SCNNG_XENLA
ID SCNNG_XENLA Reviewed; 660 AA.
AC P51171;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
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-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=7631745; DOI=10.1152/ajpcell.1995.269.1.c188;
RA Puoti A., May A., Canessa C.M., Horisberger J.-D., Schild L., Rossier B.C.;
RT "The highly selective low-conductance epithelial Na channel of Xenopus
RT laevis A6 kidney cells.";
RL Am. J. Physiol. 269:C188-C197(1995).
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.
CC {ECO:0000269|PubMed:7631745}.
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.
CC {ECO:0000305|PubMed:7631745}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000305|PubMed:7631745}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P37089}. Note=Apical membrane of epithelial
CC cells. {ECO:0000305|PubMed:7631745}.
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; U25342; AAA74972.1; -; mRNA.
DR PIR; I51684; I51684.
DR RefSeq; NP_001079123.1; NM_001085654.1.
DR AlphaFoldDB; P51171; -.
DR SMR; P51171; -.
DR PRIDE; P51171; -.
DR GeneID; 373658; -.
DR KEGG; xla:373658; -.
DR CTD; 373658; -.
DR Xenbase; XB-GENE-980900; scnn1g.L.
DR OrthoDB; 686369at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 373658; Expressed in kidney and 12 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0034706; C:sodium channel complex; ISS:UniProtKB.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IEA:InterPro.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
DR GO; GO:0055078; P:sodium ion homeostasis; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..660
FT /note="Amiloride-sensitive sodium channel subunit gamma"
FT /id="PRO_0000181280"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 56..76
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..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..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
SQ SEQUENCE 660 AA; 75622 MW; 67355F6DCEE50B1C CRC64;
MSKSGKKLTQ KLKKNLPVTG PQAPTLYELM QWYCLNTNTH GCRRIVVSKG RLRRWIWISL
TLCAVAVIFW QCALLLMSYY SVSASITVTF QKLVYPAVTI CNLNPYSYSK VKDRLAALEK
ETSQTLKNIY GFTEPLIRSK RDVGVNVENS TEDIFLKQIP LYRLESVKGS QLVVSDLKTK
KRTRMSAKVI HRDAESVQDP GNMVGFKLCD PKNSSDCTIF TFSSGVNAIQ EWYRLHYTNI
LAKISMEDKI AMGYKADELI VTCFFDGLSC DARNFTLFHH PLYGNCYTFN SAERGNLLVS
SMGGAEYGLK VVLYIDEDEY NPYLSTAAGA KILVHDQDEY PFIEYLGTEL ETATETSIGM
QLTESAKLSD PYSDCTMDGR DVSVENLYNK KYTLQICLNS CFQREMVRSC GCAHYDQPLP
NGAKYCNYEE YPSWIYCYFK VYKQFVQEEL GCQSACRESC SFKEWTLTRS LAKWPSLNSE
EWMLRVLSWE LGEKLNKNLT KNDLANLNIF YQDLNSRSIS ESPTYNIVTL LSNFGGQLGL
WMSCSMICVL EIIEVFFIDS FWVVLRQRWR NWWENRKENQ AEDTPEIPVP TMTGHDNPLC
VDNPICLGEE DPPTFNSALQ LPQSQDSHVP RTPPPKYNTL RIQSAFQLET IDSDEDVERL