SCNNB_BOVIN
ID SCNNB_BOVIN Reviewed; 641 AA.
AC A5D7U4; F1MZB9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Placenta;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; DAAA02057753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140684; AAI40685.1; -; mRNA.
DR RefSeq; NP_001091544.1; NM_001098075.1.
DR AlphaFoldDB; A5D7U4; -.
DR SMR; A5D7U4; -.
DR STRING; 9913.ENSBTAP00000016301; -.
DR PaxDb; A5D7U4; -.
DR Ensembl; ENSBTAT00000016301; ENSBTAP00000016301; ENSBTAG00000012290.
DR GeneID; 533355; -.
DR KEGG; bta:533355; -.
DR CTD; 6338; -.
DR VEuPathDB; HostDB:ENSBTAG00000012290; -.
DR VGNC; VGNC:34356; SCNN1B.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000160893; -.
DR HOGENOM; CLU_020415_0_0_1; -.
DR InParanoid; A5D7U4; -.
DR OMA; NLTIWNH; -.
DR OrthoDB; 686369at2759; -.
DR TreeFam; TF330663; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000012290; Expressed in thyroid gland and 51 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
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:0050699; F:WW domain binding; IEA:Ensembl.
DR GO; GO:0032341; P:aldosterone metabolic process; IEA:Ensembl.
DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0071468; P:cellular response to acidic pH; IEA:Ensembl.
DR GO; GO:1904045; P:cellular response to aldosterone; IEA:Ensembl.
DR GO; GO:0036254; P:cellular response to amiloride; IEA:Ensembl.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR GO; GO:0042045; P:epithelial fluid transport; IEA:Ensembl.
DR GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0002269; P:leukocyte activation involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IEA:Ensembl.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; IEA:Ensembl.
DR GO; GO:0070944; P:neutrophil-mediated killing of bacterium; IEA:Ensembl.
DR GO; GO:0055075; P:potassium ion homeostasis; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0097274; P:urea homeostasis; IEA:Ensembl.
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; 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..641
FT /note="Amiloride-sensitive sodium channel subunit beta"
FT /id="PRO_0000432888"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 51..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..533
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT TRANSMEM 534..554
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P37089"
FT REGION 597..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU38"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU38"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 641 AA; 72677 MW; 7C3A4A70ED48895B CRC64;
MHVKKYLLKG LHRLQKGPGY TYKELLVWYC DNTNTHGPKR IICEGPKKKA MWFVLTLLFT
SLVCWQWGLF IKTYLNWEVS VSLSIGFKTM DFPAVTICNA SPFQYSKVQH LLKDLDELME
AVLGRILGPE LSQVNDTRAL NLSIWHHTPL VFINEQNPHH PVVLDLFEDN FNGSASNSPA
PGRPCSAHRC KVAMRLCSHN GTTCTFRNFS SATQAVTEWY TLQATNIFAQ VPNQELVAMG
YPAERLILAC LFGAEPCNYR NFTPIFHPDY GNCYIFNWGM TEKALPSANP GTEFGLKLIL
DMGQEDYVPF LTSTAGARLM LHEQRSYPFI KEEGIYAMAG METSIGVLVD KLQRKGEPYS
QCTKNGSDVP IQNLYSNYNT TYSIQACIRS CFQEHMIREC GCGHYLYPLP HKRKYCNNQE
FPDWAHCYSA LRISLAQRET CIYACKESCN DTQYKMTISM AVWPSEASED WIFHVLSQER
DQSSNITLSR KGIVKLNIYF QEFNYRTIEE SAANNIVWLL SNLGGQFGFW MGGSVLCLIE
FGEIIIDFVW ITIIKLVALA KSVRQKRAQA RYEGPPPTVA ELVEAHTNFG FQPDLATPGP
DVEAYPHEQN PPIPGTPPPN YDSLRLQPLD VIESDSEGDA I
