SCN2A_MOUSE
ID SCN2A_MOUSE Reviewed; 2006 AA.
AC B1AWN6; A0A0J9YTW6;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Sodium channel protein type 2 subunit alpha {ECO:0000305};
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.2;
GN Name=Scn2a {ECO:0000312|MGI:MGI:98248};
GN Synonyms=Scn2a1 {ECO:0000312|MGI:MGI:98248};
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 [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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10827969; DOI=10.1016/s0006-3495(00)76829-9;
RA Planells-Cases R., Caprini M., Zhang J., Rockenstein E.M., Rivera R.R.,
RA Murre C., Masliah E., Montal M.;
RT "Neuronal death and perinatal lethality in voltage-gated sodium channel
RT alpha(II)-deficient mice.";
RL Biophys. J. 78:2878-2891(2000).
RN [4]
RP FUNCTION, MUTAGENESIS OF 880-VAL--ALA-882, AND TISSUE SPECIFICITY.
RX PubMed=11166117; DOI=10.1016/s0306-4522(00)00479-6;
RA Kearney J.A., Plummer N.W., Smith M.R., Kapur J., Cummins T.R.,
RA Waxman S.G., Goldin A.L., Meisler M.H.;
RT "A gain-of-function mutation in the sodium channel gene Scn2a results in
RT seizures and behavioral abnormalities.";
RL Neuroscience 102:307-317(2001).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 880-VAL--ALA-882.
RX PubMed=28137877; DOI=10.1073/pnas.1615774114;
RA Thompson C.H., Hawkins N.A., Kearney J.A., George A.L. Jr.;
RT "CaMKII modulates sodium current in neurons from epileptic Scn2a mutant
RT mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:1696-1701(2017).
RN [6]
RP FUNCTION.
RX PubMed=29867081; DOI=10.1038/s41593-018-0163-8;
RA Middleton S.J., Kneller E.M., Chen S., Ogiwara I., Montal M., Yamakawa K.,
RA McHugh T.J.;
RT "Altered hippocampal replay is associated with memory impairment in mice
RT heterozygous for the Scn2a gene.";
RL Nat. Neurosci. 21:996-1003(2018).
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, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient (PubMed:10827969,
CC PubMed:11166117, PubMed:28137877). Implicated in the regulation of
CC hippocampal replay occurring within sharp wave ripples (SPW-R)
CC important for memory (PubMed:29867081). {ECO:0000269|PubMed:10827969,
CC ECO:0000269|PubMed:11166117, ECO:0000269|PubMed:28137877,
CC ECO:0000269|PubMed:29867081}.
CC -!- SUBUNIT: Heterooligomer of a large alpha subunit and a smaller beta
CC subunit. Heterooligomer with SCN2B or SCN4B; disulfide-linked.
CC Interacts with NEDD4L. Interacts with CALM.
CC {ECO:0000250|UniProtKB:P04775}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10827969};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:10827969, PubMed:11166117). Detected in hippocampus, cortex and
CC brain stem (PubMed:10827969). {ECO:0000269|PubMed:10827969,
CC ECO:0000269|PubMed:11166117}.
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:P04775}.
CC -!- PTM: Sumoylated at Lys-38. Sumoylation is induced by hypoxia, increases
CC voltage-gated sodium current and mediates the early response to acute
CC hypoxia in neurons. Sumoylated SCN2A is located at the cell membrane.
CC {ECO:0000250|UniProtKB:P04775}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout mice deficient in brain are
CC morphologically and organogenically indistinguishable from their
CC heterozygous littermates. They die perinatally with severe hypoxia and
CC massive neuronal apoptosis, notably in the brainstem. Sodium channel
CC currents recorded from cultured neurons of knockout mice are sharply
CC attenuated. {ECO:0000269|PubMed:10827969}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.2/SCN2A subfamily. {ECO:0000305}.
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DR EMBL; AL772235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX284648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38130.1; -.
DR RefSeq; NP_001092768.1; NM_001099298.3.
DR AlphaFoldDB; B1AWN6; -.
DR SMR; B1AWN6; -.
DR IntAct; B1AWN6; 2.
DR MINT; B1AWN6; -.
DR STRING; 10090.ENSMUSP00000028377; -.
DR GlyGen; B1AWN6; 6 sites.
DR iPTMnet; B1AWN6; -.
DR PhosphoSitePlus; B1AWN6; -.
DR SwissPalm; B1AWN6; -.
DR MaxQB; B1AWN6; -.
DR PaxDb; B1AWN6; -.
DR PeptideAtlas; B1AWN6; -.
DR PRIDE; B1AWN6; -.
DR ProteomicsDB; 312320; -.
