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Sodium channel protein type 3 subunit alpha (Sodium channel protein brain III subunit alpha) (Sodium channel protein type III subunit alpha) (Voltage-gated sodium channel subtype III) (Voltage-gated sodium channel subunit alpha Nav1.3)

 SCN3A_HUMAN             Reviewed;        2000 AA.
Q9NY46; Q16142; Q53SX0; Q9BZB3; Q9C006; Q9NYK2; Q9P2J1; Q9UPD1;
Q9Y6P4;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
08-NOV-2002, sequence version 2.
31-JAN-2018, entry version 167.
RecName: Full=Sodium channel protein type 3 subunit alpha;
AltName: Full=Sodium channel protein brain III subunit alpha;
AltName: Full=Sodium channel protein type III subunit alpha;
AltName: Full=Voltage-gated sodium channel subtype III;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.3;
Name=SCN3A; Synonyms=KIAA1356, NAC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
Chen Y., Dale T.J., Romanos M.A., Whitaker W.R., Xie X., Clare J.J.;
"Cloning, distribution and functional analysis of the human brain type
III sodium channel from human brain.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Jeong S.-Y., Goto J., Kanazawa I.;
"Cloning of cDNA for human voltage-gated sodium channel alpha subunit,
SCN3A.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH NEDD4L, POSSIBLE UBIQUITINATION, AND MUTAGENESIS OF
TYR-1970.
PubMed=15548568; DOI=10.1152/ajpcell.00460.2004;
Rougier J.-S., van Bemmelen M.X., Bruce M.C., Jespersen T.,
Gavillet B., Apotheloz F., Cordonier S., Staub O., Rotin D.,
Abriel H.;
"Molecular determinants of voltage-gated sodium channel regulation by
the Nedd4/Nedd4-like proteins.";
Am. J. Physiol. 288:C692-C701(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4), AND
VARIANT THR-606.
PubMed=11245985; DOI=10.1016/S0378-1119(00)00594-1;
Kasai N., Fukushima K., Ueki Y., Prasad S., Nosakowski J., Sugata K.,
Sugata A., Nishizaki K., Meyer N.C., Smith R.J.H.;
"Genomic structures of SCN2A and SCN3A -- candidate genes for deafness
at the DFNA16 locus.";
Gene 264:113-122(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1415 (ISOFORMS 2 AND 4).
TISSUE=Brain;
PubMed=9589372; DOI=10.1007/BF02737087;
Lu C.M., Brown G.B.;
"Isolation of a human-brain sodium-channel gene encoding two isoforms
of the subtype III alpha-subunit.";
J. Mol. Neurosci. 10:67-70(1998).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1324-1413.
TISSUE=Placenta;
PubMed=8159690; DOI=10.1073/pnas.91.8.2975;
Malo M.S., Srivastava K., Andresen J.M., Chen X.N., Korenberg J.R.,
Ingram V.M.;
"Targeted gene walking by low stringency polymerase chain reaction:
assignment of a putative human brain sodium channel gene (SCN3A) to
chromosome 2q24-31.";
Proc. Natl. Acad. Sci. U.S.A. 91:2975-2979(1994).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1482-2000.
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1669-1750.
TISSUE=Kidney;
Tonkovich G.S., Kyle J.W.;
"Endogenous sodium current in HEK293 cells: increase in cell surface
expression of endogenous currents by stable transfection of the Beta 1
subunit.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[10]
INTERACTION WITH THE CONOTOXIN GVIIJ.
PubMed=24497506; DOI=10.1073/pnas.1324189111;
Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
"A disulfide tether stabilizes the block of sodium channels by the
conotoxin muO[section sign]-GVIIJ.";
Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
[11]
VARIANTS ASN-43 DEL AND SER-1813.
PubMed=12610651; DOI=10.1038/sj.mp.4001241;
Weiss L.A., Escayg A., Kearney J.A., Trudeau M., MacDonald B.T.,
Mori M., Reichert J., Buxbaum J.D., Meisler M.H.;
"Sodium channels SCN1A, SCN2A and SCN3A in familial autism.";
Mol. Psychiatry 8:186-194(2003).
