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Sodium channel protein type 1 subunit alpha (Sodium channel protein brain I subunit alpha) (Sodium channel protein type I subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.1)

 SCN1A_MOUSE             Reviewed;        2009 AA.
A2APX8; A2APX6; A2APX7; Q68V28;
05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
20-JUN-2018, entry version 101.
RecName: Full=Sodium channel protein type 1 subunit alpha;
AltName: Full=Sodium channel protein brain I subunit alpha;
AltName: Full=Sodium channel protein type I subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.1;
Name=Scn1a {ECO:0000312|MGI:MGI:98246};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1489-1708.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=15746173; DOI=10.1113/jphysiol.2004.079681;
Haufe V., Camacho J.A., Dumaine R., Guenther B., Bollensdorff C.,
von Banchet G.S., Benndorf K., Zimmer T.;
"Expression pattern of neuronal and skeletal muscle voltage-gated Na+
channels in the developing mouse heart.";
J. Physiol. (Lond.) 564:683-696(2005).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16921370; DOI=10.1038/nn1754;
Yu F.H., Mantegazza M., Westenbroek R.E., Robbins C.A., Kalume F.,
Burton K.A., Spain W.J., McKnight G.S., Scheuer T., Catterall W.A.;
"Reduced sodium current in GABAergic interneurons in a mouse model of
severe myoclonic epilepsy in infancy.";
Nat. Neurosci. 9:1142-1149(2006).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17928448; DOI=10.1523/JNEUROSCI.2162-07.2007;
Kalume F., Yu F.H., Westenbroek R.E., Scheuer T., Catterall W.A.;
"Reduced sodium current in Purkinje neurons from Nav1.1 mutant mice:
implications for ataxia in severe myoclonic epilepsy in infancy.";
J. Neurosci. 27:11065-11074(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
MUTAGENESIS OF ARG-1648.
PubMed=20100831; DOI=10.1074/jbc.M109.078568;
Martin M.S., Dutt K., Papale L.A., Dube C.M., Dutton S.B., de Haan G.,
Shankar A., Tufik S., Meisler M.H., Baram T.Z., Goldin A.L.,
Escayg A.;
"Altered function of the SCN1A voltage-gated sodium channel leads to
gamma-aminobutyric acid-ergic (GABAergic) interneuron abnormalities.";
J. Biol. Chem. 285:9823-9834(2010).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22914087; DOI=10.1038/nature11356;
Han S., Tai C., Westenbroek R.E., Yu F.H., Cheah C.S., Potter G.B.,
Rubenstein J.L., Scheuer T., de la Iglesia H.O., Catterall W.A.;
"Autistic-like behaviour in Scn1a+/- mice and rescue by enhanced GABA-
mediated neurotransmission.";
Nature 489:385-390(2012).
[8]
DISRUPTION PHENOTYPE.
PubMed=22908258; DOI=10.1073/pnas.1211591109;
Cheah C.S., Yu F.H., Westenbroek R.E., Kalume F.K., Oakley J.C.,
Potter G.B., Rubenstein J.L., Catterall W.A.;
"Specific deletion of NaV1.1 sodium channels in inhibitory
interneurons causes seizures and premature death in a mouse model of
Dravet syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 109:14646-14651(2012).
[9]
MUTAGENESIS OF ARG-1648.
PubMed=26694226; DOI=10.1111/gbb.12281;
Sawyer N.T., Helvig A.W., Makinson C.D., Decker M.J., Neigh G.N.,
Escayg A.;
"Scn1a dysfunction alters behavior but not the effect of stress on
seizure response.";
Genes Brain Behav. 15:335-347(2016).
[10]
FUNCTION, ENZYME REGULATION, DOMAIN, AND TISSUE SPECIFICITY.
PubMed=27281198; DOI=10.1038/nature17976;
Osteen J.D., Herzig V., Gilchrist J., Emrick J.J., Zhang C., Wang X.,
Castro J., Garcia-Caraballo S., Grundy L., Rychkov G.Y., Weyer A.D.,
Dekan Z., Undheim E.A., Alewood P., Stucky C.L., Brierley S.M.,
Basbaum A.I., Bosmans F., King G.F., Julius D.;
"Selective spider toxins reveal a role for the Nav1.1 channel in
mechanical pain.";
Nature 534:494-499(2016).
