Scnn1b

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
Inferred from direct assayⁱ
- 16172119
- 16356937
WW domain binding
Source: RGD
Inferred from direct assayⁱ
- 9923703

GO - Biological processⁱ

multicellular organismal water homeostasis Source: UniProtKB
regulation of sodium ion transport
Source: RGD
Inferred from direct assayⁱ
- 16027156
response to hypoxia
Source: RGD
Inferred from expression patternⁱ
- 12372821
sensory perception of taste Source: UniProtKB-KW
sodium ion homeostasis Source: UniProtKB
sodium ion transport
Source: RGD
Inferred from direct assayⁱ
- 15075188
wound healing, spreading of epidermal cells
Source: RGD
Inferred from mutant phenotypeⁱ
- 16844921

Complete GO annotation...

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
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

RGDⁱ	3640. Scnn1b.

Subcellular locationⁱ

Apical cell membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Immunocytochemical and immunoelectron microscopic localization of alpha-, beta-, and gamma-ENaC in rat kidney."
  Hager H., Kwon T.H., Vinnikova A.K., Masilamani S., Brooks H.L., Frokiaer J., Knepper M.A., Nielsen S.
  Am. J. Physiol. 280:F1093-F1106(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.5
  "Trafficking and cell surface stability of the epithelial Na+ channel expressed in epithelial Madin-Darby canine kidney cells."
  Hanwell D., Ishikawa T., Saleki R., Rotin D.
  J. Biol. Chem. 277:9772-9779(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
; Multi-pass membrane protein
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P37089 (SCNNA_RAT)
Cytoplasmic vesicle membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Immunocytochemical and immunoelectron microscopic localization of alpha-, beta-, and gamma-ENaC in rat kidney."
  Hager H., Kwon T.H., Vinnikova A.K., Masilamani S., Brooks H.L., Frokiaer J., Knepper M.A., Nielsen S.
  Am. J. Physiol. 280:F1093-F1106(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.5
  "Trafficking and cell surface stability of the epithelial Na+ channel expressed in epithelial Madin-Darby canine kidney cells."
  Hanwell D., Ishikawa T., Saleki R., Rotin D.
  J. Biol. Chem. 277:9772-9779(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.

Note:

Apical membrane of epithelial cells.2 Publications

Topology

Feature key	Position(s)	Length	Description	Actions
Topological domainⁱ	1 – 50	50	CytoplasmicBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P37089 (SCNNA_RAT)	Add BLAST
Transmembraneⁱ	51 – 71	21	Helical; Name=1Sequence analysis	Add BLAST
Topological domainⁱ	72 – 530	459	ExtracellularBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P37089 (SCNNA_RAT)	Add BLAST
Transmembraneⁱ	531 – 551	21	Helical; Name=2Sequence analysis	Add BLAST
Topological domainⁱ	552 – 638	87	CytoplasmicBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P37089 (SCNNA_RAT)	Add BLAST

GO - Cellular componentⁱ

apical plasma membrane
Source: RGD
Inferred from direct assayⁱ
- 11773057
- 15075188
cell surface
Source: RGD
Inferred from direct assayⁱ
- 16476738
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 key	Position(s)	Length	Description
Mutagenesisⁱ	616 – 616	1	P → A: Strong increase in channel activity. 1 Publication Manual assertion based on experiment inⁱ Ref.6 "Affinity and specificity of interactions between Nedd4 isoforms and ENaC." Henry P.C., Kanelis V., O'Brien C.M., Kim B., Gautschi I., Forman-Kay J.D., Schild L., Rotin D. J. Biol. Chem. 278:20019-20028(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PRO-616; TYR-618 AND LEU-621, INTERACTION WITH NEDD4.
Mutagenesisⁱ	618 – 618	1	Y → A: Strong increase in channel activity. 1 Publication Manual assertion based on experiment inⁱ Ref.6 "Affinity and specificity of interactions between Nedd4 isoforms and ENaC." Henry P.C., Kanelis V., O'Brien C.M., Kim B., Gautschi I., Forman-Kay J.D., Schild L., Rotin D. J. Biol. Chem. 278:20019-20028(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PRO-616; TYR-618 AND LEU-621, INTERACTION WITH NEDD4.
Mutagenesisⁱ	621 – 621	1	L → A: 2-fold increase in channel activity. 1 Publication Manual assertion based on experiment inⁱ Ref.6 "Affinity and specificity of interactions between Nedd4 isoforms and ENaC." Henry P.C., Kanelis V., O'Brien C.M., Kim B., Gautschi I., Forman-Kay J.D., Schild L., Rotin D. J. Biol. Chem. 278:20019-20028(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PRO-616; TYR-618 AND LEU-621, INTERACTION WITH NEDD4.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 638	638	Amiloride-sensitive sodium channel subunit beta		PRO_0000181271	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Glycosylationⁱ	135 – 135	1	N-linked (GlcNAc...)Sequence analysis
Glycosylationⁱ	141 – 141	1	N-linked (GlcNAc...)Sequence analysis
Modified residueⁱ	631 – 631	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9WU38 (SCNNB_MOUSE)
Modified residueⁱ	633 – 633	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9WU38 (SCNNB_MOUSE)

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

PaxDbⁱ	P37090.