[12]
VARIANT ILE-1084.
PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
"Homozygous missense mutation in the LMAN2L gene segregates with
intellectual disability in a large consanguineous Pakistani family.";
J. Med. Genet. 53:138-144(2016).
-!- 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.
-!- SUBUNIT: Heterooligomer of a large alpha subunit and 2-3 smaller
beta subunits. Heterooligomer with SCN2B or SCN4B; disulfide-
linked. Interacts with NEDD4L (PubMed:15548568). Interacts with
the conotoxin GVIIJ (PubMed:24497506).
{ECO:0000269|PubMed:15548568, ECO:0000269|PubMed:24497506}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Exons 6A and 6N only differ by a single residue.;
Name=1; Synonyms=6A-12+12b;
IsoId=Q9NY46-1; Sequence=Displayed;
Name=2; Synonyms=6A-12;
IsoId=Q9NY46-2; Sequence=VSP_001034;
Name=3; Synonyms=6N-12+12b;
IsoId=Q9NY46-3; Sequence=VSP_001033;
Name=4; Synonyms=6N-12;
IsoId=Q9NY46-4; Sequence=VSP_001033, VSP_001034;
-!- 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.
-!- PTM: Phosphorylation at Ser-1501 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.3/SCN3A subfamily. {ECO:0000305}.
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EMBL; AJ251507; CAB85895.1; -; mRNA.
EMBL; AF225987; AAK00219.1; -; mRNA.
EMBL; AF330135; AAG53414.1; -; Genomic_DNA.
EMBL; AF330118; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330119; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330120; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330121; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330122; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330123; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330124; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330125; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330126; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330127; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330128; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330129; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330130; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330131; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330132; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330133; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330134; AAG53414.1; JOINED; Genomic_DNA.
EMBL; AF330135; AAG53415.1; -; Genomic_DNA.
EMBL; AF330118; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330119; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330120; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330121; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330122; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330123; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330124; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330125; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330126; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330127; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330128; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330129; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330130; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330131; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330132; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330133; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AF330134; AAG53415.1; JOINED; Genomic_DNA.
EMBL; AC013463; AAY15072.1; -; Genomic_DNA.
EMBL; AF035685; AAC29514.1; -; mRNA.
EMBL; AF035686; AAC29515.1; -; mRNA.
EMBL; S69887; AAB30530.1; -; Genomic_DNA.
EMBL; AB037777; BAA92594.1; -; mRNA.
EMBL; AF239921; AAF44690.1; -; mRNA.
CCDS; CCDS33312.1; -. [Q9NY46-3]
CCDS; CCDS46440.1; -. [Q9NY46-2]
PIR; A54937; A54937.
RefSeq; NP_001075145.1; NM_001081676.1. [Q9NY46-4]
RefSeq; NP_001075146.1; NM_001081677.1. [Q9NY46-2]
RefSeq; NP_008853.3; NM_006922.3. [Q9NY46-3]
RefSeq; XP_011509912.1; XM_011511610.2. [Q9NY46-3]
RefSeq; XP_016860149.1; XM_017004660.1. [Q9NY46-1]
UniGene; Hs.435274; -.
ProteinModelPortal; Q9NY46; -.
SMR; Q9NY46; -.
BioGrid; 112233; 6.
IntAct; Q9NY46; 2.
MINT; MINT-8330038; -.
STRING; 9606.ENSP00000283254; -.
BindingDB; Q9NY46; -.
ChEMBL; CHEMBL5163; -.
DrugBank; DB06218; Lacosamide.
DrugBank; DB05232; Tetrodotoxin.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB00909; Zonisamide.
GuidetoPHARMACOLOGY; 580; -.
iPTMnet; Q9NY46; -.
PhosphoSitePlus; Q9NY46; -.
