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Protein

Amiloride-sensitive sodium channel subunit beta

Gene

Scnn1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

Activated by WNK1, WNK2, WNK3 and WNK4.1 Publication

GO - Molecular functioni

  • ligand-gated sodium channel activity Source: MGI
  • WW domain binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel

Keywords - Biological processi

Ion transport, Sensory transduction, Sodium transport, Taste, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Amiloride-sensitive sodium channel subunit beta
Alternative name(s):
Beta-NaCH
Epithelial Na(+) channel subunit beta
Short name:
Beta-ENaC
Nonvoltage-gated sodium channel 1 subunit beta
SCNEB
Gene namesi
Name:Scnn1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:104696. Scnn1b.

Subcellular locationi

  • Apical cell membrane By similarity; Multi-pass membrane protein By similarity
  • Cytoplasmic vesicle membrane By similarity

  • Note: Apical membrane of epithelial cells.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5050CytoplasmicBy similarityAdd
BLAST
Transmembranei51 – 7121Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini72 – 530459ExtracellularBy similarityAdd
BLAST
Transmembranei531 – 55121Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini552 – 63887CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: MGI
  • sodium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638Amiloride-sensitive sodium channel subunit betaPRO_0000181269Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence analysis
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence analysis
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence analysis
Modified residuei631 – 6311PhosphoserineCombined sources
Modified residuei633 – 6331PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated. N-glycosylation is required for interaction with BPIFA1.By similarity
Phosphorylated on serine and threonine residues. Aldosterone and insulin increase the basal level of phosphorylation.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9WU38.
PaxDbiQ9WU38.
PRIDEiQ9WU38.

PTM databases

iPTMnetiQ9WU38.
PhosphoSiteiQ9WU38.
SwissPalmiQ9WU38.

Expressioni

Tissue specificityi

Lung and kidney.1 Publication

Gene expression databases

BgeeiQ9WU38.
CleanExiMM_SCNN1B.
ExpressionAtlasiQ9WU38. baseline and differential.
GenevisibleiQ9WU38. MM.

Interactioni

Subunit structurei

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:15123669). Interacts with NEDD4L (via WW domains) (PubMed:11244092, PubMed:12424229, PubMed:15123669). Interacts with WWP1 (via WW domains). Interacts with WWP2 (via WW domains). Interacts with the full length immature form of PCSK9 (pro-PCSK9) (By similarity). Interacts (N-glycosylated) with BPIFA1; the interaction is direct and inhibits the proteolytic processing of SCNN1A and SCNN1G and the activation of ENaC (By similarity).By similarity1 Publication3 Publications

GO - Molecular functioni

  • WW domain binding Source: MGI

Protein-protein interaction databases

BioGridi203106. 5 interactions.
DIPiDIP-40891N.
MINTiMINT-90190.
STRINGi10090.ENSMUSP00000033161.

Structurei

3D structure databases

ProteinModelPortaliQ9WU38.
SMRiQ9WU38. Positions 50-534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4294. Eukaryota.
ENOG410ZNFK. LUCA.
GeneTreeiENSGT00760000119120.
HOGENOMiHOG000236286.
HOVERGENiHBG058435.
InParanoidiQ9WU38.
KOiK04825.
OMAiDTQYKMT.
OrthoDBiEOG7T1R9N.
PhylomeDBiQ9WU38.
TreeFamiTF330663.

Family and domain databases

InterProiIPR004724. ENaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERiPTHR11690. PTHR11690. 2 hits.
PfamiPF00858. ASC. 1 hit.
[Graphical view]
PRINTSiPR01078. AMINACHANNEL.
TIGRFAMsiTIGR00859. ENaC. 1 hit.
PROSITEiPS01206. ASC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WU38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVKKYLLKC LHRLQKGPGY TYKELLVWYC NNTNTHGPKR IICEGPKKKA
60 70 80 90 100
MWFLLTLLFA CLVCWQWGVF IQTYLSWEVS VSLSMGFKTM NFPAVTVCNS
110 120 130 140 150
SPFQYSKVKH LLKDLDELME AVLEKILAPE ASHSNTTRTL NFTIWNHTPL
160 170 180 190 200
VLIDERNPDH PVVLNLFGDS HNSSNPAPGS TCNAQGCKVA MRLCSANGTV
210 220 230 240 250
CTLRNFTSAT QAVTEWYILQ ATNIFSQVLP QDLVGMGYAP DRIILACLFG
260 270 280 290 300
TEPCSHRNFT PIFYPDYGNC YIFNWGMTEE TLPSANPGTE FGLKLILDIG
310 320 330 340 350
QEDYVPFLAS TAGARLMLHE QRTYPFIREE GIYAMAGTET SIGVLVDKLQ
360 370 380 390 400
RKGEPYSPCT MNGSDVAIKN LYSVYNTTYS IQACLHSCFQ DHMIRNCSCG
410 420 430 440 450
HYLYPLPEGE KYCNNRDFPD WAYCYLNLQM SVTQRETCLS MCKESCNDTQ
460 470 480 490 500
YKMTISMADW PSEASEDWIL HVLSQERDQS SNITLSRKGI VKLNIYFQEF
510 520 530 540 550
NYRTIEESPA NNIVWLLSNL GGQFGFWMGG SVLCLIEFGE IIIDFIWITI
560 570 580 590 600
IKLVASCKGL RRRRPQAPYT GPPPTVAELV EAHTNFGFQP DTTSCRPHGE
610 620 630
VYPDQQTLPI PGTPPPNYDS LRLQPLDTME SDSEVEAI
Length:638
Mass (Da):72,197
Last modified:November 1, 1999 - v1
Checksum:iF502A510BFE65392
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741S → N in BAC29591 (PubMed:16141072).Curated
Sequence conflicti239 – 2391A → T in BAC26190 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112186 mRNA. Translation: AAD21245.1.
AK028909 mRNA. Translation: BAC26190.1.
AK036819 mRNA. Translation: BAC29591.1.
CCDSiCCDS21804.1.
RefSeqiNP_001258952.1. NM_001272023.1.
NP_035455.1. NM_011325.2.
UniGeneiMm.7709.

