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Reviewed, UniProtKB/Swiss-Prot P37091 (SCNNG_RAT)

Last modified February 9, 2010. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Amiloride-sensitive sodium channel subunit gamma
Alternative name(s):
    Epithelial Na(+) channel subunit gamma
    Gamma-ENaC
    SCNEG
    Nonvoltage-gated sodium channel 1 subunit gamma
    Gamma-NaCH
Gene names
Name: Scnn1g
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (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 structure

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. Ref.6

Subcellular location

Apical cell membrane; Multi-pass membrane protein By similarity. Note: Apical membrane of epithelial cells By similarity.

Post-translational modification

Phosphorylated on serine and threonine residues. Aldosterone and insulin increase the basal level of phosphorylation. Ref.5

Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation. Ref.4

Sequence similarities

Belongs to the amiloride-sensitive sodium channel family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 650650Amiloride-sensitive sodium channel subunit gamma
PRO_0000181279

Regions

Topological domain1 – 5555Cytoplasmic Potential
Transmembrane56 – 7621 Potential
Topological domain77 – 542466Extracellular Potential
Transmembrane543 – 56321 Potential
Topological domain564 – 65087Cytoplasmic Potential

Amino acid modifications

Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis61K → R: Interferes with ubiquitination and increases amiloride-sensitive current and the number of active channels; when associated with R-13. Ref.4
Mutagenesis131K → R: Interferes with ubiquitination and increases amiloride-sensitive current and the number of active channels; when associated with R-6. Ref.4
Sequence conflict531R → P in CAA54905. Ref.1
Sequence conflict5731W → C in CAA54905. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P37091-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 701F9B28B3250D8F

FASTA65074,066
        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

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References

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

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X77933 mRNA. Translation: CAA54905.1.
X78034 mRNA. Translation: CAA54964.1.
U37539 mRNA. Translation: AAB58459.1.
U37540 mRNA. Translation: AAB58460.1.
IPIIPI00325745.
PIRA54065.
RefSeqNP_058742.1.
UniGeneRn.10360

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP37091.

PTM databases

PhosphoSiteP37091.

Proteomic databases

PRIDEP37091.

Genome annotation databases

EnsemblENSRNOT00000024057; ENSRNOP00000024057; ENSRNOG00000017842; Rattus norvegicus. [Genome view]
GeneID24768.
KEGGrno:24768.
UCSCNM_017046. rat.

Organism-specific databases

CTD24768.
RGD3641. Scnn1g.

Phylogenomic databases

eggNOGroNOG08392.
HOVERGENP37091.
InParanoidP37091.

Gene expression databases

ArrayExpressP37091.
GenevestigatorP37091.
GermOnlineENSRNOG00000017842. Rattus norvegicus.

Family and domain databases

InterProIPR004724. EnaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERPTHR11690. Na+channel_ASC. 1 hit.
PfamPF00858. ASC. 1 hit.
[Graphical view]
PRINTSPR01078. AMINACHANNEL.
TIGRFAMsTIGR00859. ENaC. 1 hit.
PROSITEPS01206. ASC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio604332.

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Entry information

Entry nameSCNNG_RAT
AccessionPrimary (citable) accession number: P37091
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents