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Sodium channel protein type 8 subunit alpha (Sodium channel protein type VIII subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.6)

 SCN8A_MOUSE             Reviewed;        1978 AA.
Q9WTU3; Q3TYI3; Q60828; Q60858; Q62449;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
30-AUG-2017, entry version 139.
RecName: Full=Sodium channel protein type 8 subunit alpha;
AltName: Full=Sodium channel protein type VIII subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.6;
Name=Scn8a; Synonyms=Nbna1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAD20438.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAD20438.1};
PubMed=9828131; DOI=10.1006/geno.1998.5550;
Plummer N.W., Galt J., Jones J.M., Burgess D.L., Sprunger L.K.,
Kohrman D.C., Meisler M.H.;
"Exon organization, coding sequence, physical mapping, and polymorphic
intragenic markers for the human neuronal sodium channel gene SCN8A.";
Genomics 54:287-296(1998).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
DISEASE.
STRAIN=C57BL/6J {ECO:0000269|PubMed:7670495};
TISSUE=Brain {ECO:0000269|PubMed:7670495};
PubMed=7670495; DOI=10.1038/ng0895-461;
Burgess D.L., Kohrman D.C., Galt J., Plummer N.W., Jones J.M.,
Spear B., Meisler M.H.;
"Mutation of a new sodium channel gene, Scn8a, in the mouse mutant
'motor endplate disease'.";
Nat. Genet. 10:461-465(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-804, AND VARIANT LEU-5.
STRAIN=C57BL/6J; TISSUE=Visual cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-205, AND DISEASE.
STRAIN=129/Sv {ECO:0000269|PubMed:8663325};
TISSUE=Brain {ECO:0000269|PubMed:8663325};
PubMed=8663325; DOI=10.1074/jbc.271.29.17576;
Kohrman D.C., Harris J.B., Meisler M.H.;
"Mutation detection in the med and medJ alleles of the sodium channel
Scn8a. Unusual splicing due to a minor class AT-AC intron.";
J. Biol. Chem. 271:17576-17581(1996).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 1411-1686.
Fan Z., Kyle J.W., Makielski J.C.;
"A putative novel Na channel alpha subunit cDNA isolated from mouse
NB2a neuroblastoma cells.";
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH NEDD4 AND NEDD4L.
PubMed=15123669; DOI=10.1074/jbc.M402820200;
Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
"Regulation of neuronal voltage-gated sodium channels by the
ubiquitin-protein ligases Nedd4 and Nedd4-2.";
J. Biol. Chem. 279:28930-28935(2004).
[7] {ECO:0000305}
ALTERNATIVE SPLICING (ISOFORMS 1; 4 AND 5).
TISSUE=Brain {ECO:0000269|PubMed:9295353}, and
Fetal brain {ECO:0000269|PubMed:9295353};
PubMed=9295353; DOI=10.1074/jbc.272.38.24008;
Plummer N.W., McBurney M.W., Meisler M.H.;
"Alternative splicing of the sodium channel SCN8A predicts a truncated
two-domain protein in fetal brain and non-neuronal cells.";
J. Biol. Chem. 272:24008-24015(1997).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19136557; DOI=10.1074/jbc.M801892200;
Carrithers M.D., Chatterjee G., Carrithers L.M., Offoha R.,
Iheagwara U., Rahner C., Graham M., Waxman S.G.;
"Regulation of podosome formation in macrophages by a splice variant
of the sodium channel SCN8A.";
J. Biol. Chem. 284:8114-8126(2009).
[9] {ECO:0000305}
VARIANT MEDJO THR-1317, AND VARIANT LEU-5.
STRAIN=DBA/2WyDi {ECO:0000269|PubMed:8815882};
PubMed=8815882;
Kohrman D.C., Smith M.R., Goldin A.L., Harris J., Meisler M.H.;
"A missense mutation in the sodium channel Scn8a is responsible for
cerebellar ataxia in the mouse mutant jolting.";
J. Neurosci. 16:5993-5999(1996).
[10] {ECO:0000305}
DISEASE.
PubMed=11532991; DOI=10.1093/hmg/10.17.1819;
De Repentigny Y., Cote P.D., Pool M., Bernier G., Girard S.,
Vidal S.M., Kothary R.;
"Pathological and genetic analysis of the degenerating muscle (dmu)
mouse: a new allele of Scn8a.";
Hum. Mol. Genet. 10:1819-1827(2001).
-!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
of excitable membranes. 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. In
macrophages, isoform 5 may participate in the control of podosome
and invadopodia formation. {ECO:0000269|PubMed:19136557}.
-!- 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 (By
similarity). Interacts with NEDD4 and NEDD4L (PubMed:15123669).