-!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
of excitable membranes (PubMed:16921370, PubMed:17928448,
PubMed:27281198). Assuming opened or closed conformations in
response to the voltage difference across the membrane, the
protein forms a sodium-selective channel through which Na(+) ions
may pass in accordance with their electrochemical gradient. Plays
a key role in brain, probably by regulating the moment when
neurotransmitters are released in neurons (PubMed:16921370,
PubMed:22914087). Involved in sensory perception of mechanical
pain: activation in somatosensory neurons induces pain without
neurogenic inflammation and produces hypersensitivity to
mechanical, but not thermal stimuli (PubMed:27281198).
{ECO:0000269|PubMed:16921370, ECO:0000269|PubMed:17928448,
ECO:0000269|PubMed:22914087, ECO:0000269|PubMed:27281198}.
-!- ENZYME REGULATION: Inactivation of this channel is specifically
inhibited by the spider toxins Hm1a and Hm1b (H.maculata, AC
P60992 and AC P0DOC5) in somatosensory neurons to elicit acute
pain and mechanical allodynia (PubMed:27281198).
{ECO:0000269|PubMed:16921370, ECO:0000269|PubMed:27281198}.
-!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
conducting pore forming alpha-subunit regulated by one or more
beta-1 (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4
(SCN4B). Beta-1 (SCN1B) and beta-3 (SCN3B) are non-covalently
associated with alpha, while beta-2 (SCN2B) and beta-4 (SCN4B) are
covalently linked by disulfide bonds. Interacts with FGF13.
Interacts with the conotoxin GVIIJ. {ECO:0000250|UniProtKB:P04774,
ECO:0000250|UniProtKB:P35498}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P35498}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:D0E0C2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=A2APX8-1; Sequence=Displayed;
Name=2;
IsoId=A2APX8-2; Sequence=VSP_058553;
Name=3;
IsoId=A2APX8-3; Sequence=VSP_058552;
-!- TISSUE SPECIFICITY: Present in cerebellar Purkinje neurons (at
protein level) (PubMed:17928448). Expressed by myelinated, non-C-
fiber neurons in sensory ganglia (PubMed:27281198).
{ECO:0000269|PubMed:17928448, ECO:0000269|PubMed:27281198}.
-!- DOMAIN: The S3b-S4 and S1-S2 loops of repeat IV are targeted by
H.maculata toxins Hm1a and Hm1b, leading to inhibit fast
inactivation of Nav1.1/SCN1A. Selectivity for H.maculata toxins
Hm1a and Hm1b depends on S1-S2 loops of repeat IV
(PubMed:27281198). {ECO:0000269|PubMed:27281198}.
-!- DOMAIN: The sequence contains 4 internal repeats, each with 5
hydrophobic segments (S1, S2, S3, S5, S6) and one positively
charged segment (S4). Segments S4 are probably the voltage-sensors
and are characterized by a series of positively charged amino
acids at every third position. {ECO:0000305}.
-!- PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000250|UniProtKB:P04775}.
-!- DISRUPTION PHENOTYPE: Homozygous mice display severe seizures and
premature death on postnatal day 15 (PubMed:16921370). Mice show
severe motor deficits, including irregularity of stride length
during locomotion, impaired motor reflexes in grasping and mild
tremor in limbs when immobile, consistent with cerebellar
dysfunction (PubMed:16921370). Heterozygous mice exhibit autistic-
like behavior, characterized by hyperactivity, stereotyped
behaviors, social interaction deficits and impaired context-
dependent spatial memory (PubMed:22914087). Defects are caused by
caused by impaired GABAergic neurotransmission (PubMed:22914087).