BioMuta; SCN3A; -.
DMDM; 25014054; -.
PaxDb; Q9NY46; -.
PeptideAtlas; Q9NY46; -.
PRIDE; Q9NY46; -.
Ensembl; ENST00000283254; ENSP00000283254; ENSG00000153253. [Q9NY46-3]
Ensembl; ENST00000360093; ENSP00000353206; ENSG00000153253. [Q9NY46-1]
Ensembl; ENST00000409101; ENSP00000386726; ENSG00000153253. [Q9NY46-2]
GeneID; 6328; -.
KEGG; hsa:6328; -.
UCSC; uc002ucx.4; human. [Q9NY46-1]
CTD; 6328; -.
DisGeNET; 6328; -.
EuPathDB; HostDB:ENSG00000153253.15; -.
GeneCards; SCN3A; -.
HGNC; HGNC:10590; SCN3A.
HPA; HPA035396; -.
MIM; 182391; gene.
neXtProt; NX_Q9NY46; -.
OpenTargets; ENSG00000153253; -.
PharmGKB; PA35005; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128242; -.
HOVERGEN; HBG053100; -.
InParanoid; Q9NY46; -.
KO; K04836; -.
OMA; EGCIKKF; -.
OrthoDB; EOG091G00FK; -.
PhylomeDB; Q9NY46; -.
TreeFam; TF323985; -.
Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
SIGNOR; Q9NY46; -.
ChiTaRS; SCN3A; human.
GeneWiki; SCN3A; -.
GenomeRNAi; 6328; -.
PRO; PR:Q9NY46; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000153253; -.
CleanEx; HS_SCN3A; -.
ExpressionAtlas; Q9NY46; baseline and differential.
Genevisible; Q9NY46; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR024583; Na_trans_cytopl.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
PROSITE; PS50096; IQ; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Sodium;
Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation; Voltage-gated channel.
CHAIN 1 2000 Sodium channel protein type 3 subunit
alpha.
/FTId=PRO_0000048493.
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 270 368 Extracellular. {ECO:0000305}.
INTRAMEM 369 393 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 394 400 Extracellular. {ECO:0000305}.
TRANSMEM 401 421 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 422 760 Cytoplasmic. {ECO:0000305}.
TRANSMEM 761 779 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 780 790 Extracellular. {ECO:0000305}.
TRANSMEM 791 810 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 811 824 Cytoplasmic. {ECO:0000305}.
TRANSMEM 825 844 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 845 846 Extracellular. {ECO:0000305}.
TRANSMEM 847 864 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 865 880 Cytoplasmic. {ECO:0000305}.
TRANSMEM 881 899 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 900 928 Extracellular. {ECO:0000305}.
INTRAMEM 929 949 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 950 962 Extracellular. {ECO:0000305}.
TRANSMEM 963 983 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 984 1207 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1208 1225 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1226 1238 Extracellular. {ECO:0000305}.
TRANSMEM 1239 1257 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1258 1271 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1272 1290 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1291 1298 Extracellular. {ECO:0000305}.
TRANSMEM 1299 1317 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1318 1334 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1335 1354 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1355 1403 Extracellular. {ECO:0000305}.
INTRAMEM 1404 1425 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1426 1442 Extracellular. {ECO:0000305}.
TRANSMEM 1443 1464 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1465 1527 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1528 1545 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1546 1556 Extracellular. {ECO:0000305}.
TRANSMEM 1557 1575 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1576 1587 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1588 1605 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1606 1618 Extracellular. {ECO:0000305}.
TRANSMEM 1619 1635 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1636 1654 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1655 1672 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1673 1694 Extracellular. {ECO:0000305}.
INTRAMEM 1695 1717 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1718 1747 Extracellular. {ECO:0000305}.
TRANSMEM 1748 1770 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1771 2000 Cytoplasmic. {ECO:0000305}.
REPEAT 110 455 I. {ECO:0000305}.
REPEAT 742 1014 II. {ECO:0000305}.