DR ProteomicsDB; 342772; -.
DR ABCD; B1AWN6; 1 sequenced antibody.
DR Antibodypedia; 33769; 175 antibodies from 24 providers.
DR Ensembl; ENSMUST00000028377; ENSMUSP00000028377; ENSMUSG00000075318.
DR Ensembl; ENSMUST00000100067; ENSMUSP00000097645; ENSMUSG00000075318.
DR GeneID; 110876; -.
DR KEGG; mmu:110876; -.
DR UCSC; uc008jwo.2; mouse.
DR CTD; 6326; -.
DR MGI; MGI:98248; Scn2a.
DR VEuPathDB; HostDB:ENSMUSG00000075318; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000154224; -.
DR InParanoid; B1AWN6; -.
DR OMA; CCENWLT; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; B1AWN6; -.
DR TreeFam; TF323985; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR BioGRID-ORCS; 110876; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Scn2a; mouse.
DR PRO; PR:B1AWN6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000075318; Expressed in piriform cortex and 135 other tissues.
DR ExpressionAtlas; B1AWN6; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043194; C:axon initial segment; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0033268; C:node of Ranvier; ISO:MGI.
DR GO; GO:0033270; C:paranode region of axon; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034706; C:sodium channel complex; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:MGI.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
DR GO; GO:0043522; F:leucine zipper domain 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:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0008627; P:intrinsic apoptotic signaling pathway in response to osmotic stress; IMP:MGI.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
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:0035725; P:sodium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR SMART; SM00015; IQ; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW Voltage-gated channel.
FT CHAIN 1..2006
FT /note="Sodium channel protein type 2 subunit alpha"
FT /id="PRO_0000446659"
FT TRANSMEM 130..148
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 156..176
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 191..208
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 215..231
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 251..270
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT INTRAMEM 370..394
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 402..422
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 761..779
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 791..810
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 825..844
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 847..864
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 881..899
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT INTRAMEM 929..949
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 963..983
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1211..1228
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1242..1260
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1275..1293
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1302..1320
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1338..1357
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT INTRAMEM 1410..1431
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1449..1470
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1534..1551
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1563..1581
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1594..1611
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1625..1641
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1661..1678
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT INTRAMEM 1701..1723
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TRANSMEM 1754..1776
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT REPEAT 111..456
FT /note="I"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT REPEAT 742..1014
FT /note="II"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT REPEAT 1191..1505
FT /note="III"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT REPEAT 1514..1812
FT /note="IV"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DOMAIN 1906..1935
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 28..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..919
FT /note="Binds SCN2B"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT REGION 1121..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..2006
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 510..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1934..1960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 330
FT /note="Binds Mu-conotoxin KIIIA"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 362
FT /note="Binds Mu-conotoxin KIIIA"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 910
FT /note="Binds SCN2B; via carbonyl oxygen"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 917
FT /note="Binds Mu-conotoxin KIIIA; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 921
FT /note="Binds Mu-conotoxin KIIIA; via carbonyl oxygen"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 946
FT /note="Binds Mu-conotoxin KIIIA"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 950
FT /note="Binds Mu-conotoxin KIIIA"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 1375
FT /note="Binds Mu-conotoxin KIIIA; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 1430
FT /note="Binds Mu-conotoxin KIIIA"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 1444
FT /note="Binds Mu-conotoxin KIIIA"
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT SITE 1490
FT /note="Important for channel closure"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 1507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 1931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 1944
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 1964
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 1967
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT MOD_RES 1972
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT CARBOHYD 285
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 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 278..338
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT DISULFID 911
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 911
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 913..919
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT DISULFID 951..960
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 1367..1387
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT DISULFID 1732..1747
FT /evidence="ECO:0000250|UniProtKB:Q99250"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT VARIANT 209
FT /note="N -> D"
FT MUTAGEN 880..882
FT /note="GAL->QQQ: Gain of function mutation. Mutant mice
FT display enhanced persistent sodium current, have seizures
FT and behavioral abnormalities. Half of the mice die before
FT four months of age, and only 10% survive to nine months.
FT Epilepsy severity in this model is strain-dependent.
FT Mutation in a C57BL/6J background exhibit a mild disorder,
FT whereas animals intercrossed with SJL7/j mice show a severe
FT phenotype."
