ID   SCNND_PANTR             Reviewed;         638 AA.
AC   O46547;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Amiloride-sensitive sodium channel subunit delta;
DE   AltName: Full=Delta-NaCH;
DE   AltName: Full=Epithelial Na(+) channel subunit delta;
DE            Short=Delta-ENaC;
DE   AltName: Full=Nonvoltage-gated sodium channel 1 subunit delta;
DE   AltName: Full=SCNED;
GN   Name=SCNN1D; Synonyms=DNACH;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Al-Khalili O.K., Eaton D.C.;
RL   Submitted (DEC-1997) 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. Controls the reabsorption of sodium in
CC       kidney, colon, lung and sweat glands. Also plays a role in taste
CC       perception. {ECO:0000250|UniProtKB:P51172}.
CC   -!- SUBUNIT: Heterotrimer containing a delta/SCNN1D, a beta/SCNN1B and a
CC       gamma/SCNN1G subunit. The additional delta/SCNN1D subunit exists only
CC       in some organisms and can replace the alpha/SCNN1A subunit to form an
CC       alternative channel with specific properties.
CC       {ECO:0000250|UniProtKB:P51172}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51172};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P51172}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. SCNN1D subfamily. {ECO:0000305}.
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DR   EMBL; AF038165; AAB92659.1; -; mRNA.
DR   RefSeq; NP_001009072.1; NM_001009072.1.
DR   AlphaFoldDB; O46547; -.
DR   SMR; O46547; -.
DR   STRING; 9598.ENSPTRP00000054494; -.
DR   GeneID; 450189; -.
DR   CTD; 6339; -.
DR   eggNOG; KOG4294; Eukaryota.
DR   InParanoid; O46547; -.
DR   Proteomes; UP000002277; Unplaced.
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; IBA:GO_Central.
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; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Sensory transduction; Sodium; Sodium channel;
KW   Sodium transport; Taste; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..638
FT                   /note="Amiloride-sensitive sodium channel subunit delta"
FT                   /id="PRO_0000181283"
FT   TOPO_DOM        1..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P51172"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..530
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P51172"
FT   TRANSMEM        531..551
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        552..638
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P51172"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   638 AA;  70188 MW;  321E9597D6A78D38 CRC64;
     MAEHRSMDGR MEAATRGGSH LQAAAQTPPR PGPPSAPPPP PKEGHQEGLV ELPASFRELL
     TFFCTNATIH GAIRLVCSRG NRLKTTSWGL LSLGALVALC WQLGLLFERH WHRPVLMAVS
     VHSERKLLPL VTLCDGNPRR PSPVLRHLEL LDEFARENID SLYNVNLSQG RAALSAPVPR
     HEPPFHLDRE IRLQRLSHSG SRVRVGFRLC NSTGGDCFYR GYTSGVAAVQ DWCHFHYVDI
     LALLPAAWED SHGSQDGHFV LSCSYDGLDC QARQFRTFHH PTYGSCYTVD GVWTAQRPGI
     THGVGLVLRV EQQPHLPLLS TLAGIRVMVH GRNHTPFLGH HSFSVRPGTE ATISIREDEV
     HRLGSPYGHC TAGAEGVEVE LLHNTSYTRQ ACLVSCFQQL MVETCSCGYY LHPLPAGAEY
     CSSARHPAWG HCFYRLYQDL ETHRLPCTSR CPRPCRESAF KLSTGTSRWP SAKSAGWTLA
     TLGEQGLPRQ SHRQRSSLAK INIVYQELNY RSVEEAPVYS VPQLLSAMGS LCSLWFGASV
     LSLLELLELL LDASALTLVL GGRRLRRAWF SWPRASPASG ASSIKPEASQ MPTPAGGTSD
     DPEPSGPHLP RVMLPGVLAG VSAEESWAGP QPLETLDT