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Database: UniProt
Entry: SCN2A_RAT
LinkDB: SCN2A_RAT
Original site: SCN2A_RAT 
ID   SCN2A_RAT               Reviewed;        2005 AA.
AC   P04775;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   28-FEB-2018, entry version 155.
DE   RecName: Full=Sodium channel protein type 2 subunit alpha;
DE   AltName: Full=Sodium channel protein brain II subunit alpha;
DE   AltName: Full=Sodium channel protein type II subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.2;
GN   Name=Scn2a; Synonyms=Scn2a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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   PHOSPHORYLATION AT SER-1506, AND MUTAGENESIS OF SER-1506.
RX   PubMed=1658937; DOI=10.1126/science.1658937;
RA   West J.W., Numann R., Murphy B.J., Scheuer T., Catterall W.A.;
RT   "A phosphorylation site in the Na+ channel required for modulation by
RT   protein kinase C.";
RL   Science 254:866-868(1991).
RN   [3]
RP   PHOSPHORYLATION AT SER-554; SER-573; SER-576 AND SER-1506.
RX   PubMed=1322892;
RA   Murphy B.J., Catterall W.A.;
RT   "Phosphorylation of purified rat brain Na+ channel reconstituted into
RT   phospholipid vesicles by protein kinase C.";
RL   J. Biol. Chem. 267:16129-16134(1992).
RN   [4]
RP   INTERACTION WITH NEDD4L, POSSIBLE UBIQUITINATION, AND MUTAGENESIS OF
RP   TYR-1975.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1963, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [6]
RP   PHOSPHORYLATION AT SER-4; SER-468; SER-471; SER-484; SER-528; SER-554;
RP   SER-610; SER-623; SER-687; SER-688; SER-721; SER-1930; THR-1966 AND
RP   SER-1971.
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
RT   subunits from rat brain.";
RL   J. Proteome Res. 9:1976-1984(2010).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-526; SER-528;
RP   SER-531; SER-553; SER-554; SER-558; SER-589; SER-721 AND THR-1943, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BOND, AND
RP   INTERACTION WITH SCN4B.
RX   PubMed=24297919; DOI=10.1073/pnas.1314557110;
RA   Gilchrist J., Das S., Van Petegem F., Bosmans F.;
RT   "Crystallographic insights into sodium-channel modulation by the beta4
RT   subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:E5016-E5024(2013).
RN   [9]
RP   MUTAGENESIS OF CYS-910, INTERACTION WITH THE CONOTOXIN GVIIJ, AND
RP   DISULFIDE BOND.
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   [10]
RP   MUTAGENESIS OF PHE-385.
RX   PubMed=26039939; DOI=10.1021/acs.biochem.5b00390;
RA   Zhang M.M., Gajewiak J., Azam L., Bulaj G., Olivera B.M.,
RA   Yoshikami D.;
RT   "Probing the redox states of sodium channel cysteines at the binding
RT   site of muO[section sign]-conotoxin GVIIJ.";
RL   Biochemistry 54:3911-3920(2015).
RN   [11]
RP   STRUCTURE BY NMR OF 1474-1526, FUNCTION, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF PHE-1489.
RX   PubMed=9893979; DOI=10.1021/bi9823380;
RA   Rohl C.A., Boeckman F.A., Baker C., Scheuer T., Catterall W.A.,
RA   Klevit R.E.;
RT   "Solution structure of the sodium channel inactivation gate.";
RL   Biochemistry 38:855-861(1999).
RN   [12]
RP   STRUCTURE BY NMR OF 1901-1927 IN COMPLEX WITH CALM, AND INTERACTION
RP   WITH CALM.
RX   PubMed=21439835; DOI=10.1016/j.str.2011.02.009;
RA   Feldkamp M.D., Yu L., Shea M.A.;
RT   "Structural and energetic determinants of apo calmodulin binding to
RT   the IQ motif of the Na(V)1.2 voltage-dependent sodium channel.";
RL   Structure 19:733-747(2011).
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       {ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:9893979}.
CC   -!- SUBUNIT: Heterooligomer of a large alpha subunit and a smaller
CC       beta subunit. Heterooligomer with SCN2B or SCN4B; disulfide-
CC       linked. Interacts with NEDD4L. Interacts with CALM. Interacts with
CC       the conotoxin GVIIJ (PubMed:24497506).
CC       {ECO:0000269|PubMed:15548568, ECO:0000269|PubMed:21439835,
CC       ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:24497506}.