FT /evidence="ECO:0000269|PubMed:11166117,
FT ECO:0000269|PubMed:28137877"
SQ SEQUENCE 2006 AA; 227945 MW; 8A607C83C4E97F0D CRC64;
MAQSVLVPPG PDSFRFFTRE SLAAIEQRIA EEKAKRPKQE RKDEDDENGP KPNSDLEAGK
SLPFIYGDIP PEMVSEPLED LDPYYINKKT FIVLNKGKAI SRFSATSALY ILTPFNPIRK
LAIKILVHSL FNVLIMCTIL TNCVFMTMSN PPDWTKNVEY TFTGIYTFES LIKILARGFC
LEDFTFLRDP WNWLDFTVIT FAYVTEFVNL GNVSALRTFR VLRALKTISV IPGLKTIVGA
LIQSVKKLSD VMILTVFCLS VFALIGLQLF MGNLRNKCLQ WPPDNSTFEI NITSFFNNSL
DWNGTAFNRT MNMFNWDEYI EDKSHFYFLE GQNDALLCGN SSDAGQCPEG YICVKAGRNP
NYGYTSFDTF SWAFLSLFRL MTQDFWENLY QLTLRAAGKT YMIFFVLVIF LGSFYLINLI
LAVVAMAYEE QNQATLEEAE QKEAEFQQML EQLKKQQEEA QAAAAAASAE SRDFSGAGGI
GVFSESSSVA SKLSSKSEKE LKNRRKKKKQ KEQAGEEEKE DAVRKSASED SIRKKGFRFS
LEGSRLTYEK RFSSPHQSLL SIRGSLFSPR RNSRASLFSF KGRVKDIGSE NDFADDEHST
FEDNDSRRDS LFVPHRHGER RPSNVSQASR ASRGIPTLPM NGKMHSAVDC NGVVSLVGGP
SALTSPVGQL LPEGTTTETE IRKRRSSSYH VSMDLLEDPT SRQRAMSMAS ILTNTMEELE
ESRQKCPPCW YKFANMCLIW DCCKPWLKVK HVVNLVVMDP FVDLAITICI VLNTLFMAME
HYPMTEQFSS VLSVGNLVFT GIFTAEMFLK IIAMDPYYYF QEGWNIFDGF IVSLSLMELG
LANVEGLSVL RSFRLLRVFK LAKSWPTLNM LIKIIGNSVG ALGNLTLVLA IIVFIFAVVG
MQLFGKSYKE CVCKISNDCE LPRWHMHDFF HSFLIVFRVL CGEWIETMWD CMEVAGQTMC
LTVFMMVMVI GNLVVLNLFL ALLLSSFSSD NLAATDDDNE MNNLQIAVGR MQKGIDFVKR
KIREFIQKAF VRKQKALDEI KPLEDLNNKK DSCISNHTTI EIGKDLNYLK DGNGTTSGIG
SSVEKYVVDE SDYMSFINNP SLTVTVPIAV GESDFENLNT EEFSSESDME ESKEKLNATS
SSEGSTVDIG APAEGEQPEA EPEESLEPEA CFTEDCVRKF KCCQISIEEG KGKLWWNLRK
TCYKIVEHNW FETFIVFMIL LSSGALAFED IYIEQRKTIK TMLEYADKVF TYIFILEMLL
KWVAYGFQMY FTNAWCWLDF LIVDVSLVSL TANALGYSEL GAIKSLRTLR ALRPLRALSR
FEGMRVVVNA LLGAIPSIMN VLLVCLIFWL IFSIMGVNLF AGKFYHCINY TTGEMFDVSV
VNNYSECQAL IESNQTARWK NVKVNFDNVG LGYLSLLQVA TFKGWMDIMY AAVDSRNVEL
QPKYEDNLYM YLYFVIFIIF GSFFTLNLFI GVIIDNFNQQ KKKFGGQDIF MTEEQKKYYN
AMKKLGSKKP QKPIPRPANK FQGMVFDFVT KQVFDISIMI LICLNMVTMM VETDDQSQEM
TNILYWINLV FIVLFTGECV LKLISLRHYY FTIGWNIFDF VVVILSIVGM FLAELIEKYF
VSPTLFRVIR LARIGRILRL IKGAKGIRTL LFALMMSLPA LFNIGLLLFL VMFIYAIFGM
SNFAYVKREV GIDDMFNFET FGNSMICLFQ ITTSAGWDGL LAPILNSGPP DCDPEKDHPG
SSVKGDCGNP SVGIFFFVSY IIISFLVVVN MYIAVILENF SVATEESAEP LSEDDFEMFY
EVWEKFDPDA TQFIEFCKLS DFAAALDPPL LIAKPNKVQL IAMDLPMVSG DRIHCLDILF
AFTKRVLGES GEMDALRIQM EERFMASNPS KVSYEPITTT LKRKQEEVSA IVIQRAYRRY
LLKQKVKKVS SIYKKDKGKE DEGTPIKEDI ITDKLNENST PEKTDVTPST TSPPSYDSVT
KPEKEKFEKD KSEKEDKGKD IRESKK
