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-APR-2013, entry version 84.
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;
OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7631745;
RA Puoti A., May A., Canessa C.M., Horisberger J.-D., Schild L.,
RA 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-
RT spectrin in A6 renal epithelial cells.";
RL J. Biol. Chem. 274:23286-23295(1999).
CC -!- FUNCTION: Sodium permeable non-voltage-sensitive ion channel
CC inhibited by the diuretic amiloride. Mediates the electrodiffusion
CC of the luminal sodium (and water, which follows osmotically)
CC through the apical membrane of epithelial cells. Controls the
CC reabsorption of sodium in kidney, colon, lung and sweat glands.
CC Also plays a role in taste perception.
CC -!- SUBUNIT: Probable heterotrimer containing one alpha, one beta and
CC one gamma subunit. A delta subunit can replace the alpha subunit
CC (By similarity). Interacts with shroom1.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane
CC protein (By similarity). Note=Apical membrane of epithelial cells
CC (By similarity).
CC -!- PTM: Ubiquitinated; this targets individual subunits for
CC proteasome-mediated degradation (By similarity).
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel
CC (TC 1.A.6) family. SCNN1A subfamily.
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DR EMBL; U23535; AAA74970.1; -; mRNA.
DR PIR; I51682; I51682.
DR RefSeq; NP_001081392.1; NM_001087923.1.
DR UniGene; Xl.2464; -.
DR GeneID; 397811; -.
DR KEGG; xla:397811; -.
DR CTD; 6337; -.
DR Xenbase; XB-GENE-996110; scnn1a.
DR HOVERGEN; HBG058435; -.
DR KO; K04824; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IEA:InterPro.
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; IEA:GOC.
DR InterPro; IPR004724; EnaC.
DR InterPro; IPR001873; Na+channel_ASC.
DR InterPro; IPR020903; Na+channel_ASC_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; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Sensory transduction; Sodium; Sodium channel; Sodium transport; Taste;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1 632 Amiloride-sensitive sodium channel
FT subunit alpha.
FT /FTId=PRO_0000181266.
FT TOPO_DOM 1 50 Cytoplasmic (By similarity).
FT TRANSMEM 51 74 Helical; (By similarity).
FT TOPO_DOM 75 501 Extracellular (By similarity).
FT TRANSMEM 502 532 Helical; (By similarity).
FT TOPO_DOM 533 632 Cytoplasmic (By similarity).
FT CARBOHYD 129 129 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 190 190 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 252 252 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 270 270 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 472 472 N-linked (GlcNAc...) (Potential).
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
//
