SCN3A_MOUSE
ID SCN3A_MOUSE Reviewed; 1947 AA.
AC A2ASI5; A0A0R5RP23; A0A0R5RP41;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Sodium channel protein type 3 subunit alpha;
DE AltName: Full=Sodium channel protein brain III subunit alpha;
DE AltName: Full=Sodium channel protein type III subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subtype III;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.3;
GN Name=Scn3a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING, AND
RP VARIANT ARG-494.
RC STRAIN=C57BL/6J; TISSUE=Cochlea;
RX PubMed=25937544; DOI=10.1007/s13238-015-0157-1;
RA Zhou Y., Fang F.H., Liu Z.R., Ji Y.H.;
RT "Dissection of voltage-gated sodium channels in developing cochlear sensory
RT epithelia.";
RL Protein Cell 6:458-462(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25172946; DOI=10.1113/jphysiol.2014.274209;
RA Zhang Q., Chibalina M.V., Bengtsson M., Groschner L.N., Ramracheya R.,
RA Rorsman N.J., Leiss V., Nassar M.A., Welling A., Gribble F.M., Reimann F.,
RA Hofmann F., Wood J.N., Ashcroft F.M., Rorsman P.;
RT "Na+ current properties in islet alpha- and beta-cells reflect cell-
RT specific Scn3a and Scn9a expression.";
RL J. Physiol. (Lond.) 592:4677-4696(2014).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=25459751; DOI=10.1016/j.bbagrm.2014.11.004;
RA Li H.J., Wan R.P., Tang L.J., Liu S.J., Zhao Q.H., Gao M.M., Yi Y.H.,
RA Liao W.P., Sun X.F., Long Y.S.;
RT "Alteration of Scn3a expression is mediated via CpG methylation and MBD2 in
RT mouse hippocampus during postnatal development and seizure condition.";
RL Biochim. Biophys. Acta 1849:1-9(2015).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29142310; DOI=10.1038/s41598-017-15834-3;
RA Strege P.R., Knutson K., Eggers S.J., Li J.H., Wang F., Linden D.,
RA Szurszewski J.H., Milescu L., Leiter A.B., Farrugia G., Beyder A.;
RT "1.3 is important for enterochromaffin cell excitability and serotonin
RT release.";
RL Sci. Rep. 7:15650-15650(2017).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, forms a sodium-
CC selective channel through which Na(+) ions may pass in accordance with
CC their electrochemical gradient (PubMed:29142310). May contribute to the
CC regulation of serotonin/5-hydroxytryptamine release by enterochromaffin
CC cells (PubMed:29142310). In pancreatic endocrine cells, required for
CC both glucagon and glucose-induced insulin secretion (PubMed:25172946).
CC {ECO:0000269|PubMed:25172946, ECO:0000269|PubMed:29142310}.
CC -!- SUBUNIT: Heterooligomer of a large alpha subunit and 2-3 smaller beta
CC subunits. Heterooligomer with SCN2B or SCN4B; disulfide-linked.
CC Interacts with NEDD4L. {ECO:0000250|UniProtKB:Q9NY46}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY46};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Basal cell
CC membrane {ECO:0000269|PubMed:29142310}. Note=In enterochromaffin cells,
CC localized highly asymmetrically, almost exclusively at the basal side.
CC {ECO:0000269|PubMed:29142310}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2ASI5-1; Sequence=Displayed;
CC Name=2; Synonyms=CbmNav1.3a;
CC IsoId=A2ASI5-2; Sequence=VSP_059663;
CC Name=3; Synonyms=CbmNav1.3b;
CC IsoId=A2ASI5-3; Sequence=VSP_059662, VSP_059663;
CC -!- TISSUE SPECIFICITY: Expressed in enterochromaffin cells in both colon
CC and small bowel (at protein level) (PubMed:29142310). Expressed in
CC pancreatic alpha and beta cells (PubMed:25172946).
CC {ECO:0000269|PubMed:25172946, ECO:0000269|PubMed:29142310}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the hippocampus at late embryonic
CC stages and during the first week after birth. Down-regulated after
CC postnatal day 7. {ECO:0000269|PubMed:25459751}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000250}.
CC -!- PTM: May be ubiquitinated by NEDD4L; which would promote its
CC endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.
