GenomeNet

Database: UniProt
Entry: SCN3A_HUMAN
LinkDB: SCN3A_HUMAN
Original site: SCN3A_HUMAN 
ID   SCN3A_HUMAN             Reviewed;        2000 AA.
AC   Q9NY46; Q16142; Q53SX0; Q9BZB3; Q9C006; Q9NYK2; Q9P2J1; Q9UPD1;
AC   Q9Y6P4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   27-SEP-2017, entry version 166.
DE   RecName: Full=Sodium channel protein type 3 subunit alpha;
DE   AltName: Full=Sodium channel protein brain III subunit alpha;
DE   AltName: Full=Sodium channel protein type III subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subtype III;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.3;
GN   Name=SCN3A; Synonyms=KIAA1356, NAC3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Chen Y., Dale T.J., Romanos M.A., Whitaker W.R., Xie X., Clare J.J.;
RT   "Cloning, distribution and functional analysis of the human brain type
RT   III sodium channel from human brain.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Jeong S.-Y., Goto J., Kanazawa I.;
RT   "Cloning of cDNA for human voltage-gated sodium channel alpha subunit,
RT   SCN3A.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH NEDD4L, POSSIBLE UBIQUITINATION, AND MUTAGENESIS OF
RP   TYR-1970.
RX   PubMed=15548568; DOI=10.1152/ajpcell.00460.2004;
RA   Rougier J.-S., van Bemmelen M.X., Bruce M.C., Jespersen T.,
RA   Gavillet B., Apotheloz F., Cordonier S., Staub O., Rotin D.,
RA   Abriel H.;
RT   "Molecular determinants of voltage-gated sodium channel regulation by
RT   the Nedd4/Nedd4-like proteins.";
RL   Am. J. Physiol. 288:C692-C701(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP   VARIANT THR-606.
RX   PubMed=11245985; DOI=10.1016/S0378-1119(00)00594-1;
RA   Kasai N., Fukushima K., Ueki Y., Prasad S., Nosakowski J., Sugata K.,
RA   Sugata A., Nishizaki K., Meyer N.C., Smith R.J.H.;
RT   "Genomic structures of SCN2A and SCN3A -- candidate genes for deafness
RT   at the DFNA16 locus.";
RL   Gene 264:113-122(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-1415 (ISOFORMS 2 AND 4).
RC   TISSUE=Brain;
RX   PubMed=9589372; DOI=10.1007/BF02737087;
RA   Lu C.M., Brown G.B.;
RT   "Isolation of a human-brain sodium-channel gene encoding two isoforms
RT   of the subtype III alpha-subunit.";
RL   J. Mol. Neurosci. 10:67-70(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1324-1413.
RC   TISSUE=Placenta;
RX   PubMed=8159690; DOI=10.1073/pnas.91.8.2975;
RA   Malo M.S., Srivastava K., Andresen J.M., Chen X.N., Korenberg J.R.,
RA   Ingram V.M.;
RT   "Targeted gene walking by low stringency polymerase chain reaction:
RT   assignment of a putative human brain sodium channel gene (SCN3A) to
RT   chromosome 2q24-31.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:2975-2979(1994).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1482-2000.
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI.
RT   The complete sequences of 150 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1669-1750.
RC   TISSUE=Kidney;
RA   Tonkovich G.S., Kyle J.W.;
RT   "Endogenous sodium current in HEK293 cells: increase in cell surface
RT   expression of endogenous currents by stable transfection of the Beta 1
RT   subunit.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   INTERACTION WITH THE CONOTOXIN GVIIJ.
RX   PubMed=24497506; DOI=10.1073/pnas.1324189111;
RA   Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
RA   Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
RA   Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
RA   Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
RT   "A disulfide tether stabilizes the block of sodium channels by the
RT   conotoxin muO[section sign]-GVIIJ.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
RN   [11]
RP   VARIANTS ASN-43 DEL AND SER-1813.
RX   PubMed=12610651; DOI=10.1038/sj.mp.4001241;
RA   Weiss L.A., Escayg A., Kearney J.A., Trudeau M., MacDonald B.T.,
RA   Mori M., Reichert J., Buxbaum J.D., Meisler M.H.;
RT   "Sodium channels SCN1A, SCN2A and SCN3A in familial autism.";
RL   Mol. Psychiatry 8:186-194(2003).