Interacts with FGF14, GBG3, GBB2 and SCN1B (By similarity).
Interacts with the conotoxin GVIIJ. {ECO:0000250|UniProtKB:O88420,
ECO:0000250|UniProtKB:Q9UQD0, ECO:0000269|PubMed:15123669}.
-!- INTERACTION:
P14873:Map1b; NbExp=7; IntAct=EBI-6396042, EBI-764653;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19136557};
Multi-pass membrane protein {ECO:0000269|PubMed:19136557}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|PubMed:9295353, ECO:0000269|PubMed:9828131};
Synonyms=18A {ECO:0000269|PubMed:9295353};
IsoId=Q9WTU3-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:7670495};
IsoId=Q9WTU3-2; Sequence=VSP_050594;
Note=Due to aberrant splicing.;
Name=3 {ECO:0000269|PubMed:9828131};
IsoId=Q9WTU3-3; Sequence=VSP_050595;
Name=4 {ECO:0000269|PubMed:9295353}; Synonyms=18N
{ECO:0000269|PubMed:9295353};
IsoId=Q9WTU3-4; Sequence=VSP_050596, VSP_050597;
Name=5 {ECO:0000269|PubMed:9295353};
IsoId=Q9WTU3-5; Sequence=VSP_050598;
-!- TISSUE SPECIFICITY: Expressed in brain, cerebellum and spinal
cord. Isoform 5 may be expressed in non-neuronal tissues, such as
peritoneal macrophages. {ECO:0000269|PubMed:19136557,
ECO:0000269|PubMed:7670495}.
-!- 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: May be ubiquitinated by NEDD4L; which would promote its
endocytosis. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-1495 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000250}.
-!- DISEASE: Note=Defects in Scn8a are the cause of motor endplate
disease (med). Med is a recessive neuromuscular disorder that is
characterized by lack of signal transmission at the neuromuscular
junction, excess preterminal arborization and degeneration of
cerebellar Purkinje cells. It produces early onset progressive
paralysis of hind limbs, severe muscle atrophy and juvenile
lethality.
-!- DISEASE: Note=Defects in Scn8a are the cause of the jolting mutant
(medjo), a mild form of motor endplate disease which is
characterized by the absence of spontaneous, regular, simple
discharges from Purkinje cells. After 3 weeks of age, jolting mice
are unsteady and have wide-based gait and a rhythmical tremor of
head and neck induced by attempted movement.
{ECO:0000269|PubMed:7670495, ECO:0000269|PubMed:8815882}.
-!- DISEASE: Note=Defects in Scn8a are a cause of degenerating muscle
(dmu). Dmu is an autosomal recessive neuromuscular disorder that
is characterized by skeletal and cardiac muscle degeneration. It
produces early onset progressive loss of mobility of the hind
limbs and subsequent lethality in the first month of life.
{ECO:0000269|PubMed:11532991, ECO:0000305|PubMed:8663325}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.6/SCN8A subfamily. {ECO:0000305}.
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EMBL; AF049617; AAD20438.1; -; mRNA.
EMBL; U26707; AAC52242.1; -; mRNA.
EMBL; AK158609; BAE34580.1; -; mRNA.
EMBL; U59964; AAC52708.1; -; Genomic_DNA.
EMBL; U59963; AAC52708.1; JOINED; Genomic_DNA.
EMBL; U23158; AAA65599.1; -; mRNA.
CCDS; CCDS57011.1; -. [Q9WTU3-1]
RefSeq; NP_001070967.1; NM_001077499.2.
RefSeq; NP_035453.2; NM_011323.3.
UniGene; Mm.385012; -.
PDB; 3WFN; X-ray; 1.95 A; B/C/D/E=1893-1914.
PDBsum; 3WFN; -.
ProteinModelPortal; Q9WTU3; -.
SMR; Q9WTU3; -.
BioGrid; 203103; 3.
IntAct; Q9WTU3; 1.
STRING; 10090.ENSMUSP00000080842; -.
BindingDB; Q9WTU3; -.
ChEMBL; CHEMBL1914275; -.
GuidetoPHARMACOLOGY; 583; -.
iPTMnet; Q9WTU3; -.
PhosphoSitePlus; Q9WTU3; -.
PaxDb; Q9WTU3; -.
PRIDE; Q9WTU3; -.
GeneID; 20273; -.
KEGG; mmu:20273; -.
CTD; 6334; -.
MGI; MGI:103169; Scn8a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG091796; -.
InParanoid; Q9WTU3; -.
KO; K04840; -.
PhylomeDB; Q9WTU3; -.
ChiTaRS; Scn8a; mouse.
PRO; PR:Q9WTU3; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_SCN8A; -.
