ID   SCN1A_RAT               Reviewed;        2009 AA.
AC   P04774;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   24-JAN-2024, entry version 179.
DE   RecName: Full=Sodium channel protein type 1 subunit alpha;
DE   AltName: Full=Sodium channel protein brain I subunit alpha;
DE   AltName: Full=Sodium channel protein type I subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.1;
GN   Name=Scn1a {ECO:0000312|RGD:69364};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3754035; DOI=10.1038/320188a0;
RA   Noda M., Ikeda T., Kayano T., Suzuki H., Takeshima H., Kurasaki M.,
RA   Takahashi H., Numa S.;
RT   "Existence of distinct sodium channel messenger RNAs in rat brain.";
RL   Nature 320:188-192(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2442385; DOI=10.3109/10799898709054998;
RA   Noda M., Numa S.;
RT   "Structure and function of sodium channel.";
RL   J. Recept. Res. 7:467-497(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 177-253.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=1658739; DOI=10.1093/nar/19.20.5673;
RA   Sarao R., Gupta S.K., Auld V.J., Dunn R.J.;
RT   "Developmentally regulated alternative RNA splicing of rat brain sodium
RT   channel mRNAs.";
RL   Nucleic Acids Res. 19:5673-5679(1991).
RN   [4]
RP   PHOSPHORYLATION AT SER-470; SER-551 AND SER-607.
RX   PubMed=20131913; DOI=10.1021/pr901171q;
RA   Berendt F.J., Park K.S., Trimmer J.S.;
RT   "Multisite phosphorylation of voltage-gated sodium channel alpha subunits
RT   from rat brain.";
RL   J. Proteome Res. 9:1976-1984(2010).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-525; SER-550;
RP   SER-551 AND SER-730, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [6]
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., Wickenden A.D.,
RA   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).
CC   -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC       excitable membranes. Assuming opened or closed conformations in
CC       response to the voltage difference across the membrane, the protein
CC       forms a sodium-selective channel through which Na(+) ions may pass in
CC       accordance with their electrochemical gradient. Plays a key role in
CC       brain, probably by regulating the moment when neurotransmitters are
CC       released in neurons. Involved in sensory perception of mechanical pain:
CC       activation in somatosensory neurons induces pain without neurogenic
CC       inflammation and produces hypersensitivity to mechanical, but not
CC       thermal stimuli. {ECO:0000250|UniProtKB:A2APX8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P35498};
CC   -!- ACTIVITY REGULATION: Inactivation of this channel is specifically
CC       inhibited by the spider toxins Hm1a and Hm1b (H.maculata, AC P60992 and
CC       AC P0DOC5) in somatosensory neurons to elicit acute pain and mechanical
CC       allodynia. {ECO:0000250|UniProtKB:A2APX8}.
CC   -!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
CC       conducting pore forming alpha-subunit regulated by one or more beta-1
CC       (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4 (SCN4B). Beta-1
CC       (SCN1B) and beta-3 (SCN3B) are non-covalently associated with alpha,
CC       while beta-2 (SCN2B) and beta-4 (SCN4B) are covalently linked by
CC       disulfide bonds. Interacts with FGF13. Interacts with TMEM233 (By
CC       similarity). Interacts with the conotoxin GVIIJ (PubMed:24497506).
CC       {ECO:0000250|UniProtKB:P04775, ECO:0000250|UniProtKB:P35498,
CC       ECO:0000269|PubMed:24497506}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35498};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC       segment (S4). Segments S4 are probably the voltage-sensors and are
CC       characterized by a series of positively charged amino acids at every
CC       third position. {ECO:0000305}.
CC   -!- DOMAIN: The S3b-S4 and S1-S2 loops of repeat IV are targeted by
CC       H.maculata toxins Hm1a and Hm1b, leading to inhibit fast inactivation
CC       of Nav1.1/SCN1A. Selectivity for H.maculata toxins Hm1a and Hm1b
CC       depends on S1-S2 loops of repeat IV. {ECO:0000250|UniProtKB:A2APX8}.