RN   [12]
RP   VARIANT ILE-1084.
RX   PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA   Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA   Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT   "Homozygous missense mutation in the LMAN2L gene segregates with
RT   intellectual disability in a large consanguineous Pakistani family.";
RL   J. Med. Genet. 53:138-144(2016).
CC   -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
CC       of excitable membranes. Assuming opened or closed conformations in
CC       response to the voltage difference across the membrane, the
CC       protein forms a sodium-selective channel through which Na(+) ions
CC       may pass in accordance with their electrochemical gradient.
CC   -!- SUBUNIT: Heterooligomer of a large alpha subunit and 2-3 smaller
CC       beta subunits. Heterooligomer with SCN2B or SCN4B; disulfide-
CC       linked. Interacts with NEDD4L (PubMed:15548568). Interacts with
CC       the conotoxin GVIIJ (PubMed:24497506).
CC       {ECO:0000269|PubMed:15548568, ECO:0000269|PubMed:24497506}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Exons 6A and 6N only differ by a single residue.;
CC       Name=1; Synonyms=6A-12+12b;
CC         IsoId=Q9NY46-1; Sequence=Displayed;
CC       Name=2; Synonyms=6A-12;
CC         IsoId=Q9NY46-2; Sequence=VSP_001034;
CC       Name=3; Synonyms=6N-12+12b;
CC         IsoId=Q9NY46-3; Sequence=VSP_001033;
CC       Name=4; Synonyms=6N-12;
CC         IsoId=Q9NY46-4; Sequence=VSP_001033, VSP_001034;
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1, S2, S3, S5, S6) and one positively
CC       charged segment (S4). Segments S4 are probably the voltage-sensors
CC       and are characterized by a series of positively charged amino
CC       acids at every third position. {ECO:0000305}.
CC   -!- PTM: May be ubiquitinated by NEDD4L; which would promote its
CC       endocytosis.
CC   -!- PTM: Phosphorylation at Ser-1501 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and
CC       reduces peak sodium currents. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.3/SCN3A subfamily. {ECO:0000305}.
DR   EMBL; AJ251507; CAB85895.1; -; mRNA.
DR   EMBL; AF225987; AAK00219.1; -; mRNA.
DR   EMBL; AF330135; AAG53414.1; -; Genomic_DNA.
DR   EMBL; AF330118; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330119; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330120; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330121; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330122; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330123; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330124; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330125; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330126; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330127; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330128; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330129; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330130; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330131; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330132; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330133; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330134; AAG53414.1; JOINED; Genomic_DNA.
DR   EMBL; AF330135; AAG53415.1; -; Genomic_DNA.
DR   EMBL; AF330118; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330119; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330120; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330121; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330122; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330123; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330124; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330125; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330126; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330127; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330128; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330129; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330130; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330131; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330132; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330133; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AF330134; AAG53415.1; JOINED; Genomic_DNA.
DR   EMBL; AC013463; AAY15072.1; -; Genomic_DNA.
DR   EMBL; AF035685; AAC29514.1; -; mRNA.
DR   EMBL; AF035686; AAC29515.1; -; mRNA.
DR   EMBL; S69887; AAB30530.1; -; Genomic_DNA.
DR   EMBL; AB037777; BAA92594.1; -; mRNA.
DR   EMBL; AF239921; AAF44690.1; -; mRNA.
DR   CCDS; CCDS33312.1; -. [Q9NY46-3]
DR   CCDS; CCDS46440.1; -. [Q9NY46-2]
DR   PIR; A54937; A54937.
DR   RefSeq; NP_001075145.1; NM_001081676.1. [Q9NY46-4]
DR   RefSeq; NP_001075146.1; NM_001081677.1. [Q9NY46-2]
DR   RefSeq; NP_008853.3; NM_006922.3. [Q9NY46-3]
DR   RefSeq; XP_011509912.1; XM_011511610.2. [Q9NY46-3]
DR   RefSeq; XP_016860149.1; XM_017004660.1. [Q9NY46-1]
DR   UniGene; Hs.435274; -.
DR   ProteinModelPortal; Q9NY46; -.
DR   SMR; Q9NY46; -.
DR   BioGrid; 112233; 6.