PaxDbⁱ

P37090.

PTM databases

iPTMnetⁱ	P37090.
PhosphoSiteⁱ	P37090.

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
Inferred from direct assayⁱ
- 9923703

Protein-protein interaction databases

BioGridⁱ	246891. 2 interactions.
IntActⁱ	P37090. 2 interactions.
STRINGⁱ	10116.ENSRNOP00000063755.

Structureⁱ

Secondary structure

1

638

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Turnⁱ	618 – 620	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1I5H

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I5H	NMR	-	B	607-621	[»]

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P37090.

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1B subfamily. [View classification]Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG4294. Eukaryota. ENOG410ZNFK. LUCA.
HOGENOMⁱ	HOG000236286.
HOVERGENⁱ	HBG058435.
InParanoidⁱ	P37090.
KOⁱ	K04825.
PhylomeDBⁱ	P37090.

Family and domain databases

InterProⁱ	IPR004724. ENaC. IPR001873. Na+channel_ASC. IPR020903. Na+channel_ASC_CS. [Graphical view]
PANTHERⁱ	PTHR11690. PTHR11690. 2 hits.
Pfamⁱ	PF00858. ASC. 1 hit. [Graphical view]
PRINTSⁱ	PR01078. AMINACHANNEL.
TIGRFAMsⁱ	TIGR00859. ENaC. 1 hit.
PROSITEⁱ	PS01206. ASC. 1 hit. [Graphical view]

Sequenceⁱ

Sequence statusⁱ: Complete.

P37090-1 [UniParc]FASTA Add 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 key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Sequence conflictⁱ	567 – 567	1	A → R in CAA54904 (PubMed:8107805).Curated
Sequence conflictⁱ	586 – 587	2	FG → CV in CAA54904 (PubMed:8107805).Curated

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.
PIRⁱ	S41159.
RefSeqⁱ	NP_036780.1. NM_012648.1.
UniGeneⁱ	Rn.9807.

Genome annotation databases

GeneIDⁱ	24767.
KEGGⁱ	rno:24767.
UCSCⁱ	RGD: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.
PIRⁱ	S41159.
RefSeqⁱ	NP_036780.1. NM_012648.1.
UniGeneⁱ	Rn.9807.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I5H	NMR	-	B	607-621	[»]

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

BioGridⁱ	246891. 2 interactions.
IntActⁱ	P37090. 2 interactions.
STRINGⁱ	10116.ENSRNOP00000063755.

PTM databases

iPTMnetⁱ	P37090.
PhosphoSiteⁱ	P37090.

Proteomic databases

PaxDbⁱ	P37090.

PaxDbⁱ

P37090.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	24767.
KEGGⁱ	rno:24767.
UCSCⁱ	RGD:3640. rat.

Organism-specific databases

CTDⁱ	6338.
RGDⁱ	3640. Scnn1b.

Phylogenomic databases

eggNOGⁱ	KOG4294. Eukaryota. ENOG410ZNFK. LUCA.
HOGENOMⁱ	HOG000236286.
HOVERGENⁱ	HBG058435.
InParanoidⁱ	P37090.
KOⁱ	K04825.
PhylomeDBⁱ	P37090.

Miscellaneous databases

EvolutionaryTraceⁱ	P37090.
PROⁱ	P37090.

Family and domain databases

InterProⁱ	IPR004724. ENaC. IPR001873. Na+channel_ASC. IPR020903. Na+channel_ASC_CS. [Graphical view]
PANTHERⁱ	PTHR11690. PTHR11690. 2 hits.
Pfamⁱ	PF00858. ASC. 1 hit. [Graphical view]
PRINTSⁱ	PR01078. AMINACHANNEL.
TIGRFAMsⁱ	TIGR00859. ENaC. 1 hit.
PROSITEⁱ	PS01206. ASC. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

SCNNB_RAT

Accessionⁱ

Primary (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:	July 6, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P37090 (SCNNB_RAT)

UniProt

P37090 - SCNNB_RAT

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Amiloride-sensitive sodium channel subunit beta

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<p>Describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.</p><p><a href='../manual/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