Genome annotation databases

EnsembliENSMUST00000033161; ENSMUSP00000033161; ENSMUSG00000030873.
GeneIDi20277.
KEGGimmu:20277.
UCSCiuc009jnx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112186 mRNA. Translation: AAD21245.1.
AK028909 mRNA. Translation: BAC26190.1.
AK036819 mRNA. Translation: BAC29591.1.
CCDSiCCDS21804.1.
RefSeqiNP_001258952.1. NM_001272023.1.
NP_035455.1. NM_011325.2.
UniGeneiMm.7709.

3D structure databases

ProteinModelPortaliQ9WU38.
SMRiQ9WU38. Positions 50-534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203106. 5 interactions.
DIPiDIP-40891N.
MINTiMINT-90190.
STRINGi10090.ENSMUSP00000033161.

PTM databases

iPTMnetiQ9WU38.
PhosphoSiteiQ9WU38.
SwissPalmiQ9WU38.

Proteomic databases

MaxQBiQ9WU38.
PaxDbiQ9WU38.
PRIDEiQ9WU38.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033161; ENSMUSP00000033161; ENSMUSG00000030873.
GeneIDi20277.
KEGGimmu:20277.
UCSCiuc009jnx.2. mouse.

Organism-specific databases

CTDi6338.
MGIiMGI:104696. Scnn1b.

Phylogenomic databases

eggNOGiKOG4294. Eukaryota.
ENOG410ZNFK. LUCA.
GeneTreeiENSGT00760000119120.
HOGENOMiHOG000236286.
HOVERGENiHBG058435.
InParanoidiQ9WU38.
KOiK04825.
OMAiDTQYKMT.
OrthoDBiEOG7T1R9N.
PhylomeDBiQ9WU38.
TreeFamiTF330663.

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.

Miscellaneous databases

PROiQ9WU38.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WU38.
CleanExiMM_SCNN1B.
ExpressionAtlasiQ9WU38. baseline and differential.
GenevisibleiQ9WU38. MM.

Family and domain databases

InterProiIPR004724. ENaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERiPTHR11690. PTHR11690. 2 hits.
PfamiPF00858. ASC. 1 hit.
[Graphical view]
PRINTSiPR01078. AMINACHANNEL.
TIGRFAMsiTIGR00859. ENaC. 1 hit.
PROSITEiPS01206. ASC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional expression of the mouse epithelial sodium channel."
    Ahn Y.J., Brooker D.R., Kosari F., Harte B.J., Li J., Mackler S.A., Kleyman T.R.
    Am. J. Physiol. 277:F121-F129(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin and Vagina.
  3. "The Nedd4-like protein KIAA0439 is a potential regulator of the epithelial sodium channel."
    Harvey K.F., Dinudom A., Cook D.I., Kumar S.
    J. Biol. Chem. 276:8597-8601(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEDD4 AND NEDD4L.
  4. "The role of individual Nedd4-2 (KIAA0439) WW domains in binding and regulating epithelial sodium channels."
    Fotia A.B., Dinudom A., Shearwin K.E., Koch J.-P., Korbmacher C., Cook D.I., Kumar S.
    FASEB J. 17:70-72(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEDD4L.
  5. "Regulation of neuronal voltage-gated sodium channels by the ubiquitin-protein ligases Nedd4 and Nedd4-2."
    Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.
    J. Biol. Chem. 279:28930-28935(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEDD4 AND NEDD4L.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.
  7. "Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium channel are regulated by multiple with no lysine (WNK) family members."
    Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S., Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L., Cobb M.H.
    J. Biol. Chem. 285:25161-25167(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiSCNNB_MOUSE
AccessioniPrimary (citable) accession number: Q9WU38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.