DR   IntAct; Q9NY46; 2.
DR   MINT; MINT-8330038; -.
DR   STRING; 9606.ENSP00000283254; -.
DR   BindingDB; Q9NY46; -.
DR   ChEMBL; CHEMBL5163; -.
DR   DrugBank; DB06218; Lacosamide.
DR   DrugBank; DB05232; Tetrodotoxin.
DR   DrugBank; DB00313; Valproic Acid.
DR   DrugBank; DB00909; Zonisamide.
DR   GuidetoPHARMACOLOGY; 580; -.
DR   iPTMnet; Q9NY46; -.
DR   PhosphoSitePlus; Q9NY46; -.
DR   BioMuta; SCN3A; -.
DR   DMDM; 25014054; -.
DR   PaxDb; Q9NY46; -.
DR   PeptideAtlas; Q9NY46; -.
DR   PRIDE; Q9NY46; -.
DR   Ensembl; ENST00000283254; ENSP00000283254; ENSG00000153253. [Q9NY46-3]
DR   Ensembl; ENST00000360093; ENSP00000353206; ENSG00000153253. [Q9NY46-1]
DR   Ensembl; ENST00000409101; ENSP00000386726; ENSG00000153253. [Q9NY46-2]
DR   GeneID; 6328; -.
DR   KEGG; hsa:6328; -.
DR   UCSC; uc002ucx.4; human. [Q9NY46-1]
DR   CTD; 6328; -.
DR   DisGeNET; 6328; -.
DR   EuPathDB; HostDB:ENSG00000153253.15; -.
DR   GeneCards; SCN3A; -.
DR   HGNC; HGNC:10590; SCN3A.
DR   HPA; HPA035396; -.
DR   MIM; 182391; gene.
DR   neXtProt; NX_Q9NY46; -.
DR   OpenTargets; ENSG00000153253; -.
DR   PharmGKB; PA35005; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128242; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; Q9NY46; -.
DR   KO; K04836; -.
DR   OMA; EGCIKKF; -.
DR   OrthoDB; EOG091G00FK; -.
DR   PhylomeDB; Q9NY46; -.
DR   TreeFam; TF323985; -.
DR   Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR   Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR   SIGNOR; Q9NY46; -.
DR   ChiTaRS; SCN3A; human.
DR   GeneWiki; SCN3A; -.
DR   GenomeRNAi; 6328; -.
DR   PRO; PR:Q9NY46; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000153253; -.
DR   CleanEx; HS_SCN3A; -.
DR   ExpressionAtlas; Q9NY46; baseline and differential.
DR   Genevisible; Q9NY46; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR   GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   InterPro; IPR024583; Na_trans_cytopl.
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   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Sodium;
KW   Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation; Voltage-gated channel.
FT   CHAIN         1   2000       Sodium channel protein type 3 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048493.
FT   TOPO_DOM      1    128       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    129    147       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    148    154       Extracellular. {ECO:0000305}.
FT   TRANSMEM    155    175       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    176    189       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    190    207       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    208    213       Extracellular. {ECO:0000305}.
FT   TRANSMEM    214    230       Helical; Name=S4 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    231    249       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    250    269       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    270    368       Extracellular. {ECO:0000305}.
FT   INTRAMEM    369    393       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    394    400       Extracellular. {ECO:0000305}.
FT   TRANSMEM    401    421       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    422    760       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    761    779       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    780    790       Extracellular. {ECO:0000305}.
FT   TRANSMEM    791    810       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    811    824       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    825    844       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    845    846       Extracellular. {ECO:0000305}.
FT   TRANSMEM    847    864       Helical; Name=S4 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    865    880       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    881    899       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    900    928       Extracellular. {ECO:0000305}.
FT   INTRAMEM    929    949       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    950    962       Extracellular. {ECO:0000305}.
FT   TRANSMEM    963    983       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    984   1207       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1208   1225       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1226   1238       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1239   1257       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1258   1271       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1272   1290       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1291   1298       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1299   1317       Helical; Name=S4 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1318   1334       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1335   1354       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1355   1403       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1404   1425       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1426   1442       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1443   1464       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1465   1527       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1528   1545       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1546   1556       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1557   1575       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1576   1587       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1588   1605       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1606   1618       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1619   1635       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1636   1654       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1655   1672       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1673   1694       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1695   1717       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1718   1747       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1748   1770       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1771   2000       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      110    455       I. {ECO:0000305}.
