[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Distal colon epithelium; DOI=10.1038/367463a0; PubMed=8107805 [NCBI, ExPASy, EBI, Israel, Japan] Canessa C.M., Schild L., Buell G., Thorens B., Gautschi I., Horisberger J.-D., Rossier B.C.; "Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits."; Nature 367:463-467(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Distal colon; PubMed=8188647 [NCBI, ExPASy, EBI, Israel, Japan] Lingueglia R., Renard S., Waldmann R., Voilley N., Champigny G., Plass H., Lazdunski M., Barbry P.; "Different homologous subunits of the amiloride-sensitive Na+ channel are differently regulated by aldosterone."; J. Biol. Chem. 269:13736-13739(1994).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Distal colon, and Kidney; PubMed=9039092 [NCBI, ExPASy, EBI, Israel, Japan] Kreutz R., Struk B., Rubattu S., Hubner N., Szpirer J., Szpirer C., Ganten D., Lindpaintner K.; "Role of the alpha-, beta-, and gamma-subunits of epithelial sodium channel in a model of polygenic hypertension."; Hypertension 29:131-136(1997).
[4]	MUTAGENESIS OF LYS-6 AND LYS-13, AND UBIQUITINATION. DOI=10.1093/emboj/16.21.6325; PubMed=9351815 [NCBI, ExPASy, EBI, Israel, Japan] Staub O., Gautschi I., Ishikawa T., Breitschopf K., Ciechanover A., Schild L., Rotin D.; "Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination."; EMBO J. 16:6325-6336(1997).
[5]	PHOSPHORYLATION. DOI=10.1073/pnas.95.6.3301; PubMed=9501257 [NCBI, ExPASy, EBI, Israel, Japan] Shimkets R.A., Lifton R., Canessa C.M.; "In vivo phosphorylation of the epithelial sodium channel."; Proc. Natl. Acad. Sci. U.S.A. 95:3301-3305(1998).
[6]	INTERACTION WITH NEDD4. DOI=10.1038/87562; PubMed=11323714 [NCBI, ExPASy, EBI, Israel, Japan] Kanelis V., Rotin D., Forman-Kay J.D.; "Solution structure of a Nedd4 WW domain-ENaC peptide complex."; Nat. Struct. Biol. 8:407-412(2001).

Comments

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. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception.
SUBUNIT: Heterotetramer of two alpha, one beta and one gamma subunit. A delta subunit can replace the alpha subunit. Interacts with the WW domains of NEDD4, NEDD4L, WWP1 and WWP2 (By similarity).
SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein (By similarity). Note=Apical membrane of epithelial cells (By similarity).
PTM: Phosphorylated on serine and threonine residues. Aldosterone and insulin increase the basal level of phosphorylation.
PTM: Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation.
SIMILARITY: Belongs to the amiloride-sensitive sodium channel family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X77933; CAA54905.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X78034; CAA54964.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U37539; AAB58459.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U37540; AAB58460.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00325745; -.

A54065; A54065.

NP_058742.1; -.

3D structure databases

ModBase

P37091.

PTM databases

PhosphoSite

P37091; -.

Organism-specific databases

RGD

3641; Scnn1g.

Gene expression databases

ArrayExpress

P37091; -.

GermOnline

ENSRNOG00000017842; Rattus norvegicus.

Ontologies

GO:0016324;	Cellular component: apical plasma membrane (inferred from direct assay from RGD).
GO:0015280;	Molecular function: amiloride-sensitive sodium channel activity (inferred from direct assay from RGD).
GO:0031402;	Molecular function: sodium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050699;	Molecular function: WW domain binding (inferred from physical interaction from RGD).
GO:0001666;	Biological process: response to hypoxia (inferred from expression pattern from RGD).
GO:0050909;	Biological process: sensory perception of taste (inferred from electronic annotation from UniProtKB-KW).
GO:0006814;	Biological process: sodium ion transport (inferred from direct assay from RGD).
GO:0035313;	Biological process: wound healing, spreading of epidermal cells (inferred from mutant phenotype from RGD).
QuickGo view.

Family and domain databases

InterPro

IPR004724; EnaC.
IPR001873; Na+channel_ASC.
Graphical view of domain structure.