Conditional knockout in forebrain GABAergic neurons leads to
premature death caused by generalized tonic-clonic seizures in
heterozygous mice (PubMed:22908258). {ECO:0000269|PubMed:16921370,
ECO:0000269|PubMed:22908258, ECO:0000269|PubMed:22914087}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.1/SCN1A subfamily. {ECO:0000305}.
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EMBL; AL844526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL928726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ810515; CAH17959.1; -; mRNA.
CCDS; CCDS38131.1; -. [A2APX8-2]
CCDS; CCDS84530.1; -. [A2APX8-1]
RefSeq; NP_001300926.1; NM_001313997.1. [A2APX8-1]
RefSeq; NP_061203.2; NM_018733.2.
RefSeq; XP_006499090.1; XM_006499027.3.
RefSeq; XP_006499091.1; XM_006499028.3.
UniGene; Mm.439704; -.
UniGene; Mm.455166; -.
ProteinModelPortal; A2APX8; -.
SMR; A2APX8; -.
STRING; 10090.ENSMUSP00000076697; -.
ChEMBL; CHEMBL3616352; -.
iPTMnet; A2APX8; -.
PhosphoSitePlus; A2APX8; -.
SwissPalm; A2APX8; -.
MaxQB; A2APX8; -.
PRIDE; A2APX8; -.
Ensembl; ENSMUST00000077489; ENSMUSP00000076697; ENSMUSG00000064329. [A2APX8-2]
Ensembl; ENSMUST00000094951; ENSMUSP00000092558; ENSMUSG00000064329. [A2APX8-3]
Ensembl; ENSMUST00000112366; ENSMUSP00000107985; ENSMUSG00000064329. [A2APX8-1]
Ensembl; ENSMUST00000112371; ENSMUSP00000107990; ENSMUSG00000064329. [A2APX8-2]
GeneID; 20265; -.
KEGG; mmu:20265; -.
UCSC; uc033hnf.1; mouse.
CTD; 6323; -.
MGI; MGI:98246; Scn1a.
eggNOG; ENOG410INF8; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00830000128242; -.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG053100; -.
InParanoid; A2APX8; -.
KO; K04833; -.
OMA; CMSNHTT; -.
OrthoDB; EOG091G00FK; -.
PhylomeDB; A2APX8; -.
TreeFam; TF323985; -.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
ChiTaRS; Scn1a; mouse.
PRO; PR:A2APX8; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000064329; -.
ExpressionAtlas; A2APX8; baseline and differential.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0043194; C:axon initial segment; IDA:MGI.
GO; GO:0014704; C:intercalated disc; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0033268; C:node of Ranvier; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0034706; C:sodium channel complex; IPI:MGI.
GO; GO:0030315; C:T-tubule; IDA:MGI.
GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0031402; F:sodium ion binding; ISO:MGI.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:UniProtKB.
GO; GO:0001508; P:action potential; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IDA:UniProtKB.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
GO; GO:0019228; P:neuronal action potential; IMP:MGI.
GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR008051; Na_channel_a1su.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR024583; Na_trans_cytopl.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
PRINTS; PR01664; NACHANNEL1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Reference proteome; Repeat; Sodium; Sodium channel;
Sodium transport; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 2009 Sodium channel protein type 1 subunit
alpha.
/FTId=PRO_0000437536.
TOPO_DOM 1 128 Cytoplasmic. {ECO:0000305}.
TRANSMEM 129 147 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 148 154 Extracellular. {ECO:0000305}.
TRANSMEM 155 175 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 176 189 Cytoplasmic. {ECO:0000305}.
TRANSMEM 190 207 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 208 213 Extracellular. {ECO:0000305}.
TRANSMEM 214 230 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 231 249 Cytoplasmic. {ECO:0000305}.
TRANSMEM 250 269 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 270 367 Extracellular. {ECO:0000305}.
INTRAMEM 368 392 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 393 399 Extracellular. {ECO:0000305}.
TRANSMEM 400 420 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 421 768 Cytoplasmic. {ECO:0000305}.
TRANSMEM 769 787 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 788 798 Extracellular. {ECO:0000305}.
TRANSMEM 799 818 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 819 832 Cytoplasmic. {ECO:0000305}.
