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Protein

Amiloride-sensitive sodium channel subunit beta

Gene

Scnn1b

Organism
Rattus norvegicus (Rat)
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.By similarity

Enzyme regulationi

Activated by WNK1, WNK2, WNK3 and WNK4.By similarity

GO - Molecular functioni

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

GO - Biological processi

  • multicellular organismal water homeostasis Source: UniProtKB
  • regulation of sodium ion transport Source: RGD
  • response to hypoxia Source: RGD
  • sensory perception of taste Source: UniProtKB-KW
  • sodium ion homeostasis Source: UniProtKB
  • sodium ion transport Source: RGD
  • wound healing, spreading of epidermal cells Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel

Keywords - Biological processi

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

Keywords - Ligandi

Sodium

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3640. Scnn1b.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 50CytoplasmicBy similarityAdd BLAST50
Transmembranei51 – 71Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini72 – 530ExtracellularBy similarityAdd BLAST459
Transmembranei531 – 551Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini552 – 638CytoplasmicBy similarityAdd BLAST87

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • cell surface Source: RGD
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
  • sodium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi616P → A: Strong increase in channel activity. 1 Publication1
Mutagenesisi618Y → A: Strong increase in channel activity. 1 Publication1
Mutagenesisi621L → A: 2-fold increase in channel activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001812711 – 638Amiloride-sensitive sodium channel subunit betaAdd BLAST638

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi135N-linked (GlcNAc...)Sequence analysis1
Glycosylationi141N-linked (GlcNAc...)Sequence analysis1
Modified residuei631PhosphoserineBy similarity1
Modified residuei633PhosphoserineBy similarity1

Post-translational modificationi

N-glycosylated (PubMed:11773057). N-glycosylation is required for interaction with BPIFA1 (By similarity).By similarity1 Publication
Phosphorylated on serine and threonine residues. Aldosterone and insulin increase the basal level of phosphorylation.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP37090.

PTM databases

iPTMnetiP37090.
PhosphoSitePlusiP37090.

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:12654927, PubMed:11323714). Interacts with NEDD4L (via WW domains) (By similarity). Interacts with WWP1 (via WW domains) (By similarity). Interacts with WWP2 (via WW domains) (By similarity). 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 similarity2 Publications

GO - Molecular functioni

  • WW domain binding Source: RGD

Protein-protein interaction databases

BioGridi246891. 2 interactors.
IntActiP37090. 2 interactors.
STRINGi10116.ENSRNOP00000063755.

Structurei

Secondary structure

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni618 – 620Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I5HNMR-B607-621[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37090.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4294. Eukaryota.
ENOG410ZNFK. LUCA.
HOGENOMiHOG000236286.
HOVERGENiHBG058435.
InParanoidiP37090.
KOiK04825.
PhylomeDBiP37090.

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.

P37090-1 [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 LLKDLYKLME AVLDKILAPK SSHTNTTSTL NFTIWNHTPL
160 170 180 190 200
VLIDERNPDH PVVLNLFGDS HNSSNPAPGS TCNAQGCKVA MRLCSANGTV
210 220 230 240 250
CTFRNFTSAT QAVTEWYILQ ATNIFSQVLP QDLVGMGYAP DRIILACLFG
260 270 280 290 300
TEPCSHRNFT PIFYPDYGNC YIFNWGMTEK ALPSANPGTE FGLKLILDIG
310 320 330 340 350
QEDYVPFLAS TAGARLMLHE QRTYPFIREE GIYAMAGTET SIGVLLDKLQ
360 370 380 390 400
GKGEPYSPCT MNGSDVAIQN LYSDYNTTYS IQACLHSCFQ DHMIHNCSCG
410 420 430 440 450
HYLYPLPAGE KYCNNRDFPD WAYCYLSLQM SVVQRETCLS MCKESCNDTQ
460 470 480 490 500
YKMTISMADW PSEASEDWIL HVLSQERDQS SNITLSRKGI VKLNIYFQEF
510 520 530 540 550
NYRTIEESPA NNIVWLLSNL GGQFGFWMGG SVLCLIEFGE IIIDFIWITV
560 570 580 590 600
IKLVASCKGL RRRRPQAPYT GPPPTVAELV EAHTNFGFQP DTTSCRPNAE
610 620 630
VYPDQQTLPI PGTPPPNYDS LRLQPLDTME SDSEVEAI
Length:638
Mass (Da):71,995
Last modified:November 1, 1997 - v2
Checksum:i79176A282D5079F1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti567A → R in CAA54904 (PubMed:8107805).Curated1
Sequence conflicti586 – 587FG → CV in CAA54904 (PubMed:8107805).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77932 mRNA. Translation: CAA54904.1.
U35174 mRNA. Translation: AAB58457.1.
U35175 mRNA. Translation: AAB58458.1.
PIRiS41159.
RefSeqiNP_036780.1. NM_012648.1.
UniGeneiRn.9807.

Genome annotation databases

GeneIDi24767.
KEGGirno:24767.
UCSCiRGD:3640. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77932 mRNA. Translation: CAA54904.1.
U35174 mRNA. Translation: AAB58457.1.
U35175 mRNA. Translation: AAB58458.1.
PIRiS41159.
RefSeqiNP_036780.1. NM_012648.1.
UniGeneiRn.9807.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I5HNMR-B607-621[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246891. 2 interactors.
IntActiP37090. 2 interactors.
STRINGi10116.ENSRNOP00000063755.

PTM databases

iPTMnetiP37090.
PhosphoSitePlusiP37090.

Proteomic databases

PaxDbiP37090.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24767.
KEGGirno:24767.
UCSCiRGD:3640. rat.

Organism-specific databases

CTDi6338.
RGDi3640. Scnn1b.

Phylogenomic databases

eggNOGiKOG4294. Eukaryota.
ENOG410ZNFK. LUCA.
HOGENOMiHOG000236286.
HOVERGENiHBG058435.
InParanoidiP37090.
KOiK04825.
PhylomeDBiP37090.

Miscellaneous databases

EvolutionaryTraceiP37090.
PROiP37090.

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...

Entry informationi

Entry nameiSCNNB_RAT
AccessioniPrimary (citable) accession number: P37090
Secondary accession number(s): O09183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.