ID   SCN4A_MOUSE             Reviewed;        1841 AA.
AC   Q9ER60; A2VDE9; B1ARK0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Sodium channel protein type 4 subunit alpha;
DE   AltName: Full=Sodium channel protein skeletal muscle subunit alpha;
DE   AltName: Full=Sodium channel protein type IV subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.4;
GN   Name=Scn4a;
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], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RX   PubMed=11834499; DOI=10.1152/ajpheart.00644.2001;
RA   Zimmer T., Bollensdorff C., Haufe V., Birch-Hirschfeld E., Benndorf K.;
RT   "Mouse heart Na+ channels: primary structure and function of two isoforms
RT   and alternatively spliced variants.";
RL   Am. J. Physiol. 282:H1007-H1017(2002).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1841.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH SNTA1; SNTB1 AND SNTB2.
RX   PubMed=9412493; DOI=10.1523/jneurosci.18-01-00128.1998;
RA   Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
RA   Froehner S.C.;
RT   "Interaction of muscle and brain sodium channels with multiple members of
RT   the syntrophin family of dystrophin-associated proteins.";
RL   J. Neurosci. 18:128-137(1998).
RN   [5]
RP   FUNCTION, MUTAGENESIS OF MET-1586, AND TISSUE SPECIFICITY.
RX   PubMed=18317596; DOI=10.1172/jci32638;
RA   Hayward L.J., Kim J.S., Lee M.Y., Zhou H., Kim J.W., Misra K.,
RA   Salajegheh M., Wu F.F., Matsuda C., Reid V., Cros D., Hoffman E.P.,
RA   Renaud J.M., Cannon S.C., Brown R.H. Jr.;
RT   "Targeted mutation of mouse skeletal muscle sodium channel produces
RT   myotonia and potassium-sensitive weakness.";
RL   J. Clin. Invest. 118:1437-1449(2008).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF ARG-663.
RX   PubMed=21881211; DOI=10.1172/jci57398;
RA   Wu F., Mi W., Burns D.K., Fu Y., Gray H.F., Struyk A.F., Cannon S.C.;
RT   "A sodium channel knockin mutant (NaV1.4-R669H) mouse model of hypokalemic
RT   periodic paralysis.";
RL   J. Clin. Invest. 121:4082-4094(2011).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=26427606; DOI=10.1093/hmg/ddv410;
RA   Bergareche A., Bednarz M., Sanchez E., Krebs C.E., Ruiz-Martinez J.,
RA   De La Riva P., Makarov V., Gorostidi A., Jurkat-Rott K., Marti-Masso J.F.,
RA   Paisan-Ruiz C.;
RT   "SCN4A pore mutation pathogenetically contributes to autosomal dominant
RT   essential tremor and may increase susceptibility to epilepsy.";
RL   Hum. Mol. Genet. 24:7111-7120(2015).
CC   -!- FUNCTION: Pore-forming subunit of a voltage-gated sodium channel
CC       complex through which Na(+) ions pass in accordance with their
CC       electrochemical gradient. Alternates between resting, activated and
CC       inactivated states (PubMed:11834499). Required for normal muscle fiber
CC       excitability, normal muscle contraction and relaxation cycles, and
CC       constant muscle strength in the presence of fluctuating K(+) levels
CC       (PubMed:18317596, PubMed:21881211). {ECO:0000269|PubMed:11834499,
CC       ECO:0000269|PubMed:18317596, ECO:0000269|PubMed:21881211}.
CC   -!- ACTIVITY REGULATION: Channel activity is regulated by the ancillary
CC       beta subunit SCN1B. SCN1B strongly enhances the presence of the pore-
CC       forming alpha subunit at the cell surface (By similarity). Interaction
CC       with SCN1B is required for rapid channel inactivation and rapid
CC       recovery after inactivation, and prevents decrease of channel activity
CC       in response to repetitive, high-frequency depolarizations (By
CC       similarity). The channel is inhibited by tetrodotoxin
CC       (PubMed:11834499). {ECO:0000250|UniProtKB:P15390,
CC       ECO:0000250|UniProtKB:P35499, ECO:0000269|PubMed:11834499}.
