Scnn1g
entrez
20278
canonical
uniprot
Q9WU39
canonical
ensembl
ENSMUSG00000000216
resolver
ensp
ENSMUSP00000000221
resolver
enst
ENSMUST00000000221
resolver
genesymbol
Scnn1g
resolver
uniprot_entry
SCNNG_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Originally identified and characterized by its inhibition by the diuretic drug amiloride. {ECO:0000269|PubMed:10409305, ECO:0000269|PubMed:12871941, ECO:0000269|PubMed:15007080}.
uniprot
proteins
amino_acid_sequence
MAPGEKIKAKIKKNLPVRGPQAPTIKDLMHWYCLNTNTHGCRRIVVSRGRLRRLLWIAFTLTAVALIIWQCALLVFSFYTVSVSIKVHFQKLDFPAVTICNINPYKYSAVSDLLTDLDSETKQALLSLYGVKDVLDSTPRKRREAGSMRSTWEGTPPRFLNLIPLLVFNENEKGKARDFFTGRKRKISGKIIHKASNVMHVHESKKLVGFQLCSNDTSDCATYTFSSGINAIQEWYKLHYMNIMAQVPLEKKINMSYSAEELLVTCFFDGMSCDARNFTLFHHPMYGNCYTFNNRENATILSTSMGGSEYGLQVILYINEDEYNPFLVSSTGAKVLVHQQNEYPFIEDVGTEIETAMSTSIGMHLTESFKLSEPYSQCTEDGSDVPVTNIYNAAYSLQICLYSCFQTKMVEKCGCAQYSQPLPPAANYCNYQQHPNWMYCYYQLYQAFVREELGCQSVCKQSCSFKEWTLTTSLAQWPSEASEKWLLNVLTWDQSQQINKKLNKTDLAKLLIFYKDLNQRSIMESPANSIEMLLSNFGGQLGLWMSCSVVCVIEIIEVFFIDFFSIIARRQWQKAKDWWARRRTPPSTETPSSQQGQDNPALDTDDDLPTFTSAMRLPPAPEAPVPGTPPPRYNTLRLDSAFSSQLTDTQLTNEF
uniprot
proteins
function
FUNCTION: This is one of the three pore-forming subunits of the heterotrimeric epithelial sodium channel (ENaC), a critical regulator of sodium balance and fluid homeostasis (PubMed:10409305, PubMed:12871941, PubMed:15007080). ENaC operates in epithelial tissues, where it mediates the electrodiffusion of sodium ions from extracellular fluid through the apical membrane of cells, with water following osmotically (PubMed:12871941, PubMed:15007080). It plays a key role in maintaining sodium homeostasis through electrogenic sodium reabsorption in the kidneys. Additionally, ENaC is essential for airway surface liquid homeostasis, which is crucial for proper mucus clearance (By similarity). {ECO:0000250|UniProtKB:P51170, ECO:0000269|PubMed:10409305, ECO:0000269|PubMed:12871941, ECO:0000269|PubMed:15007080}.
uniprot
proteins
mass_dalton
74635
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and threonine residues. Aldosterone and insulin increase the basal level of phosphorylation. {ECO:0000250|UniProtKB:P37091}.; PTM: Ubiquitinated. Can be ubiquitinated at multiple sites and undergo monoubiquitination and polyubiquitination. Ubiquitination by NEDD4 or NEDD4L inhibits the ENaC channel through endocytosis, intracellular retention and degradation of its individual subunits. {ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:12424229, ECO:0000269|PubMed:15123669}.; PTM: ENaC is activated through the proteolytic maturation of its subunits. Furin cleaves the SCNN1G subunit first, followed by cleavage by prostasin (PRSS8), which results in a stepwise increase in the open probability of the channel due to the release of an inhibitory tract (PubMed:12871941, PubMed:15007080, PubMed:18650438). BPIFA1, which is recruited by the SCNN1B subunit, prevents the proteolytic activation of ENaC (By similarity). {ECO:0000250|UniProtKB:P51170, ECO:0000269|PubMed:12871941, ECO:0000269|PubMed:15007080, ECO:0000269|PubMed:18650438}.; PTM: N-glycosylated. N-linked glycans are processed to complex type during ENaC complex assembly and transport to the plasma membrane. {ECO:0000269|PubMed:12871941}.
uniprot
proteins
protein_family
Amiloride-sensitive sodium channel (TC 1.A.6) family
uniprot
proteins
protein_family
SCNN1G subfamily
uniprot
proteins
pubmed
10409305
uniprot
proteins
pubmed
11244092
uniprot
proteins
pubmed
12424229
uniprot
proteins
pubmed
12871941
uniprot
proteins
pubmed
15007080
uniprot
proteins
pubmed
15123669
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18650438
uniprot
proteins
sequence_length
655
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305|PubMed:10409305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51170}.
uniprot
proteins
transmembrane_region
TRANSMEM 56..76; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 548..568; /note="Helical; Name=2"; /evidence="ECO:0000255
uniprot
proteins