PANTHER

PTHR11690; Na+channel_ASC; 1.

Pfam

PF00858; ASC; 1.
Pfam graphical view of domain structure.

PRINTS

PR01078; AMINACHANNEL.

TIGRFAMs

TIGR00859; ENaC; 1.

PROSITE

PS01206; ASC; 1.

Proteomic databases

PRIDE

P37091; -.

Genome annotation databases

Ensembl

ENSRNOG00000017842; Rattus norvegicus. [Contig view]

GeneID

24768; -.

KEGG

rno:24768; -.

Phylogenomic databases

HOVERGEN

P37091; -.

Other

604332; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein; Sensory transduction; Sodium; Sodium channel; Sodium transport; Taste; Transmembrane; Transport; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 650`	`650`	`Amiloride-sensitive sodium channel subunit gamma.`	`PRO_0000181279`
`TOPO_DOM`	`1 55`	`55`	`Cytoplasmic (Potential).`
`TRANSMEM`	`56 76`	`21`	`Potential.`
`TOPO_DOM`	`77 542`	`466`	`Extracellular (Potential).`
`TRANSMEM`	`543 563`	`21`	`Potential.`
`TOPO_DOM`	`564 650`	`87`	`Cytoplasmic (Potential).`
`CARBOHYD`	`210 210`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`249 249`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`272 272`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`292 292`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`498 498`		`N-linked (GlcNAc...) (Potential).`
`MUTAGEN`	`6 6`		`K->R: Interferes with ubiquitination and increases amiloride-sensitive current and the number of active channels; when associated with R-13.`
`MUTAGEN`	`13 13`		`K->R: Interferes with ubiquitination and increases amiloride-sensitive current and the number of active channels; when associated with R-6.`
`CONFLICT`	`53 53`		`R -> P (in Ref. 1; CAA54905).`
`CONFLICT`	`573 573`		`W -> C (in Ref. 1; CAA54905).`

Sequence information

Length: 650 AA [This is the length of the unprocessed precursor]

Molecular weight: 74066 Da [This is the MW of the unprocessed precursor]

CRC64: 701F9B28B3250D8F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPGEKIKAK IKKNLPVRGP QAPTIKDLMH WYCMNTNTHG CRRIVVSRGR LRRLLWIAFT 

        70         80         90        100        110        120 
LTAVALIIWQ CALLVFSFYT VSVSIKVHFQ KLDFPAVTIC NINPYKYSAV SDLLTDLDSE 

       130        140        150        160        170        180 
TKQALLSLYG VKESRKRREA GSMPSTLEGT PPRFFKLIPL LVFNENEKGK ARDFFTGRKR 

       190        200        210        220        230        240 
KISGKIIHKA SNVMHVHESK KLVGFQLCSN DTSDCATYTF SSGINAIQEW YKLHYMNIMA 

       250        260        270        280        290        300 
QVPLEKKINM SYSAEELLVT CFFDGMSCDA RNFTLFHHPM YGNCYTFNNK ENATILSTSM 

       310        320        330        340        350        360 
GGSEYGLQVI LYINEDEYNP FLVSSTGAKV LIHQQNEYPF IEDVGMEIET AMSTSIGMHL 

       370        380        390        400        410        420 
TESFKLSEPY SQCTEDGSDV PVTNIYNAAY SLQICLYSCF QTKMVEKCGC AQYSQPLPPA 

       430        440        450        460        470        480 
ANYCNYQQHP NWMYCYYQLY QAFVREELGC QSVCKQSCSF KEWTLTTSLA QWPSEASEKW 

       490        500        510        520        530        540 
LLNVLTWDQS QQINKKLNKT DLAKLLIFYK DLNQRSIMES PANSIEMLLS NFGGQLGLWM 

       550        560        570        580        590        600 
SCSVVCVIEI IEVFFIDFFS IIARRQWHKA KDWWARRQTP PSTETPSSRQ GQDNPALDTD 

       610        620        630        640        650 
DDLPTFTSAM RLPPAPGSTV PGTPPPRYNT LRLDRAFSSQ LTDTQLTNEL

P37091 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools