SCNNB_MOUSE
ID SCNNB_MOUSE Reviewed; 638 AA.
AC Q9WU38;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Amiloride-sensitive sodium channel subunit beta;
DE AltName: Full=Beta-NaCH;
DE AltName: Full=Epithelial Na(+) channel subunit beta;
DE Short=Beta-ENaC;
DE AltName: Full=Nonvoltage-gated sodium channel 1 subunit beta;
DE AltName: Full=SCNEB;
GN Name=Scnn1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=10409305; DOI=10.1152/ajprenal.1999.277.1.f121;
RA Ahn Y.J., Brooker D.R., Kosari F., Harte B.J., Li J., Mackler S.A.,
RA Kleyman T.R.;
RT "Cloning and functional expression of the mouse epithelial sodium
RT channel.";
RL Am. J. Physiol. 277:F121-F129(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH NEDD4 AND NEDD4L.
RX PubMed=11244092; DOI=10.1074/jbc.c000906200;
RA Harvey K.F., Dinudom A., Cook D.I., Kumar S.;
RT "The Nedd4-like protein KIAA0439 is a potential regulator of the epithelial
RT sodium channel.";
RL J. Biol. Chem. 276:8597-8601(2001).
RN [4]
RP INTERACTION WITH NEDD4L.
RX PubMed=12424229; DOI=10.1096/fj.02-0497fje;
RA Fotia A.B., Dinudom A., Shearwin K.E., Koch J.-P., Korbmacher C.,
RA Cook D.I., Kumar S.;
RT "The role of individual Nedd4-2 (KIAA0439) WW domains in binding and
RT regulating epithelial sodium channels.";
RL FASEB J. 17:70-72(2003).
RN [5]
RP INTERACTION WITH NEDD4 AND NEDD4L.
RX PubMed=15123669; DOI=10.1074/jbc.m402820200;
RA Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
RT "Regulation of neuronal voltage-gated sodium channels by the ubiquitin-
RT protein ligases Nedd4 and Nedd4-2.";
RL J. Biol. Chem. 279:28930-28935(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-633, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=20525693; DOI=10.1074/jbc.m110.103432;
RA Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S.,
RA Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L., Cobb M.H.;
RT "Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium
RT channel are regulated by multiple with no lysine (WNK) family members.";
RL J. Biol. Chem. 285:25161-25167(2010).
CC -!- FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited
CC by the diuretic amiloride. Mediates the electrodiffusion of the luminal
CC sodium (and water, which follows osmotically) through the apical
CC membrane of epithelial cells. Plays an essential role in electrolyte
CC and blood pressure homeostasis, but also in airway surface liquid
CC homeostasis, which is important for proper clearance of mucus. Controls
CC the reabsorption of sodium in kidney, colon, lung and sweat glands.
CC Also plays a role in taste perception. {ECO:0000269|PubMed:10409305}.
CC -!- ACTIVITY REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
CC {ECO:0000269|PubMed:20525693}.
CC -!- SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a
CC gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in
CC some organisms and can replace the alpha/SCNN1A subunit to form an
CC alternative channel with specific properties (By similarity). Interacts
CC with NEDD4 (via WW domains) (PubMed:11244092, PubMed:15123669).
CC Interacts with NEDD4L (via WW domains) (PubMed:11244092,
CC PubMed:12424229, PubMed:15123669). Interacts with WWP1 (via WW
CC domains). Interacts with WWP2 (via WW domains). Interacts with the
CC full-length immature form of PCSK9 (pro-PCSK9) (By similarity).
CC Interacts (N-glycosylated) with BPIFA1; the interaction is direct and
CC inhibits the proteolytic processing of SCNN1A and SCNN1G and the
CC activation of ENaC (By similarity). {ECO:0000250|UniProtKB:P51168,
CC ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:12424229,
CC ECO:0000269|PubMed:15123669, ECO:0000305|PubMed:10409305}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P37090}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial
CC cells. {ECO:0000250|UniProtKB:P37090}.
CC -!- TISSUE SPECIFICITY: Lung and kidney. {ECO:0000269|PubMed:10409305}.
CC -!- PTM: N-glycosylated. N-glycosylation is required for interaction with
CC BPIFA1. {ECO:0000250|UniProtKB:P51168}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Aldosterone and
CC insulin increase the basal level of phosphorylation.
CC {ECO:0000250|UniProtKB:P37090}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. SCNN1B subfamily. {ECO:0000305}.
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DR EMBL; AF112186; AAD21245.1; -; mRNA.
DR EMBL; AK028909; BAC26190.1; -; mRNA.
DR EMBL; AK036819; BAC29591.1; -; mRNA.
DR CCDS; CCDS21804.1; -.
DR RefSeq; NP_001258952.1; NM_001272023.1.
DR RefSeq; NP_035455.1; NM_011325.2.
DR AlphaFoldDB; Q9WU38; -.
DR SMR; Q9WU38; -.
DR BioGRID; 203106; 10.
DR ComplexPortal; CPX-315; Amiloride-sensitive sodium channel complex, alpha-beta-gamma.
DR DIP; DIP-40891N; -.
DR IntAct; Q9WU38; 3.