GO; GO:0030425; C:dendrite; 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:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0034706; C:sodium channel complex; IPI:MGI.
GO; GO:0001518; C:voltage-gated sodium channel complex; IC:UniProtKB.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:UniProtKB.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0007517; P:muscle organ development; IMP:MGI.
GO; GO:0050905; P:neuromuscular process; IMP:MGI.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0009636; P:response to toxic substance; IDA:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR008054; Na_channel_a8su.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR024583; Na_trans_cytopl.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF00612; IQ; 1.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
PRINTS; PR01667; NACHANNEL8.
SMART; SM00015; IQ; 1.
PROSITE; PS50096; IQ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Sodium;
Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation; Voltage-gated channel.
CHAIN 1 1978 Sodium channel protein type 8 subunit
alpha.
/FTId=PRO_0000048501.
TOPO_DOM 1 132 Cytoplasmic. {ECO:0000305}.
TRANSMEM 133 151 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 152 158 Extracellular. {ECO:0000305}.
TRANSMEM 159 179 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 180 193 Cytoplasmic. {ECO:0000305}.
TRANSMEM 194 211 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 212 217 Extracellular. {ECO:0000305}.
TRANSMEM 218 234 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 235 253 Cytoplasmic. {ECO:0000305}.
TRANSMEM 254 273 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 274 355 Extracellular. {ECO:0000305}.
INTRAMEM 356 380 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 381 387 Extracellular. {ECO:0000305}.
TRANSMEM 388 408 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 409 751 Cytoplasmic. {ECO:0000305}.
TRANSMEM 752 770 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 771 781 Extracellular. {ECO:0000305}.
TRANSMEM 782 801 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 802 815 Cytoplasmic. {ECO:0000305}.
TRANSMEM 816 835 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 836 837 Extracellular. {ECO:0000305}.
TRANSMEM 838 855 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 856 871 Cytoplasmic. {ECO:0000305}.
TRANSMEM 872 890 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 891 919 Extracellular. {ECO:0000305}.
INTRAMEM 920 940 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 941 953 Extracellular. {ECO:0000305}.
TRANSMEM 954 974 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 975 1197 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1198 1215 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1216 1228 Extracellular. {ECO:0000305}.
TRANSMEM 1229 1247 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1248 1261 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1262 1280 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1281 1288 Extracellular. {ECO:0000305}.
TRANSMEM 1289 1307 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1308 1324 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1325 1344 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1345 1397 Extracellular. {ECO:0000305}.
INTRAMEM 1398 1419 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1420 1436 Extracellular. {ECO:0000305}.
TRANSMEM 1437 1458 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1459 1521 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1522 1539 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1540 1550 Extracellular. {ECO:0000305}.
TRANSMEM 1551 1569 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1570 1581 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1582 1599 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1600 1612 Extracellular. {ECO:0000305}.
TRANSMEM 1613 1629 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1630 1648 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1649 1666 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1667 1688 Extracellular. {ECO:0000305}.
INTRAMEM 1689 1711 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1712 1740 Extracellular. {ECO:0000305}.
TRANSMEM 1741 1763 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1764 1978 Cytoplasmic. {ECO:0000305}.
REPEAT 114 442 I. {ECO:0000305}.
REPEAT 733 1005 II. {ECO:0000305}.
REPEAT 1178 1493 III. {ECO:0000305}.
REPEAT 1502 1799 IV. {ECO:0000305}.
DOMAIN 1893 1922 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116, ECO:0000305}.
NP_BIND 891 898 ATP. {ECO:0000255}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000250|UniProtKB:O88420}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000250|UniProtKB:O88420}.
MOD_RES 1495 1495 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q15858}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 326 326 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1356 1356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1370 1370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1381 1381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 281 333 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 902 902 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 902 902 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 942 951 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 428 673 Missing (in isoform 2).
{ECO:0000303|PubMed:7670495}.
/FTId=VSP_050594.
VAR_SEQ 664 664 E -> EVKIDKAATDS (in isoform 3).
{ECO:0000303|PubMed:9828131}.
/FTId=VSP_050595.
VAR_SEQ 1272 1312 Missing (in isoform 5).
{ECO:0000303|PubMed:9295353}.
/FTId=VSP_050598.
VAR_SEQ 1273 1280 SLVSLIAN -> PLSLSGLI (in isoform 4).
{ECO:0000303|PubMed:9295353}.
/FTId=VSP_050596.
VAR_SEQ 1281 1978 Missing (in isoform 4).
{ECO:0000303|PubMed:9295353}.
/FTId=VSP_050597.
VARIANT 5 5 V -> L. {ECO:0000269|PubMed:16141072,
ECO:0000269|PubMed:8815882}.
VARIANT 1317 1317 A -> T (in medjo).
