SCNNG_RABIT
ID SCNNG_RABIT Reviewed; 653 AA.
AC Q28738; Q9N131; Q9TSH7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Amiloride-sensitive sodium channel subunit gamma;
DE AltName: Full=Epithelial Na(+) channel subunit gamma;
DE Short=Gamma-ENaC;
DE AltName: Full=Gamma-NaCH;
DE AltName: Full=Nonvoltage-gated sodium channel 1 subunit gamma;
DE AltName: Full=SCNEG;
GN Name=SCNN1G;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kudlacek O., Weisz E., Wiener H., Plass H.;
RT "The rabbit epithelial sodium channel.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 237-436.
RA Velazquez H., Silva T.C., Andujar E., Jaffer A., Ortiz D.;
RT "The rabbit DCT does not express amiloride sensitive sodium channel.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 432-572.
RX PubMed=8760073; DOI=10.1152/ajpcell.1996.271.1.c423;
RA Denault D.L., Fejes-Toth G., Naray-Fejes-Toth A.;
RT "Aldosterone regulation of sodium channel gamma-subunit mRNA in cortical
RT collecting duct cells.";
RL Am. J. Physiol. 271:C423-C428(1996).
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. Controls
CC the reabsorption of sodium in kidney, colon, lung and sweat glands.
CC Also plays a role in taste perception. {ECO:0000250|UniProtKB:P51170}.
CC -!- ACTIVITY REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
CC {ECO:0000250|UniProtKB:Q9WU39}.
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. Interacts with NEDD4; via
CC the WW domains. Interacts with NEDD4L; via the WW domains. Interacts
CC with WWP1; via the WW domains. Interacts with WWP2; via the WW domains.
CC Interacts with the full length immature form of PCSK9 (pro-PCSK9).
CC {ECO:0000250|UniProtKB:P51170}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P37091}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P37089}. Note=Apical membrane of epithelial
CC cells. {ECO:0000250|UniProtKB:P37091}.
CC -!- PTM: ENaC cleavage by furin, and subsequently by prostasin (PRSS8),
CC leads to a stepwise increase in the open probability of the channel as
CC a result of release of the alpha and gamma subunit inhibitory tracts,
CC respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects
CC ENaC against proteolytic activation. {ECO:0000250|UniProtKB:P51170}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Aldosterone and
CC insulin increase the basal level of phosphorylation.
CC {ECO:0000250|UniProtKB:P37091}.
CC -!- PTM: Ubiquitinated; this targets individual subunits for endocytosis
CC and proteasome-mediated degradation. {ECO:0000250|UniProtKB:P37091}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. SCNN1G subfamily. {ECO:0000305}.
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DR EMBL; AJ132110; CAA10573.1; -; mRNA.
DR EMBL; AF229027; AAF43682.1; -; mRNA.
DR EMBL; U48960; AAB04952.1; -; mRNA.
DR RefSeq; NP_001075595.1; NM_001082126.1.
DR AlphaFoldDB; Q28738; -.
DR SMR; Q28738; -.
DR STRING; 9986.ENSOCUP00000014947; -.
DR PRIDE; Q28738; -.
DR GeneID; 100008850; -.
DR KEGG; ocu:100008850; -.
DR CTD; 6340; -.
DR eggNOG; KOG4294; Eukaryota.
DR InParanoid; Q28738; -.
DR OrthoDB; 686369at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; 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:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sensory transduction; Sodium;
KW Sodium channel; Sodium transport; Taste; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..653
FT /note="Amiloride-sensitive sodium channel subunit gamma"
FT /id="PRO_0000181278"
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..538
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 539..559
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 582..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 267
FT /note="D -> E (in Ref. 2; AAF43682)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="M -> L (in Ref. 3; AAB04952)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="W -> L (in Ref. 3; AAB04952)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="F -> L (in Ref. 3; AAB04952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 74287 MW; C62256B6911F3672 CRC64;
MAPGEKIKAK IKKNLPVKGP QAPTIKELMR WYCLNTNTHG CRRIVVSPGR LRRLLWIAFT
LTAVGLIFWQ CALLVFSFYT VSVSIKVHFQ KLDFPAVTIC NINPYKYSVV RDLLADLEQE
TRGALKSLYG FSEVKSRKQR DTESWSPAWE GVRPKFLNLV PLLIFNRDEK GKARDFLSLG
RKRKISGNII HKASNVVQVH ESKKVVGFQL CPNDSSDCAT YTFSSGINAI QEWYKLHYMN
IMAQVPLEKK INMSYSAEEL LVTCFFDGMS CDARNFTLFH HPMYGNCYTF NNRENETILS
TSMGGSEYGL QVILYINEEE YNPFLVSATG AKVLIHRQDE YPFIEDVGTE IETAMSTSIG
MHLTESFKLS EPYSQCTEDG SDVPIKNIYN AAYSLQICLY SCFQTKMVEK CGCAQYSQPL
PPAANYCNYQ QHPNWMYCYY QLYQAFVQEE LGCQSVCKQS CSFKEWALTT SLAQWPSAVS
EKWLLPVLTW DQGQQINKKL NKTDWAKLLI FYKDLNQRSI MESPANSIEM LLSNFGGQLG
LWMSCSVVCV IEIIEVFFID SLSIVTRRQW QKAKEWWARR KAAPSAEAPS GAQGQENPAL
EIDDDLPTFT SALSLPPAPG AQVPGTPPPR YNTLRLERTF SQQLADTRLP DEP