CC   -!- PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and reduces
CC       peak sodium currents. {ECO:0000250|UniProtKB:P04775}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.1/SCN1A subfamily. {ECO:0000305}.
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DR   EMBL; X03638; CAA27286.1; -; mRNA.
DR   EMBL; M22253; AAA79965.1; -; mRNA.
DR   PIR; A25019; A25019.
DR   RefSeq; NP_110502.1; NM_030875.1.
DR   AlphaFoldDB; P04774; -.
DR   BMRB; P04774; -.
DR   SMR; P04774; -.
DR   BioGRID; 249530; 3.
DR   CORUM; P04774; -.
DR   STRING; 10116.ENSRNOP00000073986; -.
DR   BindingDB; P04774; -.
DR   ChEMBL; CHEMBL4906; -.
DR   DrugCentral; P04774; -.
DR   GuidetoPHARMACOLOGY; 578; -.
DR   GlyCosmos; P04774; 9 sites, No reported glycans.
DR   GlyGen; P04774; 9 sites.
DR   iPTMnet; P04774; -.
DR   PhosphoSitePlus; P04774; -.
DR   SwissPalm; P04774; -.
DR   PaxDb; 10116-ENSRNOP00000008026; -.
DR   ABCD; P04774; 3 sequenced antibodies.
DR   GeneID; 81574; -.
DR   KEGG; rno:81574; -.
DR   UCSC; RGD:69364; rat.
DR   AGR; RGD:69364; -.
DR   CTD; 6323; -.
DR   RGD; 69364; Scn1a.
DR   eggNOG; KOG2301; Eukaryota.
DR   InParanoid; P04774; -.
DR   OrthoDB; 1110761at2759; -.
DR   PhylomeDB; P04774; -.
DR   PRO; PR:P04774; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR   GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR   GO; GO:0033268; C:node of Ranvier; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0034706; C:sodium channel complex; ISO:RGD.
DR   GO; GO:0030315; C:T-tubule; ISO:RGD.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
DR   GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR   GO; GO:0031402; F:sodium ion binding; IDA:RGD.
DR   GO; GO:0099508; F:voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR   GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISS:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR   GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
DR   GO; GO:0086010; P:membrane depolarization during action potential; ISS:UniProtKB.
DR   GO; GO:0021675; P:nerve development; ISO:RGD.
DR   GO; GO:0050884; P:neuromuscular process controlling posture; ISO:RGD.
DR   GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR   GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR   GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR   CDD; cd13433; Na_channel_gate; 1.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR008051; Na_channel_a1su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR044564; Na_chnl_inactivation_gate.
DR   InterPro; IPR010526; Na_trans_assoc_dom.
DR   InterPro; IPR024583; Na_trans_cytopl.