TRANSMEM 833 852 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 853 854 Extracellular. {ECO:0000305}.
TRANSMEM 855 872 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 873 888 Cytoplasmic. {ECO:0000305}.
TRANSMEM 889 907 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 908 936 Extracellular. {ECO:0000305}.
INTRAMEM 937 957 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 958 970 Extracellular. {ECO:0000305}.
TRANSMEM 971 991 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 992 1219 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1220 1237 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1238 1250 Extracellular. {ECO:0000305}.
TRANSMEM 1251 1269 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1270 1283 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1284 1302 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1303 1310 Extracellular. {ECO:0000305}.
TRANSMEM 1311 1329 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1330 1346 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1347 1366 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1367 1418 Extracellular. {ECO:0000305}.
INTRAMEM 1419 1440 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1441 1457 Extracellular. {ECO:0000305}.
TRANSMEM 1458 1479 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1480 1542 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1543 1560 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1561 1571 Extracellular. {ECO:0000305}.
TRANSMEM 1572 1590 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1591 1602 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1603 1620 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1621 1633 Extracellular. {ECO:0000305}.
TRANSMEM 1634 1650 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1651 1669 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1670 1687 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1688 1709 Extracellular. {ECO:0000305}.
INTRAMEM 1710 1732 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1733 1762 Extracellular. {ECO:0000305}.
TRANSMEM 1763 1785 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1786 2009 Cytoplasmic. {ECO:0000305}.
REPEAT 110 454 I. {ECO:0000250|UniProtKB:P04774}.
REPEAT 750 1022 II. {ECO:0000250|UniProtKB:P04774}.
REPEAT 1200 1514 III. {ECO:0000250|UniProtKB:P04774}.
REPEAT 1523 1821 IV. {ECO:0000250|UniProtKB:P04774}.
DOMAIN 1915 1944 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
REGION 1561 1571 S1-S2 loop of repeat IV.
{ECO:0000269|PubMed:27281198}.
REGION 1619 1636 S3b-S4 loop of repeat IV.
{ECO:0000269|PubMed:27281198}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000250|UniProtKB:P04774}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000250|UniProtKB:P04774}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000250|UniProtKB:P04774}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000250|UniProtKB:P04774}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000250|UniProtKB:P04774}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000250|UniProtKB:P04774}.
MOD_RES 1516 1516 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P04775}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 277 345 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 919 919 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 919 919 Interchain; with the conotoxin GVIIJ
(when the channel is not linked to SCN2B
or SCN4B; the bond to SCN2B or SCN4B
protects the channel from the inhibition
by toxin).
{ECO:0000250|UniProtKB:P04775}.
DISULFID 959 968 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 654 681 Missing (in isoform 3).
/FTId=VSP_058552.
VAR_SEQ 671 681 Missing (in isoform 2).
/FTId=VSP_058553.
MUTAGEN 1648 1648 R->H: Homozygous mice display spontaneous
generalized seizures and premature death
between P16 and P26. Heterozygous mice
show infrequent spontaneous seizures,
increased susceptibility to chemically
and hyperthermia-induced generalized
seizures and sleep abnormalities.
Heterozygous mice also show deficits in
social behavior, spatial memory, cued
fear conditioning, pre-pulse inhibition
and risk assessment.
{ECO:0000269|PubMed:20100831,
ECO:0000269|PubMed:26694226}.