CC -!- PTM: Phosphorylation at Ser-1453 in a highly conserved cytoplasmic loop
CC slows inactivation of the channel and reduces peak sodium currents.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.3/SCN3A subfamily. {ECO:0000305}.
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DR EMBL; KM373689; AIW80041.1; -; mRNA.
DR EMBL; KM373690; AIW80042.1; -; mRNA.
DR EMBL; AL772235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50596.1; -. [A2ASI5-1]
DR RefSeq; NP_061202.3; NM_018732.3. [A2ASI5-1]
DR RefSeq; XP_011237695.1; XM_011239393.1.
DR RefSeq; XP_017172210.1; XM_017316721.1.
DR AlphaFoldDB; A2ASI5; -.
DR SMR; A2ASI5; -.
DR STRING; 10090.ENSMUSP00000097647; -.
DR GlyConnect; 2719; 1 N-Linked glycan (1 site).
DR GlyGen; A2ASI5; 8 sites, 1 N-linked glycan (1 site).
DR iPTMnet; A2ASI5; -.
DR PhosphoSitePlus; A2ASI5; -.
DR SwissPalm; A2ASI5; -.
DR MaxQB; A2ASI5; -.
DR PaxDb; A2ASI5; -.
DR PeptideAtlas; A2ASI5; -.
DR PRIDE; A2ASI5; -.
DR ProteomicsDB; 341494; -. [A2ASI5-1]
DR Antibodypedia; 33767; 135 antibodies from 25 providers.
DR DNASU; 20269; -.
DR Ensembl; ENSMUST00000066432; ENSMUSP00000065023; ENSMUSG00000057182. [A2ASI5-1]
DR Ensembl; ENSMUST00000100069; ENSMUSP00000097647; ENSMUSG00000057182. [A2ASI5-1]
DR GeneID; 20269; -.
DR KEGG; mmu:20269; -.
DR UCSC; uc012bwa.1; mouse. [A2ASI5-1]
DR CTD; 6328; -.
DR MGI; MGI:98249; Scn3a.
DR VEuPathDB; HostDB:ENSMUSG00000057182; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000157130; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; A2ASI5; -.
DR OMA; AFETNIT; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; A2ASI5; -.
DR TreeFam; TF323985; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR BioGRID-ORCS; 20269; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Scn3a; mouse.
DR PRO; PR:A2ASI5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2ASI5; protein.
DR Bgee; ENSMUSG00000057182; Expressed in superior cervical ganglion and 122 other tissues.
DR ExpressionAtlas; A2ASI5; baseline and differential.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0016528; C:sarcoplasm; IDA:MGI.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0005272; F:sodium channel activity; TAS:Reactome.
DR GO; GO:0031402; F:sodium ion binding; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISO:MGI.
DR GO; GO:0071236; P:cellular response to antibiotic; ISO:MGI.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0046684; P:response to pyrethroid; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 2.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..1947
FT /note="Sodium channel protein type 3 subunit alpha"
FT /id="PRO_0000444899"
FT TOPO_DOM 1..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..147
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 148..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 176..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..207
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 208..213
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..230
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 231..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..269
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 270..368
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 369..393
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 394..400
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 422..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 712..730
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 731..741
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 742..761
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 762..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 776..795
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 796..797
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 798..815
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 816..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 832..850
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 851..879
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 880..900
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 901..913
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 914..934
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 935..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1159..1177
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1178..1190
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1191..1209
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1210..1223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1224..1242
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1243..1250
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1251..1269
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1270..1286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1287..1306