DR   InterPro; IPR043203; VGCC_Ca_Na.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF280; SODIUM CHANNEL PROTEIN TYPE 1 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   Pfam; PF11933; Na_trans_cytopl; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   PRINTS; PR01664; NACHANNEL1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Sodium;
KW   Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN           1..2009
FT                   /note="Sodium channel protein type 1 subunit alpha"
FT                   /id="PRO_0000048490"
FT   TOPO_DOM        1..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        129..147
FT                   /note="Helical; Name=S1 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        148..154
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        155..175
FT                   /note="Helical; Name=S2 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        176..189
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        190..207
FT                   /note="Helical; Name=S3 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        208..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        214..230
FT                   /note="Helical; Name=S4 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        231..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        250..269
FT                   /note="Helical; Name=S5 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        270..367
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        368..392
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        393..399
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        400..420
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        421..768
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        769..787
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        788..798
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        799..818
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        819..832
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        833..852
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        853..854
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        855..872
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        873..888
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        889..907
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        908..936
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        937..957
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        958..970
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        971..991
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        992..1219
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1220..1237
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1238..1250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1251..1269
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1270..1283
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1284..1302
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1303..1310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1311..1329
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1330..1346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1347..1366
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1367..1418
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1419..1440
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1441..1457
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1458..1479
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1480..1542
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1543..1560
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1561..1571
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1572..1590
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1591..1602
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1603..1620
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1621..1633
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1634..1650
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1651..1669
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1670..1687
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1688..1709
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1710..1732
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1733..1762
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1763..1785
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1786..2009
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REPEAT          110..454
FT                   /note="I"
FT                   /evidence="ECO:0000305"
FT   REPEAT          750..1022
FT                   /note="II"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1200..1514
FT                   /note="III"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1523..1821
FT                   /note="IV"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1915..1944
FT                   /note="IQ"
FT   REGION          28..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1129..1163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1561..1571
FT                   /note="S1-S2 loop of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:A2APX8"
FT   REGION          1619..1636
FT                   /note="S3b-S4 loop of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:A2APX8"
FT   REGION          1986..2009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1990..2009
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:20131913"
FT   MOD_RES         523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:20131913,
FT                   ECO:0007744|PubMed:22673903"
FT   MOD_RES         607
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:20131913"
FT   MOD_RES         730
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1516
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P04775"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        277..345
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   DISULFID        919
FT                   /note="Interchain; with SCN2B or SCN4B"
FT                   /evidence="ECO:0000250|UniProtKB:P04775"
FT   DISULFID        919
FT                   /note="Interchain; with the conotoxin GVIIJ (when the
FT                   channel is not linked to SCN2B or SCN4B; the bond to SCN2B
FT                   or SCN4B protects the channel from the inhibition by
FT                   toxin)"
FT                   /evidence="ECO:0000250|UniProtKB:P04775"
FT   DISULFID        959..968
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
SQ   SEQUENCE   2009 AA;  228770 MW;  6808466F6368373B 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 SIEKNVTTDY
     NGTLVNETVF EFDWKSYIQD SRYHYFLEGV LDALLCGNSS DAGQCPEGYM CVKAGRNPNY
     GYTSFDTFSW AFLSLFRLMT QDFWENLYQL TLRAAGKTYM IFFVLVIFLG SFYLINLILA
     VVAMAYEEQN QATLEEAEQK EAEFQQMLEQ LKKQQEAAQQ AAAATASEHS REPSAAGRLS
     DSSSEASKLS SKSAKERRNR RKKRKQKEQS GGEEKDDDEF HKSESEDSIR RKGFRFSIEG
     NRLTYEKRYS SPHQSLLSIR GSLFSPRRNS RTSLFSFRGR AKDVGSENDF ADDEHSTFED
     NESRRDSLFV PRRHGERRNS NLSQTSRSSR MLAGLPANGK 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 VFMMVMVIRN LVVLNLFLAL LLSSFSADNL AATDDDNEMN NLQIAVDRMH
     KGVAYVKRKI YEFIQQSFVR KQKILDEIKP LDDLNNRKDN CTSNHTTEIG KDLDCLKDVN
     GTTSGIGTGS SVEKYIIDES DYMSFINNPS LTVTVPIAVG ESDFENLNTE DFSSESDLEE
     SKEKLNESSS SSEGSTVDIG APAEEQPVME PEETLEPEAC FTEGCVQRFK CCQISVEEGR
     GKQWWNLRRT CFRIVEHNWF ETFIVFMILL SSGALAFEDI YIDQRKTIKT MLEYADKVFT
     YIFILEMLLK WVAYGYQTYF TNAWCWLDFL IVDVSLVSLT ANALGYSELG AIKSLRTLRA
     LRPLRALSRF EGMRVVVNAL LGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCVNTT
     TGDTFEITEV 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 ANLLVKEDMI IDRINENSIT EKTDLTMSTA
     ACPPSYDRVT KPIVEKHEQE GKDEKAKGK
//