CC   -!- INTERACTION:
CC       P07463:CAM (xeno); NbExp=2; IntAct=EBI-2619448, EBI-15916571;
CC       P21707:Syt1; NbExp=2; IntAct=EBI-2619448, EBI-458098;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24297919,
CC       ECO:0000269|PubMed:9893979}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:9893979}.
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-1506 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and
CC       reduces peak sodium currents. {ECO:0000269|PubMed:1322892,
CC       ECO:0000269|PubMed:1658937, ECO:0000269|PubMed:20131913}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.2/SCN2A subfamily. {ECO:0000305}.
DR   EMBL; X03639; CAA27287.1; -; mRNA.
DR   RefSeq; NP_036779.1; NM_012647.1.
DR   UniGene; Rn.89192; -.
DR   PDB; 1BYY; NMR; -; A=1474-1526.
DR   PDB; 2KXW; NMR; -; B=1901-1927.
DR   PDB; 2M5E; NMR; -; B=1901-1927.
DR   PDBsum; 1BYY; -.
DR   PDBsum; 2KXW; -.
DR   PDBsum; 2M5E; -.
DR   ProteinModelPortal; P04775; -.
DR   SMR; P04775; -.
DR   BioGrid; 246890; 4.
DR   CORUM; P04775; -.
DR   DIP; DIP-57088N; -.
DR   IntAct; P04775; 2.
DR   STRING; 10116.ENSRNOP00000007069; -.
DR   BindingDB; P04775; -.
DR   ChEMBL; CHEMBL3399; -.
DR   GuidetoPHARMACOLOGY; 579; -.
DR   iPTMnet; P04775; -.
DR   PhosphoSitePlus; P04775; -.
DR   SwissPalm; P04775; -.
DR   PaxDb; P04775; -.
DR   PRIDE; P04775; -.
DR   GeneID; 24766; -.
DR   KEGG; rno:24766; -.
DR   UCSC; RGD:3632; rat.
DR   CTD; 6326; -.
DR   RGD; 3632; Scn2a.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   HOGENOM; HOG000231755; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; P04775; -.
DR   KO; K04834; -.
DR   PhylomeDB; P04775; -.
DR   EvolutionaryTrace; P04775; -.
DR   PRO; PR:P04775; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0043194; C:axon initial segment; IDA:RGD.
DR   GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR   GO; GO:0033270; C:paranode region of axon; ISO:RGD.
DR   GO; GO:0034706; C:sodium channel complex; IDA:UniProtKB.
DR   GO; GO:0030315; C:T-tubule; ISO:RGD.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
DR   GO; GO:0043522; F:leucine zipper domain binding; IPI:RGD.
DR   GO; GO:0031402; F:sodium ion binding; IDA:RGD.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:UniProtKB.
DR   GO; GO:0008627; P:intrinsic apoptotic signaling pathway in response to osmotic stress; ISO:RGD.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0042552; P:myelination; IEP:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; ISO:RGD.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR   Gene3D; 1.20.120.350; -; 4.
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   InterPro; IPR027359; Volt_channel_dom_sf.
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   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW   Voltage-gated channel.
FT   CHAIN         1   2005       Sodium channel protein type 2 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048492.
FT   TOPO_DOM      1    129       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    130    148       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    149    155       Extracellular. {ECO:0000305}.
FT   TRANSMEM    156    176       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    177    190       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    191    208       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    209    214       Extracellular. {ECO:0000305}.
FT   TRANSMEM    215    231       Helical; Name=S4 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    232    250       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    251    270       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    271    369       Extracellular. {ECO:0000305}.
FT   INTRAMEM    370    394       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    395    401       Extracellular. {ECO:0000305}.
FT   TRANSMEM    402    422       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    423    759       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    760    778       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    779    789       Extracellular. {ECO:0000305}.
FT   TRANSMEM    790    809       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    810    823       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    824    843       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    844    845       Extracellular. {ECO:0000305}.
FT   TRANSMEM    846    863       Helical; Name=S4 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    864    879       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    880    898       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    899    927       Extracellular. {ECO:0000305}.
FT   INTRAMEM    928    948       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    949    961       Extracellular. {ECO:0000305}.
FT   TRANSMEM    962    982       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    983   1209       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1210   1227       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1228   1240       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1241   1259       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1260   1273       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1274   1292       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1293   1300       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1301   1319       Helical; Name=S4 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1320   1336       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1337   1356       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1357   1408       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1409   1430       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1431   1447       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1448   1469       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1470   1532       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1533   1550       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1551   1561       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1562   1580       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1581   1592       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1593   1610       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1611   1623       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1624   1640       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1641   1659       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1660   1677       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1678   1699       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1700   1722       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1723   1752       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1753   1775       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1776   2005       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      111    456       I. {ECO:0000305}.
