ID   SCNNH_XENLA             Reviewed;         663 AA.
AC   O13263;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Amiloride-sensitive sodium channel subunit gamma-2;
DE   AltName: Full=Epithelial Na(+) channel subunit gamma-2;
DE            Short=Gamma-2-ENaC;
DE   AltName: Full=Gamma-2-NaCH;
DE   AltName: Full=Nonvoltage-gated sodium channel 1 subunit gamma-2;
DE   AltName: Full=SCNEG2;
GN   Name=scnn1g-b;
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.
RX   PubMed=9159181; DOI=10.1073/pnas.94.11.5949;
RA   Puoti A., May A., Rossier B.C., Horisberger J.-D.;
RT   "Novel isoforms of the beta and gamma subunits of the Xenopus epithelial Na
RT   channel provide information about the amiloride binding site and
RT   extracellular sodium sensing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5949-5954(1997).
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:9159181}.
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:9159181}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000305|PubMed:9159181}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P37089}. Note=Apical membrane of epithelial
CC       cells. {ECO:0000305|PubMed:9159181}.
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; Y12001; CAA72730.1; -; mRNA.
DR   RefSeq; NP_001079131.1; NM_001085662.1.
DR   AlphaFoldDB; O13263; -.
DR   SMR; O13263; -.
DR   GeneID; 373668; -.
DR   KEGG; xla:373668; -.
DR   CTD; 373668; -.
DR   Xenbase; XB-GENE-6252871; scnn1g.S.
DR   OrthoDB; 686369at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 373668; Expressed in egg cell and 8 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015280; F:ligand-gated sodium channel activity; IEA:InterPro.
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..663
FT                   /note="Amiloride-sensitive sodium channel subunit gamma-2"
FT                   /id="PRO_0000181281"
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..544
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   TRANSMEM        545..565
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        566..663
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
SQ   SEQUENCE   663 AA;  75881 MW;  35E20225DF6B80CC CRC64;
     MSNSGKKLTQ KLKKNLPVTG PQAPTLYELM QWYCLNTNTH GCRRIVVSKG RLRRWIWIVL
     TLIAVALIFW QCALLLMTYY SVSASITVTF QKLVYPAVTI CNLNPYSYSK IKDRLATLEK
     TTNQTLKKIY GFTEPLIRSK RDLDVNDENS TEDIFLKQIP LFRLESIKGN QLVVSDLKTK
     KRTQISGKVI QRDAGSVQDS DNMVGFKLCD ANNSSDCTIF TFGSGVNAIQ EWYRLHYNNI
     LAKISMEDKI AMGYKADELI VTCLFDGLSC DARNFTLFHH PLYGNCYTFN SAERGNLLVS
     SMGGAEYGLK VVLYIDEDEY NPYLSTAAGA KILVHDQDEY PFIEDLGTEL ETGTETSIGM
     QLTESTKLSD PYSDCTIDGS DISVENLYNK KYTLQICLNS CFQREMVRSC GCAHYDQPLP
     NGAKYCNYEE YPNWIYCYVK LYKQFVQEEL GCQSTCRESC SFKEWTLTRS LAKWPSLNSE
     EWMLRVLSWE LGEKLNKNLT KNDLGNLNIF YQDLNSRSIS ESPTYNIVTL LSNFGGQLGL
     WMSCSMVCGL EIVEVFFIDS FWVILRQKWH KLCNWWKNRK ENEIEEIPDI TVPAMAGHNN
     PLCVDHPICL GEDDPPTFHS ALQLPQAQDC RVPRTPPPKY NTLRIQSAFH LETIDSDEDV
     ERF