CC   -!- SUBUNIT: Component of a voltage-sensitive sodium channel complex that
CC       consists of a pore-forming alpha subunit and one or more regulatory
CC       beta subunits. Interacts with SCN1B (By similarity). Heterooligomer
CC       with SCN2B or SCN4B; disulfide-linked (By similarity). Interacts with
CC       the PDZ domain of the syntrophins SNTA1, SNTB1 and SNTB2
CC       (PubMed:9412493). Interacts with TMEM233 (By similarity). Interacts
CC       with the conotoxin GVIIJ (By similarity).
CC       {ECO:0000250|UniProtKB:P04775, ECO:0000250|UniProtKB:P15390,
CC       ECO:0000250|UniProtKB:P35499, ECO:0000269|PubMed:9412493}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834499};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P35499}.
CC   -!- TISSUE SPECIFICITY: Detected in quadriceps muscle (at protein level)
CC       (PubMed:18317596). Detected in hind-limb skeletal muscles, but not in
CC       heart or brain (PubMed:18317596). Detected at low levels in the
CC       myocardium. According to Pubme=26427606 detected also in brain.
CC       {ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:18317596,
CC       ECO:0000269|PubMed:26427606}.
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|UniProtKB:P35499}.
CC   -!- PTM: Phosphorylation at Ser-1322 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and reduces
CC       peak sodium currents. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.4/SCN4A subfamily. {ECO:0000305}.
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DR   EMBL; AJ278787; CAC17146.1; -; mRNA.
DR   EMBL; AL604045; CAM23795.1; -; Genomic_DNA.
DR   EMBL; BC129805; AAI29806.1; -; mRNA.
DR   CCDS; CCDS48961.1; -.
DR   RefSeq; NP_573462.2; NM_133199.2.
DR   AlphaFoldDB; Q9ER60; -.
DR   SMR; Q9ER60; -.
DR   STRING; 10090.ENSMUSP00000021056; -.
DR   BindingDB; Q9ER60; -.
DR   ChEMBL; CHEMBL3616353; -.
DR   GlyCosmos; Q9ER60; 10 sites, No reported glycans.
DR   GlyGen; Q9ER60; 10 sites.
DR   iPTMnet; Q9ER60; -.
DR   PhosphoSitePlus; Q9ER60; -.
DR   MaxQB; Q9ER60; -.
DR   PaxDb; 10090-ENSMUSP00000021056; -.
DR   ProteomicsDB; 253413; -.
DR   DNASU; 110880; -.
DR   GeneID; 110880; -.
DR   KEGG; mmu:110880; -.
DR   AGR; MGI:98250; -.
DR   CTD; 6329; -.
DR   MGI; MGI:98250; Scn4a.
DR   eggNOG; KOG2301; Eukaryota.
DR   InParanoid; Q9ER60; -.
DR   OrthoDB; 1110761at2759; -.
DR   PhylomeDB; Q9ER60; -.
DR   BioGRID-ORCS; 110880; 2 hits in 77 CRISPR screens.
DR   PRO; PR:Q9ER60; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9ER60; Protein.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; ISS:UniProtKB.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR   GO; GO:0015871; P:choline transport; ISO:MGI.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0006812; P:monoatomic cation transport; ISO:MGI.
DR   GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   GO; GO:0100001; P:regulation of skeletal muscle contraction by action potential; ISS:UniProtKB.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR   CDD; cd13433; Na_channel_gate; 1.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR008052; Na_channel_a4su_mammal.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR044564; Na_chnl_inactivation_gate.
DR   InterPro; IPR010526; Na_trans_assoc_dom.
