SCNN1G
entrez
6340
canonical
uniprot
P51170
canonical
ensembl
ENSG00000166828
resolver
ensp
ENSP00000300061
resolver
ensp
ENSP00000546201
resolver
enst
ENST00000300061
resolver
enst
ENST00000876142
resolver
genesymbol
SCNN1G
resolver
hgnc
HGNC:10602
resolver
uniprot
A5X2V1
resolver
uniprot
P78437
resolver
uniprot
Q6PCC2
resolver
uniprot
Q93023
resolver
uniprot
Q93024
resolver
uniprot
Q93025
resolver
uniprot
Q93026
resolver
uniprot
Q93027
resolver
uniprot
Q96TD2
resolver
uniprot_entry
A5X2V1_HUMAN
resolver
uniprot_entry
SCNNG_HUMAN
resolver
uniprot_sec
P78437
resolver
uniprot_sec
Q6PCC2
resolver
uniprot_sec
Q93023
resolver
uniprot_sec
Q93024
resolver
uniprot_sec
Q93025
resolver
uniprot_sec
Q93026
resolver
uniprot_sec
Q93027
resolver
uniprot_sec
Q96TD2
resolver
activity_regulation
ACTIVITY REGULATION: Originally identified and characterized by its inhibition by the diuretic drug amiloride. {ECO:0000269|PubMed:7762608, ECO:0000269|PubMed:9792722}.
uniprot
proteins
amino_acid_sequence
MAPGEKIKAKIKKNLPVTGPQAPTIKELMRWYCLNTNTHGCRRIVVSRGRLRRLLWIGFTLTAVALILWQCALLVFSFYTVSVSIKVHFRKLDFPAVTICNINPYKYSTVRHLLADLEQETREALKSLYGFPESRKRREAESWNSVSEGKQPRFSHRIPLLIFDQDEKGKARDFFTGRKRKVGGSIIHKASNVMHIESKQVVGFQLCSNDTSDCATYTFSSGINAIQEWYKLHYMNIMAQVPLEKKINMSYSAEELLVTCFFDGVSCDARNFTLFHHPMHGNCYTFNNRENETILSTSMGGSEYGLQVILYINEEEYNPFLVSSTGAKVIIHRQDEYPFVEDVGTEIETAMVTSIGMHLTESFKLSEPYSQCTEDGSDVPIRNIYNAAYSLQICLHSCFQTKMVEKCGCAQYSQPLPPAANYCNYQQHPNWMYCYYQLHRAFVQEELGCQSVCKEACSFKEWTLTTSLAQWPSVVSEKWLLPVLTWDQGRQVNKKLNKTDLAKLLIFYKDLNQRSIMESPANSIEMLLSNFGGQLGLWMSCSVVCVIEIIEVFFIDFFSIIARRQWQKAKEWWAWKQAPPCPEAPRSPQGQDNPALDIDDDLPTFNSALHLPPALGTQVPGTPPPKYNTLRLERAFSNQLTDTQMLDEL
uniprot
proteins
disease_involvement
DISEASE: Liddle syndrome 2 (LIDLS2) [MIM:618114]: A form of Liddle syndrome, an autosomal dominant disorder characterized by early onset of hypertension, hypokalemic alkalosis, and suppression of plasma renin activity and aldosterone secretion. {ECO:0000269|PubMed:12473862, ECO:0000269|PubMed:17634077, ECO:0000269|PubMed:7550319}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bronchiectasis with or without elevated sweat chloride 3 (BESC3) [MIM:613071]: A debilitating respiratory disease characterized by chronic, abnormal dilatation of the bronchi and other cystic fibrosis-like symptoms in the absence of known causes of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary dyskinesia, common variable immunodeficiency, foreign body obstruction). Clinical features include sub-normal lung function, sinopulmonary infections, chronic productive cough, excessive sputum production, and elevated sweat chloride in some cases. {ECO:0000269|PubMed:18507830, ECO:0000269|PubMed:19017867}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pseudohypoaldosteronism 1B3, autosomal recessive (PHA1B3) [MIM:620126]: A form of pseudohypoaldosteronism type 1, a rare salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. The disorder affects multiple organs, and is characterized by an often fulminant presentation in the neonatal period with dehydration, hyponatremia, hyperkalemia, metabolic acidosis, failure to thrive and weight loss. {ECO:0000269|PubMed:8640238}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:30251954, PubMed:32729833, PubMed:7550319, PubMed:7762608, PubMed:9792722). 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:24124190). It plays a key role in maintaining sodium homeostasis through electrogenic sodium reabsorption in the kidneys (PubMed:12107247, PubMed:7550319, PubMed:8640238). Additionally, ENaC is essential for airway surface liquid homeostasis, which is crucial for proper mucus clearance (PubMed:18507830, PubMed:19017867, PubMed:24124190). {ECO:0000269|PubMed:12107247, ECO:0000269|PubMed:18507830, ECO:0000269|PubMed:19017867, ECO:0000269|PubMed:24124190, ECO:0000269|PubMed:30251954, ECO:0000269|PubMed:32729833, ECO:0000269|PubMed:7550319, ECO:0000269|PubMed:7762608, ECO:0000269|PubMed:8640238, ECO:0000269|PubMed:9792722}.
uniprot
proteins
mass_dalton
74270
uniprot
proteins
mutagenesis
MUTAGEN 627; /note="Y->A: Loss of ubiquitination by NEDD4L."; /evidence="ECO:0000269|PubMed:17502380
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:12167593, ECO:0000269|PubMed:17502380, ECO:0000269|PubMed:9792722}.; 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:24124190). BPIFA1, which is recruited by the SCNN1B subunit, prevents the proteolytic activation of ENaC (PubMed:24124190). {ECO:0000269|PubMed:24124190}.; PTM: N-glycosylated. N-linked glycans are processed to complex type during ENaC complex assembly and transport to the plasma membrane. {ECO:0000250|UniProtKB:Q9WU39}.
uniprot
proteins
protein_family
Amiloride-sensitive sodium channel (TC 1.A.6) family
uniprot
proteins
protein_family
SCNN1G subfamily
uniprot
proteins
pubmed
10391210
uniprot
proteins
pubmed
10404817
uniprot
proteins
pubmed
11244092
uniprot
proteins
pubmed
12107247
uniprot
proteins
pubmed
12167593
uniprot
proteins
pubmed
12473862
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16423824
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17502380
uniprot
proteins
pubmed
17634077
uniprot
proteins
pubmed
18507830
uniprot
proteins
pubmed
19017867
uniprot
proteins
pubmed
22207244
uniprot
proteins
pubmed
22493497
uniprot
proteins
pubmed
24124190
uniprot
proteins
pubmed
26772908
uniprot
proteins
pubmed
30251954
uniprot
proteins
pubmed
32729833
uniprot
proteins
pubmed
7490094
uniprot
proteins
pubmed
7499195
uniprot
proteins
pubmed
7550319
uniprot
proteins
pubmed
7762608
uniprot
proteins
pubmed
8640238
uniprot
proteins
pubmed
8824247
uniprot
proteins
pubmed
9169421
uniprot
proteins
pubmed
9792722
uniprot
proteins
sequence_length
649
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:24124190}; Multi-pass membrane protein {ECO:0000269|PubMed:30251954, ECO:0000269|PubMed:32729833}.
uniprot
proteins
transmembrane_region
TRANSMEM 56..76; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 542..562; /note="Helical; Name=2"; /evidence="ECO:0000255
uniprot
proteins