SCNNA_XENLA
ID SCNNA_XENLA Reviewed; 632 AA.
AC P51167;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Amiloride-sensitive sodium channel subunit alpha;
DE AltName: Full=Alpha-NaCH;
DE AltName: Full=Epithelial Na(+) channel subunit alpha;
DE Short=Alpha-ENaC;
DE AltName: Full=Nonvoltage-gated sodium channel 1 subunit alpha;
DE AltName: Full=SCNEA;
GN Name=scnn1a;
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=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).
RN [2]
RP INTERACTION WITH SHROOM1.
RX PubMed=10438504; DOI=10.1074/jbc.274.33.23286;
RA Zuckerman J.B., Chen X., Jacobs J.D., Hu B., Kleyman T.R., Smith P.R.;
RT "Association of the epithelial sodium channel with Apx and alpha-spectrin
RT in A6 renal epithelial cells.";
RL J. Biol. Chem. 274:23286-23295(1999).
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:P37088, 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 (Probable). Interacts with
CC shroom1 (PubMed:10438504). {ECO:0000269|PubMed:10438504,
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}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:P37088}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P37088}. Cytoplasm
CC {ECO:0000250|UniProtKB:P37088}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium,
CC flagellum {ECO:0000250|UniProtKB:P37089}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. SCNN1A subfamily. {ECO:0000305}.
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DR EMBL; U23535; AAA74970.1; -; mRNA.
DR PIR; I51682; I51682.
DR RefSeq; NP_001081392.1; NM_001087923.1.
DR AlphaFoldDB; P51167; -.
DR SMR; P51167; -.
DR GeneID; 397811; -.
DR KEGG; xla:397811; -.
DR CTD; 397811; -.
DR Xenbase; XB-GENE-996110; scnn1a.L.
DR OrthoDB; 686369at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 397811; Expressed in lung and 12 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; 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; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW Flagellum; Ion channel; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..632
FT /note="Amiloride-sensitive sodium channel subunit alpha"
FT /id="PRO_0000181266"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 50..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..520
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 521..541
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 612..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 72627 MW; B771519A8A601031 CRC64;
MTKEEKNEKE ALIEFFSSYR ELFEFFCSNT TIHGAIRLVC SRRNRMKTAF WLVLFLVTFG
LMYWQFGLLF GQYFSYPVSI NLNVNSDKLP FPAVTVCTLN PYRYKAIQND LQELDKETQR
TLYELYKYNS TGVQGWIPNN QRVKRDRAGL PYLLELLPPG SETHRVSRSV IEEELQVKRR
EWNIGFKLCN ETGGDCFYQT YTSGVDAIRE WYRFHYINIL ARVPQEAAID GEQLENFIFA
CRFNEESCTK ANYSSFHHAI YGNCYTFNQN QSDQSNLWSS SMPGIKNGLT LVLRTEQHDY
IPLLSSVAGA RVLVHGHKEP AFMDDNGFNI PPGMETSIGM KKETINRLGG KYSDCSEDGS
DVDVKNLFQS EYTEQVCVRS CFQAAMVARC GCGYAFYPLS PGDQYCDYNK HKSWGHCYYK
LIIEFTSNKL GCFTKCRKPC LVSEYQLTAG YSKWPNRVSQ DWVLHTLSRQ YNLTDRNGIA
KLNIYFEELN YKTILESPTI NMAMLLSLLG SQWSLWFGSS VLSVVEMLEL VIDFVIIGVM
ILLHRYYYKK ANEGEETTVV PTPAPAFADL EQQVPHIPRG DLSQRQISVV ADITPPPAYE
SLDLRSVGTL SSRSSSMRSN RSYYEENGGR RN