DR   InterPro; IPR043203; VGCC_Ca_Na.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF223; SODIUM CHANNEL PROTEIN TYPE 4 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   PRINTS; PR01665; NACHANNEL4.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Sodium;
KW   Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN           1..1841
FT                   /note="Sodium channel protein type 4 subunit alpha"
FT                   /id="PRO_0000371316"
FT   TOPO_DOM        1..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        132..150
FT                   /note="Helical; Name=S1 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        151..157
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=S2 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        179..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        193..210
FT                   /note="Helical; Name=S3 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        211..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        217..233
FT                   /note="Helical; Name=S4 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        234..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        253..272
FT                   /note="Helical; Name=S5 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        273..385
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        386..410
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        411..417
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        418..438
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        439..572
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        573..591
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        592..602
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        603..622
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        623..636
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        637..656
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        657..658
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        659..676
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        677..692
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        693..711
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        712..740
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        741..761
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        762..772
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        773..791
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        792..1026
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1027..1044
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1045..1057
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1058..1076
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1077..1090
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1091..1109
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1110..1117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1118..1136
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1137..1153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1154..1173
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1174..1224
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1225..1246
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1247..1263
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1264..1285
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1286..1348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1349..1366
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1367..1377
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1378..1396
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1397..1408
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1409..1426
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1427..1439
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1440..1456
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1457..1475
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1476..1493
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1494..1515
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1516..1538
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1539..1568
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1569..1591
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   TOPO_DOM        1592..1841
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REPEAT          113..448
FT                   /note="I"
FT                   /evidence="ECO:0000305"
FT   REPEAT          554..826
FT                   /note="II"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1007..1320
FT                   /note="III"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1329..1627
FT                   /note="IV"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1721..1750
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          32..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          925..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1304..1306
FT                   /note="Important for rapid channel inactivation"
FT                   /evidence="ECO:0000250|UniProtKB:P15390"
FT   REGION          1776..1841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..888
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..983
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1782..1797
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1811..1829
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            401
FT                   /note="Important for inhibition by tetrodotoxin"
FT                   /evidence="ECO:0000250|UniProtKB:P15390"
FT   MOD_RES         1322
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        280..354
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   DISULFID        363..369
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   DISULFID        723
FT                   /note="Interchain; with SCN2B or SCN4B"
FT                   /evidence="ECO:0000250|UniProtKB:P04775"
FT   DISULFID        723
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        725..731
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   DISULFID        763..772
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   DISULFID        1183..1203
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   DISULFID        1547..1562
FT                   /evidence="ECO:0000250|UniProtKB:P35499"
FT   MUTAGEN         663
FT                   /note="R->F: Homozygous mice are born at the expected
FT                   Mendelian rate and have no visible phenotype. Hind-limb
FT                   muscles show decreased excitability and decreased force
FT                   when K(+) levels are low (in vivo). Isolated soleus muscle
FT                   from homozygous mice has an increased susceptibility to
FT                   loss of force generation at 2 mMK(+)."
FT                   /evidence="ECO:0000269|PubMed:21881211"
FT   MUTAGEN         1586
FT                   /note="M->V: A very low percentage of homozygous mice are
FT                   present at 30 days after birth, suggesting high perinatal
FT                   lethality. In anesthesized heterozygous mice,
FT                   electromyographs from hind-limb muscle show high background
FT                   activity, indicative of myotonia. Isolated extensor
FT                   digitorum longus muscle from heterozygous mice displays
FT                   reduced twitch force, with a normal speed of muscle
FT                   contraction, but an increased muscle relaxation half-time.
FT                   Isolated skeletal muscle from heterozygous mice has
FT                   strongly decreased force when the K(+) levels are increased
FT                   to 10 mM. Homozygous mice display prominent hind-limb
FT                   weakness and muscle atrophy."
