SCNNB_CANLF
ID SCNNB_CANLF Reviewed; 641 AA.
AC Q95165; F1PGD1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 129.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 531-618.
RX PubMed=9720188;
RA Zhou T., Nonneman D., Shibuya H., Khan S., Liu P.C., Johnson G.S.;
RT "An AvaII PCR/RFLP in an exon of the canine gene for the beta subunit of
RT the amiloride-sensitive sodium channel (SCNN1B).";
RL Anim. Genet. 29:239-239(1998).
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; AAEX03004450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U68062; AAB09034.1; -; Genomic_DNA.
DR RefSeq; NP_001300793.1; NM_001313864.1.
DR RefSeq; XP_005621477.1; XM_005621420.2.
DR AlphaFoldDB; Q95165; -.
DR SMR; Q95165; -.
DR STRING; 9612.ENSCAFP00000026101; -.
DR PaxDb; Q95165; -.
DR GeneID; 489972; -.
DR KEGG; cfa:489972; -.
DR CTD; 6338; -.
DR eggNOG; KOG4294; Eukaryota.
DR HOGENOM; CLU_020415_0_0_1; -.
DR OMA; NLTIWNH; -.
DR OrthoDB; 686369at2759; -.
DR TreeFam; TF330663; -.
DR Reactome; R-CFA-2672351; Stimuli-sensing channels.
DR Reactome; R-CFA-9730628; Sensory perception of salty taste.
DR Proteomes; UP000002254; Chromosome 6.
DR Bgee; ENSCAFG00000017687; Expressed in metanephros cortex and 38 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: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; IBA:GO_Central.
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 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..641
FT /note="Amiloride-sensitive sodium channel subunit beta"
FT /id="PRO_0000181267"
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 593..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 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 567
FT /note="R -> Q (in Ref. 2; AAB09034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 72654 MW; 5A040E85895D751E CRC64;
MHLKKYLLKG LHRLQKGPGY SYKELLVWYC NNTNTHGPKR IICEGPKKKA MWFLITLLFT
SLVCWQWGVF IRTYLSWEVS VSLSLGFKTM DFPAVTICNA SPFQYSKVKH LLRDLDELME
AVLERILAPE HSDANATRTL NVTMWNYTPL VLIDEQNPHC PVVLDLFGDI HNGSASSSPA
PARSCTVHGC KVAMRLCSLN GTVCTFRNFT SATQAVTEWY LLQATNIFSQ VPQRELVEMS
YPAERLILAC LFGAEPCSYR NFTSIFHPDY GNCYIFNWGM TEKALPSANP GAEFGLKLIL
DIGQEDYVPF LTSTAGARLM LHEQRSYPFI KDEGIYAMSG TETSIGVLVD RLERKGEPYS
QCTVNGSDVP VRNLYSDYNT TYSIQACIRS CFQDHMIQNC SCAHYLYPLP RGERYCNNRE
FPDWAYCYSH LRMSVAQRET CINMCKESCN DTQYKMTISM ADWPSEASED WIFHVLSQER
DQSTNITLSR KGVVKLNIYF QEFNYRTIEE SAANNIVWLL SNLGGQFGFW MGGSVLCLIE
FGEILIDFVW ITIIKLVAFA KSLRQKRAQA RYAGPPPTVA ELVEAHTNFG FQPDVARPGP
DPGTYPDEQT LPIPGTPPPN YDSLRLQPLD VIESDSEGDA I