FT   REPEAT      741   1013       II. {ECO:0000305}.
FT   REPEAT     1190   1504       III. {ECO:0000305}.
FT   REPEAT     1513   1811       IV. {ECO:0000305}.
FT   DOMAIN     1905   1934       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   SITE       1489   1489       Important for channel closure.
FT   MOD_RES       4      4       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES     468    468       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES     471    471       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES     484    484       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903,
FT                                ECO:0000269|PubMed:20131913}.
FT   MOD_RES     526    526       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     528    528       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903,
FT                                ECO:0000269|PubMed:20131913}.
FT   MOD_RES     531    531       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     553    553       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     554    554       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903,
FT                                ECO:0000269|PubMed:1322892,
FT                                ECO:0000269|PubMed:20131913}.
FT   MOD_RES     554    554       Phosphoserine; by PKC; in vitro.
FT                                {ECO:0000244|PubMed:22673903,
FT                                ECO:0000269|PubMed:1322892,
FT                                ECO:0000269|PubMed:20131913}.
FT   MOD_RES     558    558       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     573    573       Phosphoserine; by PKC; in vitro.
FT                                {ECO:0000269|PubMed:1322892}.
FT   MOD_RES     576    576       Phosphoserine; by PKC; in vitro.
FT                                {ECO:0000269|PubMed:1322892}.
FT   MOD_RES     589    589       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     610    610       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES     623    623       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES     687    687       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES     688    688       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES     721    721       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903,
FT                                ECO:0000269|PubMed:20131913}.
FT   MOD_RES    1506   1506       Phosphoserine; by PKC.
FT                                {ECO:0000269|PubMed:1322892,
FT                                ECO:0000269|PubMed:1658937}.
FT   MOD_RES    1930   1930       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES    1943   1943       Phosphothreonine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1963   1963       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16641100}.
FT   MOD_RES    1966   1966       Phosphothreonine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   MOD_RES    1971   1971       Phosphoserine.
FT                                {ECO:0000269|PubMed:20131913}.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    285    285       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    291    291       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    297    297       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    303    303       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    340    340       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1368   1368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1382   1382       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1393   1393       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    278    347       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    910    910       Interchain; with SCN2B or SCN4B.
FT                                {ECO:0000305|PubMed:24497506}.
FT   DISULFID    910    910       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). {ECO:0000269|PubMed:24497506}.
FT   DISULFID    950    959       {ECO:0000250|UniProtKB:D0E0C2}.
FT   MUTAGEN     385    385       F->C: Sodium current is irreversibly
FT                                blocked by methanethiosulfonate (MTSET);
FT                                the mutated Cys residue has a free thiol
FT                                susceptible to reaction with MTSET, and
FT                                inhibition of current is due to the fact
FT                                that the residue is close to the
FT                                selectivity filter.
FT                                {ECO:0000250|UniProtKB:P15389,
FT                                ECO:0000269|PubMed:26039939}.
FT   MUTAGEN     910    910       C->L: >1000-fold reduction of sensitivity
FT                                to the conotoxin GVIIJ(SSG).
FT                                {ECO:0000269|PubMed:24497506}.
FT   MUTAGEN    1489   1489       F->Q: Strongly impairs channel
FT                                inactivation.
FT                                {ECO:0000269|PubMed:9893979}.
FT   MUTAGEN    1506   1506       S->A: Blocks the reduction of Na+ current
FT                                and the slowing of inactivation caused by
FT                                PKC. {ECO:0000269|PubMed:1658937}.
FT   MUTAGEN    1975   1975       Y->A: Abolishes interaction with NEDD4L.
FT                                {ECO:0000269|PubMed:15548568}.
FT   HELIX      1492   1502       {ECO:0000244|PDB:1BYY}.
FT   HELIX      1904   1922       {ECO:0000244|PDB:2KXW}.