REPEAT 1188 1499 III. {ECO:0000305}.
REPEAT 1508 1806 IV. {ECO:0000305}.
DOMAIN 1900 1929 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:P08104}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000250|UniProtKB:P08104}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000250|UniProtKB:P08104}.
MOD_RES 1501 1501 Phosphoserine; by PKC. {ECO:0000250}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1366 1366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1380 1380 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 277 346 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 911 911 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 911 911 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 951 960 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 208 208 S -> D (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:9589372,
ECO:0000303|Ref.2}.
/FTId=VSP_001033.
VAR_SEQ 625 673 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:9589372,
ECO:0000303|Ref.1}.
/FTId=VSP_001034.
VARIANT 43 43 Missing. {ECO:0000269|PubMed:12610651}.
/FTId=VAR_029743.
VARIANT 606 606 S -> T. {ECO:0000269|PubMed:11245985}.
/FTId=VAR_014275.
VARIANT 1084 1084 V -> I (in dbSNP:rs140990288).
{ECO:0000269|PubMed:26566883}.
/FTId=VAR_076435.
VARIANT 1107 1107 V -> A (in dbSNP:rs12474273).
/FTId=VAR_029744.
VARIANT 1803 1803 D -> N (in dbSNP:rs3731762).
/FTId=VAR_055640.
VARIANT 1813 1813 L -> S. {ECO:0000269|PubMed:12610651}.
/FTId=VAR_029745.
MUTAGEN 1970 1970 Y->A: Abolishes interaction with NEDD4L.
{ECO:0000269|PubMed:15548568}.
CONFLICT 175 175 A -> V (in Ref. 4; AAC29514/AAC29515).
{ECO:0000305}.
CONFLICT 318 318 Y -> N (in Ref. 4; AAC29514/AAC29515).
{ECO:0000305}.
CONFLICT 401 401 M -> T (in Ref. 4; AAC29514/AAC29515).
{ECO:0000305}.
CONFLICT 475 475 I -> V (in Ref. 2; AAK00219).
{ECO:0000305}.
CONFLICT 495 495 S -> G (in Ref. 2; AAK00219).
{ECO:0000305}.
CONFLICT 604 604 S -> G (in Ref. 2; AAK00219).
{ECO:0000305}.
CONFLICT 613 613 V -> E (in Ref. 4; AAC29514/AAC29515).
{ECO:0000305}.
CONFLICT 1060 1060 E -> A (in Ref. 4; AAC29514/AAC29515).
{ECO:0000305}.
CONFLICT 1163 1163 L -> F (in Ref. 2; AAK00219).
{ECO:0000305}.
CONFLICT 1274 1274 W -> R (in Ref. 4; AAC29514/AAC29515).
{ECO:0000305}.
CONFLICT 1329 1329 V -> L (in Ref. 6; AAB30530).
{ECO:0000305}.
CONFLICT 1414 1415 AT -> VS (in Ref. 4; AAC29514/AAC29515).
{ECO:0000305}.
CONFLICT 1614 1614 F -> S (in Ref. 2; AAK00219).
{ECO:0000305}.
CONFLICT 1741 1743 CGN -> RGD (in Ref. 2; AAK00219).
{ECO:0000305}.
CONFLICT 1862 1862 G -> C (in Ref. 2; AAK00219).
{ECO:0000305}.
CONFLICT 1966 1966 S -> P (in Ref. 2; AAK00219).
{ECO:0000305}.