FT                   /evidence="ECO:0000269|PubMed:18317596"
FT   CONFLICT        131
FT                   /note="A -> T (in Ref. 2; CAM23795)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1056
FT                   /note="R -> Q (in Ref. 2; CAM23795)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1841 AA;  208798 MW;  0766DFD33A9E0E55 CRC64;
     MASSSLPTLV PPGPHCLRPF TPESLAAIEQ RAMEEEARLQ RNKQMEIEEP ERKPRSDLEA
     GKNLPLIYGD PPPEVIGVPL EDLDPYYSDK KTFIVLNKGK AIFRFSATPA LYMLSPFSIV
     RRVAIKVLIH ALFSMFIMIT ILTNCVFMTM SNPPSWSKDV EYTFTGIYTF ESLIKMLARG
     FCIDDFTFLR DPWNWLDFSV ITMAYVTEFV DLGNISALRT FRVLRALKTI TVIPGLKTIV
     GALIQSVKKL SDVMILTVFC LSVFALVGLQ LFMGNLRQKC VRWPPPMNDT NTTWYGNDTW
     YGNDTWYGND TWYGNDTWNS QESWVSNSTF DWEAYINDEG NFYFLEGSND ALLCGNSSDA
     GHCPEGYECM KAGRNPNYGY TSYDTFSWAF LALFRLMTQD YWENLFQLTL RAAGKTYMIF
     FVVIIFLGSF YLINLILAVV AMAYAEQNEA TLAEDQEKEE EFQQMLEKFK KHQEELEKAK
     AAQALEGGEE ADGDPTHSKD CNGSLDTSGE KGPPRPSCSA ESAISDAMEE LEEAHQKCPP
     WWYKCAHKVL IWNCCAPWVK FKHIILLIVM DPFVDLGITI CIVLNTLFMA MEHYPMTEHF
     DNVLSVGNLV FTGIFTAEMV LKLIAMDPYE YFQQGWNIFD SFIVTLSLVE LGLANVQGLS
     VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV VGMQLFGKSY
     KECVCKIASD CSLPRWHMHD FFHSFLIVFR ILCGEWIETM WDCMEVAGQA MCLTVFLMVM
     VIGNLVVLNL FLALLLSSFS ADSLAASDED GEMNNLQIAI GRIKWGIAFA KTFLLGLLHG
     KILSLKDIML SLGEPGGAGE NGESPPEDEK KEPPPEDGNK ELKDNHILNH VGLTDGPRSS
     IEMDHLNFIN NPYLTIHVPI ASEESDLEMP TEEETDTFSE PEDIKKPLQP LYDGNSSVCS
     TADYKPPEED PEEQAEENPE GELPEECFTE ACVKRCPCLY VDISQGRGKM WWTLRRACFK
     IVEHNWFETF IVFMILLSSG ALAFEDIYIE QRRVIRTILE YADKVFTYIF ILEMLLKWVA
     YGFKVYFTNA WCWLDFLIVD VSIISLVANW LGYSELGPIK SLRTLRALRP LRALSRFEGM
     RVVVNALLGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKF YYCINTTTSE RFDISVVNNK
     SECESLMYTG QVRWMNVKVN YDNVGLGYLS LLQVATFKGW MDIMYAAVDS REKEEQPDYE
     VNLYMYLYFV IFIIFGSFFT LNLFIGVIID NFNQQKKKFG GKDIFMTEEQ KKYYNAMKKL
     GSKKPQKPIP RPQNKIQGMV YDFVTKQVFD ISIMILICLN MVTMMVETDD QSQLKVDILY
     NINMVFIIVF TGECVLKMFA LRHYYFTIGW NIFDFVVVIL SIVGLALSDL IQKYFVSPTL
     FRVIRLARIG RVLRLIRGAK GIRTLLFALM MSLPALFNIG LLLFLVMFIY SIFGMSNFAY
     VKKESGIDDM FNFETFGNSI ICLFEITTSA GWDGLLNPIL NSGPPDCDPT LENPGTNIKG
     DCGNPSIGIC FFCSYIIISF LIVVNMYIAI ILENFNVATE ESSEPLCEDD FEMFYETWEK
     FDPDATQFID YSRLSDFVDT LQEPLKIAKP NKIKLITLDL PMVPGDKIHC LDILFALTKE
     VLGDSGEMDA LKQTMEEKFM AANPSKVSYE PITTTLKRKQ EEVCAIKIQR AYRRHLLQRS
     VKQASYMYRH SQEGNGDGAP EKEGLLANTM NKMYGSEKED NGVQSQGEKE KDSTEDAGPT
     TEVTAPSSSD TALTPPPPSP PPPSSPPQGQ TVRPGVKESL V
//