFFKE LNYKTNSESP
SVTMVTLLSN LGSQWSLWFG SSVLSVVEMA ELVFDLLVIM FLMLLRRFRS RYWSPGRGGR
GAQEVASTLA SSPPSHFCPH PMSLSLSQPG PAPSPALTAP PPAYATLGPR PSPGGSAGAS
SSTCPLGGP


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