SQ   SEQUENCE   2005 AA;  227874 MW;  861BE583D79F8324 CRC64;
     MARSVLVPPG PDSFRFFTRE SLAAIEQRIA EEKAKRPKQE RKDEDDENGP KPNSDLEAGK
     SLPFIYGDIP PEMVSEPLED LDPYYINKKT FIVLNKGKAI SRFSATSALY ILTPFNPIRK
     LAIKILVHSL FNVLIMCTIL TNCVFMTMSN PPDWTKNVEY TFTGIYTFES LIKILARGFC
     LEDFTFLRNP WNWLDFTVIT FAYVTEFVNL GNVSALRTFR VLRALKTISV IPGLKTIVGA
     LIQSVKKLSD VMILTVFCLS VFALIGLQLF MGNLRNKCLQ WPPDNSTFEI NITSFFNNSL
     DWNGTAFNRT VNMFNWDEYI EDKSHFYFLE GQNDALLCGN SSDAGQCPEG YICVKAGRNP
     NYGYTSFDTF SWAFLSLFRL MTQDFWENLY QLTLRAAGKT YMIFFVLVIF LGSFYLINLI
     LAVVAMAYEE QNQATLEEAE QKEAEFQQML EQLKKQQEEA QAAAAAASAE SRDFSGAGGI
     GVFSESSSVA SKLSSKSEKE LKNRRKKKKQ KEQAGEEEKE DAVRKSASED SIRKKGFQFS
     LEGSRLTYEK RFSSPHQSLL SIRGSLFSPR RNSRASLFNF KGRVKDIGSE NDFADDEHST
     FEDNDSRRDS LFVPHRHGER RPSNVSQASR ASRGIPTLPM NGKMHSAVDC NGVVSLVGGP
     SALTSPVGQL LPEGTTTETE IRKRRSSSYH VSMDLLEDPS RQRAMSMASI LTNTMEELEE
     SRQKCPPCWY KFANMCLIWD CCKPWLKVKH VVNLVVMDPF VDLAITICIV LNTLFMAMEH
     YPMTEQFSSV LSVGNLVFTG IFTAEMFLKI IAMDPYYYFQ EGWNIFDGFI VSLSLMELGL
     ANVEGLSVLR SFRLLRVFKL AKSWPTLNML IKIIGNSVGA LGNLTLVLAI IVFIFAVVGM
     QLFGKSYKEC VCKISNDCEL PRWHMHHFFH SFLIVFRVLC GEWIETMWDC MEVAGQTMCL
     TVFMMVMVIG NLVVLNLFLA LLLSSFSSDN LAATDDDNEM NNLQIAVGRM QKGIDFVKRK
     IREFIQKAFV RKQKALDEIK PLEDLNNKKD SCISNHTTIE IGKDLNYLKD GNGTTSGIGS
     SVEKYVVDES DYMSFINNPS LTVTVPIALG ESDFENLNTE EFSSESDMEE SKEKLNATSS
     SEGSTVDIGA PAEGEQPEAE PEESLEPEAC FTEDCVRKFK CCQISIEEGK GKLWWNLRKT
     CYKIVEHNWF ETFIVFMILL SSGALAFEDI YIEQRKTIKT MLEYADKVFT YIFILEMLLK
     WVAYGFQMYF TNAWCWLDFL IVDVSLVSLT ANALGYSELG AIKSLRTLRA LRPLRALSRF
     EGMRVVVNAL LGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCINYT TGEMFDVSVV
     NNYSECQALI ESNQTARWKN VKVNFDNVGL GYLSLLQVAT FKGWMDIMYA AVDSRNVELQ
     PKYEDNLYMY LYFVIFIIFG SFFTLNLFIG VIIDNFNQQK KKFGGQDIFM TEEQKKYYNA
     MKKLGSKKPQ KPIPRPANKF QGMVFDFVTK QVFDISIMIL ICLNMVTMMV ETDDQSQEMT
     NILYWINLVF IVLFTGECVL KLISLRHYYF TIGWNIFDFV VVILSIVGMF LAELIEKYFV
     SPTLFRVIRL ARIGRILRLI KGAKGIRTLL FALMMSLPAL FNIGLLLFLV MFIYAIFGMS
     NFAYVKREVG IDDMFNFETF GNSMICLFQI TTSAGWDGLL APILNSGPPD CDPEKDHPGS
     SVKGDCGNPS VGIFFFVSYI IISFLVVVNM YIAVILENFS VATEESAEPL SEDDFEMFYE
     VWEKFDPDAT QFIEFCKLSD FAAALDPPLL IAKPNKVQLI AMDLPMVSGD RIHCLDILFA
     FTKRVLGESG EMDALRIQME ERFMASNPSK VSYEPITTTL KRKQEEVSAI VIQRAYRRYL
     LKQKVKKVSS IYKKDKGKED EGTPIKEDII TDKLNENSTP EKTDVTPSTT SPPSYDSVTK
     PEKEKFEKDK SEKEDKGKDI RESKK
//
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