DR STRING; 10090.ENSMUSP00000033161; -.
DR GuidetoPHARMACOLOGY; 739; -.
DR GlyGen; Q9WU38; 3 sites.
DR iPTMnet; Q9WU38; -.
DR PhosphoSitePlus; Q9WU38; -.
DR SwissPalm; Q9WU38; -.
DR MaxQB; Q9WU38; -.
DR PaxDb; Q9WU38; -.
DR PRIDE; Q9WU38; -.
DR ProteomicsDB; 256755; -.
DR Antibodypedia; 2607; 480 antibodies from 31 providers.
DR DNASU; 20277; -.
DR Ensembl; ENSMUST00000033161; ENSMUSP00000033161; ENSMUSG00000030873.
DR GeneID; 20277; -.
DR KEGG; mmu:20277; -.
DR UCSC; uc009jnx.2; mouse.
DR CTD; 6338; -.
DR MGI; MGI:104696; Scnn1b.
DR VEuPathDB; HostDB:ENSMUSG00000030873; -.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000160893; -.
DR HOGENOM; CLU_020415_0_0_1; -.
DR InParanoid; Q9WU38; -.
DR OMA; NLTIWNH; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q9WU38; -.
DR TreeFam; TF330663; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-9730628; Sensory perception of salty taste.
DR BioGRID-ORCS; 20277; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9WU38; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9WU38; protein.
DR Bgee; ENSMUSG00000030873; Expressed in vestibular membrane of cochlear duct and 78 other tissues.
DR ExpressionAtlas; Q9WU38; baseline and differential.
DR Genevisible; Q9WU38; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0034706; C:sodium channel complex; IDA:MGI.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:MGI.
DR GO; GO:0005272; F:sodium channel activity; IDA:MGI.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0050699; F:WW domain binding; IPI:MGI.
DR GO; GO:0032341; P:aldosterone metabolic process; IMP:MGI.
DR GO; GO:0014824; P:artery smooth muscle contraction; IMP:MGI.
DR GO; GO:0071468; P:cellular response to acidic pH; ISO:MGI.
DR GO; GO:1904045; P:cellular response to aldosterone; IDA:MGI.
DR GO; GO:0036254; P:cellular response to amiloride; IDA:ComplexPortal.
DR GO; GO:1904117; P:cellular response to vasopressin; IC:ComplexPortal.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0042045; P:epithelial fluid transport; IMP:MGI.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0002269; P:leukocyte activation involved in inflammatory response; IDA:MGI.
DR GO; GO:0070254; P:mucus secretion; IDA:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:MGI.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; IDA:MGI.
DR GO; GO:0070944; P:neutrophil-mediated killing of bacterium; IDA:MGI.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IC:ComplexPortal.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0032094; P:response to food; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0050914; P:sensory perception of salty taste; IC:ComplexPortal.
DR GO; GO:0050915; P:sensory perception of sour taste; IC:ComplexPortal.
DR GO; GO:0055078; P:sodium ion homeostasis; IMP:MGI.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IDA:ComplexPortal.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR GO; GO:0097274; P:urea homeostasis; IMP:MGI.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:MGI.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
DR PROSITE; PS01206; ASC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sensory transduction; Sodium; Sodium channel; Sodium transport; Taste;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..638
FT /note="Amiloride-sensitive sodium channel subunit beta"
FT /id="PRO_0000181269"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 51..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..530
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 531..551
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 594..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 174
FT /note="S -> N (in Ref. 2; BAC29591)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="A -> T (in Ref. 2; BAC26190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 72197 MW; F502A510BFE65392 CRC64;
MPVKKYLLKC LHRLQKGPGY TYKELLVWYC NNTNTHGPKR IICEGPKKKA MWFLLTLLFA
CLVCWQWGVF IQTYLSWEVS VSLSMGFKTM NFPAVTVCNS SPFQYSKVKH LLKDLDELME
AVLEKILAPE ASHSNTTRTL NFTIWNHTPL VLIDERNPDH PVVLNLFGDS HNSSNPAPGS
TCNAQGCKVA MRLCSANGTV CTLRNFTSAT QAVTEWYILQ ATNIFSQVLP QDLVGMGYAP
DRIILACLFG TEPCSHRNFT PIFYPDYGNC YIFNWGMTEE TLPSANPGTE FGLKLILDIG
QEDYVPFLAS TAGARLMLHE QRTYPFIREE GIYAMAGTET SIGVLVDKLQ RKGEPYSPCT
MNGSDVAIKN LYSVYNTTYS IQACLHSCFQ DHMIRNCSCG HYLYPLPEGE KYCNNRDFPD
WAYCYLNLQM SVTQRETCLS MCKESCNDTQ YKMTISMADW PSEASEDWIL HVLSQERDQS
SNITLSRKGI VKLNIYFQEF NYRTIEESPA NNIVWLLSNL GGQFGFWMGG SVLCLIEFGE
IIIDFIWITI IKLVASCKGL RRRRPQAPYT GPPPTVAELV EAHTNFGFQP DTTSCRPHGE
VYPDQQTLPI PGTPPPNYDS LRLQPLDTME SDSEVEAI