FT   REPEAT      742   1014       II. {ECO:0000305}.
FT   REPEAT     1188   1499       III. {ECO:0000305}.
FT   REPEAT     1508   1806       IV. {ECO:0000305}.
FT   DOMAIN     1900   1929       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   MOD_RES     484    484       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08104}.
FT   MOD_RES     485    485       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08104}.
FT   MOD_RES     486    486       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08104}.
FT   MOD_RES    1501   1501       Phosphoserine; by PKC. {ECO:0000250}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    290    290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    302    302       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    339    339       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1366   1366       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1380   1380       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    277    346       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    911    911       Interchain; with SCN2B or SCN4B.
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   DISULFID    911    911       Interchain; with the conotoxin GVIIJ
FT                                (when the channel is not linked to SCN2B
FT                                or SCN4B; the bond to SCN2B or SCN4B
FT                                protects the channel from the inhibition
FT                                by toxin).
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   DISULFID    951    960       {ECO:0000250|UniProtKB:D0E0C2}.
FT   VAR_SEQ     208    208       S -> D (in isoform 3 and isoform 4).
FT                                {ECO:0000303|PubMed:9589372,
FT                                ECO:0000303|Ref.2}.
FT                                /FTId=VSP_001033.
FT   VAR_SEQ     625    673       Missing (in isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:9589372,
FT                                ECO:0000303|Ref.1}.
FT                                /FTId=VSP_001034.
FT   VARIANT      43     43       Missing. {ECO:0000269|PubMed:12610651}.
FT                                /FTId=VAR_029743.
FT   VARIANT     606    606       S -> T. {ECO:0000269|PubMed:11245985}.
FT                                /FTId=VAR_014275.
FT   VARIANT    1084   1084       V -> I (in dbSNP:rs140990288).
FT                                {ECO:0000269|PubMed:26566883}.
FT                                /FTId=VAR_076435.
FT   VARIANT    1107   1107       V -> A (in dbSNP:rs12474273).
FT                                /FTId=VAR_029744.
FT   VARIANT    1803   1803       D -> N (in dbSNP:rs3731762).
FT                                /FTId=VAR_055640.
FT   VARIANT    1813   1813       L -> S. {ECO:0000269|PubMed:12610651}.
FT                                /FTId=VAR_029745.
FT   MUTAGEN    1970   1970       Y->A: Abolishes interaction with NEDD4L.
FT                                {ECO:0000269|PubMed:15548568}.
FT   CONFLICT    175    175       A -> V (in Ref. 4; AAC29514/AAC29515).
FT                                {ECO:0000305}.
FT   CONFLICT    318    318       Y -> N (in Ref. 4; AAC29514/AAC29515).
FT                                {ECO:0000305}.
FT   CONFLICT    401    401       M -> T (in Ref. 4; AAC29514/AAC29515).
FT                                {ECO:0000305}.
FT   CONFLICT    475    475       I -> V (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
FT   CONFLICT    495    495       S -> G (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
FT   CONFLICT    604    604       S -> G (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
FT   CONFLICT    613    613       V -> E (in Ref. 4; AAC29514/AAC29515).
FT                                {ECO:0000305}.
FT   CONFLICT   1060   1060       E -> A (in Ref. 4; AAC29514/AAC29515).
FT                                {ECO:0000305}.
FT   CONFLICT   1163   1163       L -> F (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
FT   CONFLICT   1274   1274       W -> R (in Ref. 4; AAC29514/AAC29515).
FT                                {ECO:0000305}.
FT   CONFLICT   1329   1329       V -> L (in Ref. 6; AAB30530).
FT                                {ECO:0000305}.
FT   CONFLICT   1414   1415       AT -> VS (in Ref. 4; AAC29514/AAC29515).
FT                                {ECO:0000305}.
FT   CONFLICT   1614   1614       F -> S (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
FT   CONFLICT   1741   1743       CGN -> RGD (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
FT   CONFLICT   1862   1862       G -> C (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
FT   CONFLICT   1966   1966       S -> P (in Ref. 2; AAK00219).
FT                                {ECO:0000305}.
SQ   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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