SCNNB_PANTR
ID SCNNB_PANTR Reviewed; 650 AA.
AC H2QAR6;
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 beta;
DE AltName: Full=Beta-NaCH;
DE AltName: Full=Epithelial Na(+) channel subunit beta;
DE Short=Beta-ENaC;
DE AltName: Full=Nonvoltage-gated sodium channel 1 subunit beta;
DE AltName: Full=SCNEB;
GN Name=SCNN1B;
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:P51168}.
CC -!- ACTIVITY REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
CC {ECO:0000250|UniProtKB:Q9WU38}.
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 WW domains). Interacts with NEDD4L (via WW domains). Interacts with
CC WWP1 (via WW domains). Interacts with WWP2 (via WW domains). Interacts
CC with the full-length immature form of PCSK9 (pro-PCSK9). Interacts (N-
CC glycosylated) with BPIFA1; the interaction is direct and inhibits the
CC proteolytic processing of SCNN1A and SCNN1G and the activation of ENaC.
CC {ECO:0000250|UniProtKB:P51168}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P37090}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial
CC cells. {ECO:0000250|UniProtKB:P37090}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Aldosterone and
CC insulin increase the basal level of phosphorylation.
CC {ECO:0000250|UniProtKB:P37090}.
CC -!- PTM: N-glycosylated. N-glycosylation is required for interaction with
CC BPIFA1. {ECO:0000250|UniProtKB:P51168}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. SCNN1B subfamily. {ECO:0000305}.
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DR EMBL; AACZ03104220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03104227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ03107266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2QAR6; -.
DR SMR; H2QAR6; -.
DR STRING; 9598.ENSPTRP00000013457; -.
DR PaxDb; H2QAR6; -.
DR eggNOG; KOG4294; Eukaryota.
DR HOGENOM; CLU_020415_0_0_1; -.
DR InParanoid; H2QAR6; -.
DR TreeFam; TF330663; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR11690; PTHR11690; 2.
DR Pfam; PF00858; ASC; 2.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sensory transduction; Sodium; Sodium channel; Sodium transport; Taste;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..650
FT /note="Amiloride-sensitive sodium channel subunit beta"
FT /id="PRO_0000432889"
FT TOPO_DOM 1..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 96..116
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..542
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 543..563
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 600..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU38"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU38"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 650 AA; 73560 MW; E6DA44E18D0E4AB7 CRC64;
MLLHINPAYL FKLLHGFPPW IMPTDGNLGD KNFQMGKPGH REGATMHVKK YLLKGLHRLQ
KGPGYTYKEL LVWYCDNTNT HGPKRIICEG PKKKAMWFLL TLLFTALVCW QWGIFIRTYL
SWEVSVSLSV GFKTMDFPAV TICNASPFKY SKIKHLLKDL DELMEAVLER ILAPELSHAN
ATRNLNFSIW NHTPLVLIDE RNPHHPMVLD LFGDNHNGLT RSSASEKICN AHGCKMAMRL
CSLNGTQCTF RNFTSATQAV TEWYILQATN IFAQVPQQEL VEMSYPGEQM ILACLFGAEP
CNYRNFTSIF YPHYGNCYIF NWGMTEKALP SANPGTEFGL KLILDIGQED YVPFLASTAG
VRLMLHEQRS YPFIRDEGIY AMSGTETSIG VLVDKLQRMG EPYSPCTVNG SEVPVQNFYS
DYNTTYSIQD FDWAHCYSDL QMSVAQRETC IGMCKESCND TQYKMTISMA DWPSEASEDW
IFHVLSQERD QSTNITLSRK GIVKLNIYFQ EFNYRTIEES AANNIVWLLS NLGGQFGFWM
GGSVLCLIEF GEIIIDFVWI TIIKLVALAK SLRQRRAQAS YAGPPPTVAE LVEAHTNFGF
QPDTAPRSPN TGPYPNEQAL PIPGTPPPNY DSLRLQPLDV IESDSEGDAI
