SCNNG_BOVIN
ID SCNNG_BOVIN Reviewed; 652 AA.
AC F1MJW3;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Amiloride-sensitive sodium channel subunit gamma;
DE AltName: Full=Epithelial Na(+) channel subunit gamma;
DE Short=Gamma-ENaC;
DE AltName: Full=Gamma-NaCH;
DE AltName: Full=Nonvoltage-gated sodium channel 1 subunit gamma;
DE AltName: Full=SCNEG;
GN Name=SCNN1G;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited
CC by the diuretic amiloride. Mediates the electrodiffusion of the luminal
CC sodium (and water, which follows osmotically) through the apical
CC membrane of epithelial cells. Plays an essential role in electrolyte
CC and blood pressure homeostasis, but also in airway surface liquid
CC homeostasis, which is important for proper clearance of mucus. Controls
CC the reabsorption of sodium in kidney, colon, lung and sweat glands.
CC Also plays a role in taste perception. {ECO:0000250|UniProtKB:P51170}.
CC -!- ACTIVITY REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
CC {ECO:0000250|UniProtKB:Q9WU39}.
CC -!- SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a
CC gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in
CC some organisms and can replace the alpha/SCNN1A subunit to form an
CC alternative channel with specific properties. Interacts with NEDD4; via
CC the WW domains. Interacts with NEDD4L; via the WW domains. Interacts
CC with WWP1; via the WW domains. Interacts with WWP2; via the WW domains.
CC Interacts with the full length immature form of PCSK9 (pro-PCSK9).
CC {ECO:0000250|UniProtKB:P51170}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P37091}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P37089}. Note=Apical membrane of epithelial
CC cells. {ECO:0000250|UniProtKB:P37091}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Aldosterone and
CC insulin increase the basal level of phosphorylation.
CC {ECO:0000250|UniProtKB:P37091}.
CC -!- PTM: Ubiquitinated; this targets individual subunits for endocytosis
CC and proteasome-mediated degradation. {ECO:0000250|UniProtKB:P37091}.
CC -!- PTM: ENaC cleavage by furin, and subsequently by prostasin (PRSS8),
CC leads to a stepwise increase in the open probability of the channel as
CC a result of release of the alpha and gamma subunit inhibitory tracts,
CC respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects
CC ENaC against proteolytic activation. {ECO:0000250|UniProtKB:P51170}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. SCNN1G subfamily. {ECO:0000305}.
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DR EMBL; DAAA02057732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001180103.1; NM_001193174.1.
DR RefSeq; XP_005224821.1; XM_005224764.3.
DR AlphaFoldDB; F1MJW3; -.
DR SMR; F1MJW3; -.
DR STRING; 9913.ENSBTAP00000013412; -.
DR PaxDb; F1MJW3; -.
DR Ensembl; ENSBTAT00000013412; ENSBTAP00000013412; ENSBTAG00000010163.
DR GeneID; 617802; -.
DR KEGG; bta:617802; -.
DR CTD; 6340; -.
DR VEuPathDB; HostDB:ENSBTAG00000010163; -.
DR VGNC; VGNC:34358; SCNN1G.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000160352; -.
DR HOGENOM; CLU_020415_0_0_1; -.
DR InParanoid; F1MJW3; -.
DR OMA; MHVHESK; -.
DR OrthoDB; 686369at2759; -.
DR TreeFam; TF330663; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000010163; Expressed in adult mammalian kidney and 56 other tissues.
DR ExpressionAtlas; F1MJW3; differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0034706; C:sodium channel complex; IBA:GO_Central.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
DR PROSITE; PS01206; ASC; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sensory transduction; Sodium;
KW Sodium channel; Sodium transport; Taste; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..652
FT /note="Amiloride-sensitive sodium channel subunit gamma"
FT /id="PRO_0000432863"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..537
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 538..558
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 610..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 652 AA; 74321 MW; 36EFEC2AB7253826 CRC64;
MAPGEKIKAK IKKNLPVTGP QAPNIKELMQ WYCLNTNTHG CRRIVVSRGR LRRLLWILFT
LTAVALIFWQ CALLISSFYT VSVSIKVHFQ KLDFPAVTIC NINPYKYSAV RHLLADLEQE
TRAALKTLYG FSEITSRKRR EAQSWSSVRK GTDPKFLNLA PLMAFEKGDT GKARDFFTGR
KRKVNARIIH KASDVMHIHN SKEVVGFQLC SNDTSDCAVY TFSSGVNAIQ EWYKLHYMNI
MAQVSQEKKI NMSYSADELL VTCFFDGVSC DARNFTLFHH PMYGNCYTFN NRQNETILST
SMGGSEFGLQ VILYINEEEY NPFLVSSTGA KVIIHRQDEY PFVEDVGTEI ETAMATSIGM
HLTESFKLSD PYSQCTEDWS DVQITNIYNA TYSLQICLHS CFQAKMVENC GCAQYSQPLP
RGADYCNYQQ HPNWMYCYYQ LHQAFVREEL GCQSVCKEAC SFKEWTLTTS LAQWPSEVSE
KWLLSILTWD QSQQIKKKLN KTDLAKLLIF YKDLNQRSIM ENPANSIEQL LSNIGGQLGL
WMSCSVVCVI EIIEVFFIDS LSIIARHQWH KAKGWWARRR APACPEAPRA PQGRDNPSLD
IDDDLPTFTS ALSLPPAPGS QVPGTPPPRY NTLRLERAFS SQLTDTQTTF PH