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1307..1355
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1356..1377
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1378..1394
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1395..1416
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1417..1479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1480..1497
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1498..1508
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1509..1527
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1528..1539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1540..1557
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1558..1570
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1571..1587
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1588..1606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1607..1624
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1625..1646
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1647..1669
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1670..1699
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1700..1722
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1723..1947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 110..455
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 693..965
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1140..1451
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1460..1758
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1852..1881
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1901..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08104"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08104"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08104"
FT MOD_RES 1453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..346
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 862
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 862
FT /note="Interchain; with the conotoxin GVIIJ (when the
FT channel is not linked to SCN2B or SCN4B; the bond to SCN2B
FT or SCN4B protects the channel from the inhibition by
FT toxin)"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 902..911
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT VAR_SEQ 208
FT /note="D -> S (in isoform 3)"
FT /id="VSP_059662"
FT VAR_SEQ 624
FT /note="N -> NVSQ (in isoform 2 and isoform 3)"
FT /id="VSP_059663"
FT VARIANT 494
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:25937544"
SQ SEQUENCE 1947 AA; 220880 MW; B5E01EEC78004E15 CRC64;
MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDIDDENKPK PNSDLEAGKN
LPFIYGDIPP EMVSEPLEDL DPYYVSKKTF VVLNKGKAIF RFSATSALYI LTPLNPVRKI
AIKILVHSLF SMLIMCTILT NCVFMTLSNP PDWTKNVEYT FTGIYTFESL IKILARGFCL
EDFTFLRDPW NWLDFSVIVM AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCLQW PPSDSAFEIN TTSYFNGTMD
SNGTFVNVTM STFNWKDYIA DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY ICVKAGRNPN
YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY MIFFVLVIFL GSFYLVNLIL
AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE QLKKQQEEAQ AVAAASAASR DFSGIGGLGE
LLESSSEASK LSSKSAKEWR NRRKKRRQRE HLEGNHRPEG DRFPKSESED SVKRRSFLFS
LDGNPLSGDK KLCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
FEDSESRRDS LFVPHRPGER RNSNGTTTET EVRKRRLSSY QISMEMLEDS SGRQRAMSIA
SILTNTMEEL EESRQKCPPC WYRFANVFLI WDCCDSWLKV KHLVNLIVMD PFVDLAITIC
IVLNTLFMAM EHYPMTEQFS SVLTVGNLVF TGIFTAEMVL KIIAMDPYYY FQEGWNIFDG
IIVSLSLMEL GLANVEGLSV LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL
AIIVFIFAVV GMQLFGKSYK ECVCKINEDC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW
DCMEVAGQTM CLIVFMLVMV IGNLVVLNLF LALLLSSFSS DNLAATDDDN EMNNLQIAVG
RMQKGIDYVK NKIRECFRKA FFRKPKVIEI HEGNKIDSCM SNNTGVVEIS KELNYLKDGN
GTTSGVGTGS SVEKYVIDEN DYMSFINNPS LTVTVPIAVG ESDFENLNTE EFSSESELEE
SKEKLNATSS SEGSTVDVAP PREGEQAEIE PEEDLKPEAC FTEGCIKKFP FCQVSTEEGK
GKIWWNLRKT CYSIVEHNWF ETFIVFMILL SSGALAFEDI YIEQRKTIKT MLEYADKVFT
YIFILEMLLK WVAYGFQTYF TNAWCWLDFL IVDVSLVSLV ANALGYSELG AIKSLRTLRA
LRPLRALSRF EGMRVVVNAL VGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCVNMT
TGSMFDMSEV NNFSDCQALG KQARWKNVKV NFDNVGAGYL ALLQVATFKG WMDIMYAAVD
SRDVKLQPVY EENLYMYLYF VIFIIFGSFF TLNLFIGVII DNFNQQKKKF GGQDIFMTEE
QKKYYNAMKK LGSKKPQKPI PRPANKFQGM VFDFVTRQVF DISIMILICL NMVTMMVETD
DQSKYMTLVL SRINLVFIVL FTGEFLLKLI SLRYYYFTIG WNIFDFVVVI LSIVGMFLAE
LIEKYFVSPT LFRVIRLARI GRILRLIKGA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI
YAIFGMSNFA YVKKEAGIDD MFNFETFGNS MICLFQITTS AGWDGLLAPI LNSAPPDCDP
DAIHPGSSVK GDCGNPSVGI FFFVSYIIIS FLVVVNMYIA VILENFSVAT EESAEPLSED
DFEMFYEVWE KFDPDATQFI EFCKLSDFAA ALDPPLLIAK PNKVQLIAMD LPMVSGDRIH
CLDILFAFTK RVLGESGEMD ALRIQMEDRF MASNPSKVSY EPITTTLKRK QEEVSAAIIQ
RNYRCYLLKQ RLKNISNTYD KETIKGRIVL PIKGDMVIDK LNGNSTPEKT DGSSSTTSPP
SYDSVTKPDK EKFEKDKPEK ESKGKEV