SEQUENCE 2000 AA; 226294 MW; F754A1C7D49ECB58 CRC64;
MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDNDDENKPK PNSDLEAGKN
LPFIYGDIPP EMVSEPLEDL DPYYINKKTF IVMNKGKAIF RFSATSALYI LTPLNPVRKI
AIKILVHSLF SMLIMCTILT NCVFMTLSNP PDWTKNVEYT FTGIYTFESL IKILARGFCL
EDFTFLRDPW NWLDFSVIVM AYVTEFVSLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCLQW PPSDSAFETN TTSYFNGTMD
SNGTFVNVTM STFNWKDYIG DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY ICVKAGRNPN
YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY MIFFVLVIFL GSFYLVNLIL
AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE QLKKQQEEAQ AVAAASAASR DFSGIGGLGE
LLESSSEASK LSSKSAKEWR NRRKKRRQRE HLEGNNKGER DSFPKSESED SVKRSSFLFS
MDGNRLTSDK KFCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
FEDSESRRDS LFVPHRHGER RNSNVSQASM SSRMVPGLPA NGKMHSTVDC NGVVSLVGGP
SALTSPTGQL PPEGTTTETE VRKRRLSSYQ ISMEMLEDSS GRQRAVSIAS ILTNTMEELE
ESRQKCPPCW YRFANVFLIW DCCDAWLKVK HLVNLIVMDP FVDLAITICI VLNTLFMAME
HYPMTEQFSS VLTVGNLVFT GIFTAEMVLK IIAMDPYYYF QEGWNIFDGI IVSLSLMELG
LSNVEGLSVL RSFRLLRVFK LAKSWPTLNM LIKIIGNSVG ALGNLTLVLA IIVFIFAVVG
MQLFGKSYKE CVCKINDDCT LPRWHMNDFF HSFLIVFRVL CGEWIETMWD CMEVAGQTMC
LIVFMLVMVI GNLVVLNLFL ALLLSSFSSD NLAATDDDNE MNNLQIAVGR MQKGIDYVKN
KMRECFQKAF FRKPKVIEIH EGNKIDSCMS NNTGIEISKE LNYLRDGNGT TSGVGTGSSV
EKYVIDENDY MSFINNPSLT VTVPIAVGES DFENLNTEEF SSESELEESK EKLNATSSSE
GSTVDVVLPR EGEQAETEPE EDLKPEACFT EGCIKKFPFC QVSTEEGKGK IWWNLRKTCY
SIVEHNWFET FIVFMILLSS GALAFEDIYI EQRKTIKTML EYADKVFTYI FILEMLLKWV
AYGFQTYFTN AWCWLDFLIV DVSLVSLVAN ALGYSELGAI KSLRTLRALR PLRALSRFEG
MRVVVNALVG AIPSIMNVLL VCLIFWLIFS IMGVNLFAGK FYHCVNMTTG NMFDISDVNN
LSDCQALGKQ ARWKNVKVNF DNVGAGYLAL LQVATFKGWM DIMYAAVDSR DVKLQPVYEE
NLYMYLYFVI FIIFGSFFTL NLFIGVIIDN FNQQKKKFGG QDIFMTEEQK KYYNAMKKLG
SKKPQKPIPR PANKFQGMVF DFVTRQVFDI SIMILICLNM VTMMVETDDQ GKYMTLVLSR
INLVFIVLFT GEFVLKLVSL RHYYFTIGWN IFDFVVVILS IVGMFLAEMI EKYFVSPTLF
RVIRLARIGR ILRLIKGAKG IRTLLFALMM SLPALFNIGL LLFLVMFIYA IFGMSNFAYV
KKEAGIDDMF NFETFGNSMI CLFQITTSAG WDGLLAPILN SAPPDCDPDT IHPGSSVKGD
CGNPSVGIFF FVSYIIISFL VVVNMYIAVI LENFSVATEE SAEPLSEDDF EMFYEVWEKF
DPDATQFIEF SKLSDFAAAL DPPLLIAKPN KVQLIAMDLP MVSGDRIHCL DILFAFTKRV
LGESGEMDAL RIQMEDRFMA SNPSKVSYEP ITTTLKRKQE EVSAAIIQRN FRCYLLKQRL
KNISSNYNKE AIKGRIDLPI KQDMIIDKLN GNSTPEKTDG SSSTTSPPSY DSVTKPDKEK
FEKDKPEKES KGKEVRENQK


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