SCNNA_NEOFS
ID SCNNA_NEOFS Reviewed; 655 AA.
AC H1AFJ5;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 25-MAY-2022, entry version 28.
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; Synonyms=enacalpha {ECO:0000312|EMBL:BAL46406.1};
OS Neoceratodus forsteri (Australian lungfish) (Ceratodus forsteri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Dipnomorpha; Ceratodontiformes; Ceratodontoidei; Ceratodontidae;
OC Neoceratodus.
OX NCBI_TaxID=7892;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Gill;
RX PubMed=23055064; DOI=10.1098/rspb.2012.1945;
RA Uchiyama M., Maejima S., Yoshie S., Kubo Y., Konno N., Joss J.M.P.;
RT "The epithelial sodium channel in the Australian lungfish, Neoceratodus
RT forsteri (Osteichthyes: Dipnoi).";
RL Proc. R. Soc. B 279:4795-4802(2012).
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:23055064}.
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:P37088}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:23055064}; 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 -!- TISSUE SPECIFICITY: Strongly expressed in gill, kidney and rectum (at
CC protein level). More weakly expressed in muscle, brain, heart, liver
CC and intestine. {ECO:0000269|PubMed:23055064}.
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; AB675922; BAL46406.1; -; mRNA.
DR AlphaFoldDB; H1AFJ5; -.
DR SMR; H1AFJ5; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0034706; C:sodium channel complex; IC:UniProtKB.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IEA:InterPro.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA: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; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..655
FT /note="Amiloride-sensitive sodium channel subunit alpha"
FT /id="PRO_0000433086"
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..531
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 532..552
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 561..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 73378 MW; 615705BF0772518F CRC64;
MTDKEEEAEG GKKKEPMIGF YDSYQELFEF FCNNTTIHGT IRMVCSKHNN MKTVSWTILF
ITTFGVMYWQ FGLLLGQYYS YPVSITMSVN FDKLIFPAVT VCTLNPYRYN VVSTQLANLD
CYTEELLSTL YHYNPLTSGN QSACNSSSTA GTRAFDESYM KLEFLNDENT AYSGPVKGAT
NSTSPVNHTE FYRIGFKLCN ATGEDCFYQT YSSGVDALRE WYKFQYINIM AQIPSQSNQE
DDSQISNFVY ACEFNKVSCG VENYTRFRHP VYGNCYTYND GQSATPWASF VPGVGNGLSL
VLRTEQNDFL PFLSTVAGAR VLVHDQNQPP FMEDSGLDIR PGVETSIGMK KEIISRLGGV
YGNCTDGSDI DVVNLYNSDY NQQACVRSCF QATIVQQCGC GYYFYPLPSG AEYCSYSRNK
SWGYCYYKLY KAFAADELGC FRRCRKPCQY TDYKMTAGYA QWPSSVSESW ITSILSQENQ
YNMTSGRKNI AKLNVYFYEL NYQTMGESPS FTVVTLLSNM GSQWSLWFGS SVLSVVEMGE
LVFDLIAVGV IVLRRRRREK CQASSDGEGT SDSTAGTHRG QENASRSGRD VACNRFVVVA
EISPPPAYDT LQLDVPVACA PDCECTQHVS HASVHSQAPC SSQPEQEASE GPTVL