{ECO:0000269|PubMed:8815882}.
CONFLICT 207 207 V -> I (in Ref. 3; BAE34580).
{ECO:0000305}.
CONFLICT 212 212 D -> N (in Ref. 3; BAE34580).
{ECO:0000305}.
CONFLICT 554 554 P -> T (in Ref. 3; BAE34580).
{ECO:0000305}.
CONFLICT 596 596 G -> D (in Ref. 3; BAE34580).
{ECO:0000305}.
CONFLICT 1498 1498 P -> A (in Ref. 5; AAA65599).
{ECO:0000305}.
CONFLICT 1504 1504 R -> E (in Ref. 5; AAA65599).
{ECO:0000305}.
HELIX 1893 1912 {ECO:0000244|PDB:3WFN}.
SEQUENCE 1978 AA; 225141 MW; 9EA4A8E610707220 CRC64;
MAARVLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED SKPKPNSDLE
AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG KTLFRFSATP ALYILSPFNL
IRRIAIKILI HSVFSMIIMC TILTNCVFMT FSNPPEWSKN VEYTFTGIYT FESLVKIIAR
GFCIDGFTFL RDPWNWLDFS VIMMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI
VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTRGF
DWEEYINNKT NFYMVPGMLE PLLCGNSSDA GQCPEGFQCM KAGRNPNYGY TSFDTFSWAF
LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF YLVNLILAVV AMAYEEQNQA
TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA MATSAGTVSE DAIEEEGEDG VGSPRSSSEL
SKLSSKSAKE RRNRRKKRKQ KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF
SIMNQSLLSI PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS
LFIPIRARER RSSYSGYSGY SQCSRSSRIF PSLRRSVKRN STVDCNGVVS LIGPGSHIGR
LLPEATTEVE IKKKGPGSLL VSMEQLASYG RKDRINSIMS VVTNTLVEEL EESQRKCPPC
WYKFANTFLI WECHPYWIKL KEIVNLIVMD PFVDLAITIC IVLNTLFMAM EHHPMTPQFE
HVLAVGNLVF TGIFTAEMFL KLIAMDPYYY FQEGWNIFDG FIVSLSLMEL GLADVEGLSV
LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL AIIVFIFAVV GMQLFGKSYK
ECVCKISQEC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW DCMEVAGQAM CLIVFMMVMV
IGNLVVLNLF LALLLSSFSA DNLAATDDDG EMNNLQISVI RIKKGVAWAK VKVHAFMQAH
FKQREADEVK PLDELYEKKA NCIANHTGVD IHRNGDFQKN GNGTTSGIGS SVEKYIIDED
HMSFINNPNL TVRVPIAVGE SDFENLNTED VSSESDPEGS KDKLDDTSSS EGSTIDIKPE
VEEVPVEQPE EYLDPDACFT EGCVQRFKCC QVNIEEGLGK SWWILRKTCF LIVEHNWFET
FIIFMILLSS GALAFEDIYI EQRKTIRTIL EYADKVFTYI FILEMLLKWT AYGFVKFFTN
AWCWLDFLIV AVSLVSLIAN ALGYSELGAI KSLRTLRALR PLRALSRFEG MRVVVNALVG
AIPSIMNVLL VCLIFWLIFS IMGVNLFAGK YHYCFNETSE IRFEIDEVNN KTDCEKLMEG
NNTEIRWKNV KINFDNVGAG YLALLQVATF KGWMDIMYAA VDSRKPDEQP DYEGNIYMYI
YFVIFIIFGS FFTLNLFIGV IIDNFNQQKK KFGGQDIFMT EEQKKYYNAM KKLGSKKPQK
PIPRPLNKIQ GIVFDFVTQQ AFDIVIMMLI CLNMVTMMVE TDTQSKQMEN ILYWINLVFV
IFFTCECVLK MFALRHYYFT IGWNIFDFVV VILSIVGMFL ADIIEKYFVS PTLFRVIRLA
RIGRILRLIK GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIFSIFGMSN FAYVKHEAGI
DDMFNFETFG NSMICLFQIT TSAGWDGLLL PILNRPPDCS LDKEHPGSGF KGDCGNPSVG
IFFFVSYIII SFLIVVNMYI AIILENFSVA TEESADPLSE DDFETFYEIW EKFDPDATQF
IEYCKLADFA DALEHPLRVP KPNTIELIAM DLPMVSGDRI HCLDILFAFT KRVLGDSGEL
DILRQQMEER FVASNPSKVS YEPITTTLRR KQEEVSAVVL QRAYRGHLAR RGFICRKITS
NKLENGGTHR EKKESTPSTA SLPSYDSVTK PDKEKQQRAE EGRRERAKRQ KEVRESKC


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