SCNNG_PANTR
ID SCNNG_PANTR Reviewed; 585 AA.
AC H2QAR5;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 45.
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 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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
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: 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 -!- 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 -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. SCNN1G subfamily. {ECO:0000305}.
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DR EMBL; AACZ03104215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2QAR5; -.
DR SMR; H2QAR5; -.
DR STRING; 9598.ENSPTRP00000013456; -.
DR PaxDb; H2QAR5; -.
DR eggNOG; KOG4294; Eukaryota.
DR HOGENOM; CLU_020415_0_0_1; -.
DR InParanoid; H2QAR5; -.
DR TreeFam; TF330663; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 2.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
DR PROSITE; PS01206; ASC; 1.
PE 3: Inferred from homology;
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..585
FT /note="Amiloride-sensitive sodium channel subunit gamma"
FT /id="PRO_0000432865"
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..477
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 478..498
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 513..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 66990 MW; A579076F4FE890ED CRC64;
MAPGEKIKAK IKKNLPVTGP QAPTIKELMR WYCLNTNTHG CRRIVVSRGR LRRLLWIGFT
LTAVALILWQ CALLVFSFYT VSVSIKVHFR KLDFPAVTIC NINPYKYSTV RHLLADLEQE
TREALKSLYG FPESRKRREA ESWSSISEGK QPRFSHRIPL LIFDQDEKGK ARDFFTGRKR
KVGGSIIHKA SNVMHIESKQ VVGFQLNFTL FHHPMHGNCY TFNNRENETI LSTSMGGSEY
GLQVILYINE EEYNPFLVSS TGAKVIIHRQ DEYPFVEDVG TEIETAMVTS IGMHLTESFK
LSEPYSQCTE DGSDVPIRNI YNAAYSLQIC LHSCFQTKMV EKCGCAQYSQ PLPPAANYCN
YQQHPNWMYC YYQLHRAFVQ EELGCQSVCK EACSFKEWTL TTSLAQWPSV VSEKWLLPVL
TWDQGRQVNK KLNKTDLAKL LIFYKDLNQR SIMESPANSI EMLLSNFGGQ LGLWMSCSVV
CVIEIIEVFF IDFFSIIARR QWQKAKEWWA RKQAPPCPEA PRSPQGQDNP ALDIDDDLPT
FNSALHLPPA LGTQVPGTPP PKYNTLRLER AFSNQLTDTQ MLDEL
