ID   SCNNC_XENLA             Reviewed;         646 AA.
AC   O13262; Q5D066;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Amiloride-sensitive sodium channel subunit beta-2;
DE   AltName: Full=Beta-2-NaCH;
DE   AltName: Full=Epithelial Na(+) channel subunit beta-2;
DE            Short=Beta-2-ENaC;
DE   AltName: Full=Nonvoltage-gated sodium channel 1 subunit beta-2;
DE   AltName: Full=SCNEB2;
GN   Name=scnn1b-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].
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P51169}.
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:0000250|UniProtKB:P51169}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P51169}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial
CC       cells. {ECO:0000250|UniProtKB:P51169}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. SCNN1B subfamily. {ECO:0000305}.
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DR   EMBL; Y12000; CAA72729.1; -; mRNA.
DR   EMBL; BC059965; AAH59965.1; -; mRNA.
DR   RefSeq; NP_001081525.1; NM_001088056.1.
DR   AlphaFoldDB; O13262; -.
DR   SMR; O13262; -.
DR   DNASU; 397893; -.
DR   GeneID; 397893; -.
DR   KEGG; xla:397893; -.
DR   CTD; 397893; -.
DR   Xenbase; XB-GENE-6252312; scnn1b.S.
DR   OrthoDB; 686369at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 397893; Expressed in kidney and 12 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030659; C:cytoplasmic vesicle 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   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..646
FT                   /note="Amiloride-sensitive sodium channel subunit beta-2"
FT                   /id="PRO_0000181275"
FT   TOPO_DOM        1..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..551
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   TRANSMEM        552..572
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        573..646
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P37089"
FT   REGION          586..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  74112 MW;  30126C9D864BFBF0 CRC64;
     MIQGKLKRLK RYFTRALHRI QKGPGYTYKE LLVWFCDNTN THGPKRIIKE GPKKRVMWFI
     LTLVFAGLVF WQWGLLILTY LSYGVSVSLS IGFKTMEFPA VTVCNTNPYK YSRVKPLLKD
     LDELVATALD RIQYSSQTQA NTFTYNNTRQ NVTLDPALWN HIPLVVIDEN DPSNPVIHNI
     FDNSVFYSKN NLLRNSSEDQ TSYAQRYKVA MKLCTNNNTQ CVYRNFTSGV QALREWYLLQ
     LSIIFSNVPL SDRVDMGFKA EDLILTCLFG GQPCSYRNFT HIYDADYGNC YIFNWGQEGD
     DTMSSANPGA DFGLKLVLDI EQDEYLPFLQ TTAAARLILH QQRSFPFVKD LGIYAKPGTE
     TSIAVLVDQL QQMEAPYSSC TVNGSDIPVQ NLYEEFNSSY SIQSCLRSCY QEEMVKTCKC
     AHYQYPLPNG SEYCTNNKHP DWVPCYYGLR DSVAIRENCI SLCQQPCNDT HYKMVISMAD
     WPSAGAEDWI FHVLSYEKDS SYDITVNRNG IIRLNIYFQE FNYRSISESE ATNVVWLLSN
     LGGQFGFWMG GSVLCIIEFG EIIIDCMWIT ILKLLAWIRN RRQRRQRPQY ADPPPTVSEL
     VEAHTNPGFQ HDDGNHVTED IPGTPPPNYD SLRVNTIEPV SSDEEN