SEQUENCE 2009 AA; 228800 MW; A373BA0B710C501E CRC64;
MEQTVLVPPG PDSFNFFTRE SLAAIERRIA EEKAKNPKPD KKDDDENGPK PNSDLEAGKN
LPFIYGDIPP EMVSEPLEDL DPYYINKKTF IVLNKGKAIF RFSATSALYI LTPFNPLRKI
AIKILVHSLF SMLIMCTILT NCVFMTMSNP PDWTKNVEYT FTGIYTFESL IKIIARGFCL
EDFTFLRDPW NWLDFTVITF AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCVQW PPTNASLEEH SIEKNITMDY
NGTLVNETVF EFDWKSYIQD SRYHYFLEGV LDALLCGNSS DAGQCPEGYM CVKAGRNPNY
GYTSFDTFSW AFLSLFRLMT QDFWENLYQL TLRAAGKTYM IFFVLVIFLG SFYLINLILA
VVAMAYEEQN QATLEEAEQK EAEFQQMLEQ LKKQQEAAQQ AAATTASEHS REPSAAGRLS
DSSSEASKLS SKSAKERRNR RKKRKQKEQS GGEEKDDDEF HKSESEDSIR RKGFRFSIEG
NRLTYEKRYS SPHQSLLSIR GSLFSPRRNS RTSLFSFRGR AKDVGSENDF ADDEHSTFED
NESRRDSLFV PRRHGERRNS NLSQTSRSSR MLAVFPANGK MHSTVDCNGV VSLVGGPSVP
TSPVGQLLPE VIIDKPATDD NGTTTETEMR KRRSSSFHVS MDFLEDPSQR QRAMSIASIL
TNTVEELEES RQKCPPCWYK FSNIFLIWDC SPYWLKVKHI VNLVVMDPFV DLAITICIVL
NTLFMAMEHY PMTEHFNHVL TVGNLVFTGI FTAEMFLKII AMDPYYYFQE GWNIFDGFIV
TLSLVELGLA NVEGLSVLRS FRLLRVFKLA KSWPTLNMLI KIIGNSVGAL GNLTLVLAII
VFIFAVVGMQ LFGKSYKDCV CKIATDCKLP RWHMNDFFHS FLIVFRVLCG EWIETMWDCM
EVAGQAMCLT VFMMVMVIGN LVVLNLFLAL LLSSFSADNL AATDDDNEMN NLQIAVDRMH
KGIAYVKRKI YEFIQQSFVK KQKILDEIKP LDDLNNRKDN CISNHTTEIG KDLDCLKDVN
GTTSGIGTGS SVEKYIIDES DYMSFINNPS LTVTVPIAVG ESDFENLNTE DFSSESDLEE
SKEKLNESSS SSEGSTVDIG APAEEQPVIE PEETLEPEAC FTEGCVQRFK CCQISVEEGR
GKQWWNLRRT CFRIVEHNWF ETFIVFMILL SSGALAFEDI YIDQRKTIKT MLEYADKVFT
YIFILEMLLK WVAYGYQTYF TNAWCWLDFL IVDVSLVSLT ANALGYSELG AIKSLRTLRA
LRPLRALSRF EGMRVVVNAL LGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCVNTT
TGDIFEISEV NNHSDCLKLI ERNETARWKN VKVNFDNVGF GYLSLLQVAT FKGWMDIMYA
AVDSRNVELQ PKYEESLYMY LYFVIFIIFG SFFTLNLFIG VIIDNFNQQK KKFGGQDIFM
TEEQKKYYNA MKKLGSKKPQ KPIPRPGNKF QGMVFDFVTR QVFDISIMIL ICLNMVTMMV
ETDDQSDYVT SILSRINLVF IVLFTGECVL KLISLRHYYF TIGWNIFDFV VVILSIVGMF
LAELIEKYFV SPTLFRVIRL ARIGRILRLI KGAKGIRTLL FALMMSLPAL FNIGLLLFLV
MFIYAIFGMS NFAYVKREVG IDDMFNFETF GNSMICLFQI TTSAGWDGLL APILNSKPPD
CDPNKVNPGS SVKGDCGNPS VGIFFFVSYI IISFLVVVNM YIAVILENFS VATEESAEPL
SEDDFEMFYE VWEKFDPDAT QFMEFEKLSQ FAAALEPPLN LPQPNKLQLI AMDLPMVSGD
RIHCLDILFA FTKRVLGESG EMDALRIQME ERFMASNPSK VSYQPITTTL KRKQEEVSAV
IIQRAYRRHL LKRTVKQASF TYNKNKLKGG ANLLVKEDML IDRINENSIT EKTDLTMSTA
ACPPSYDRVT KPIVEKHEQE GKDEKAKGK


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