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Sodium channel protein type 2 subunit alpha (Sodium channel protein brain II subunit alpha) (Sodium channel protein type II subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.2)

 SCN2A_RAT               Reviewed;        2005 AA.
P04775;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
20-JUN-2018, entry version 157.
RecName: Full=Sodium channel protein type 2 subunit alpha;
AltName: Full=Sodium channel protein brain II subunit alpha;
AltName: Full=Sodium channel protein type II subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.2;
Name=Scn2a; Synonyms=Scn2a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3754035; DOI=10.1038/320188a0;
Noda M., Ikeda T., Kayano T., Suzuki H., Takeshima H., Kurasaki M.,
Takahashi H., Numa S.;
"Existence of distinct sodium channel messenger RNAs in rat brain.";
Nature 320:188-192(1986).
[2]
PHOSPHORYLATION AT SER-1506, AND MUTAGENESIS OF SER-1506.
PubMed=1658937; DOI=10.1126/science.1658937;
West J.W., Numann R., Murphy B.J., Scheuer T., Catterall W.A.;
"A phosphorylation site in the Na+ channel required for modulation by
protein kinase C.";
Science 254:866-868(1991).
[3]
PHOSPHORYLATION AT SER-554; SER-573; SER-576 AND SER-1506.
PubMed=1322892;
Murphy B.J., Catterall W.A.;
"Phosphorylation of purified rat brain Na+ channel reconstituted into
phospholipid vesicles by protein kinase C.";
J. Biol. Chem. 267:16129-16134(1992).
[4]
INTERACTION WITH NEDD4L, POSSIBLE UBIQUITINATION, AND MUTAGENESIS OF
TYR-1975.
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1963, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[6]
PHOSPHORYLATION AT SER-4; SER-468; SER-471; SER-484; SER-528; SER-554;
SER-610; SER-623; SER-687; SER-688; SER-721; SER-1930; THR-1966 AND
SER-1971.
PubMed=20131913; DOI=10.1021/pr901171q;
Berendt F.J., Park K.S., Trimmer J.S.;
"Multisite phosphorylation of voltage-gated sodium channel alpha
subunits from rat brain.";
J. Proteome Res. 9:1976-1984(2010).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-526; SER-528;
SER-531; SER-553; SER-554; SER-558; SER-589; SER-721 AND THR-1943, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[8]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BOND, AND
INTERACTION WITH SCN4B.
PubMed=24297919; DOI=10.1073/pnas.1314557110;
Gilchrist J., Das S., Van Petegem F., Bosmans F.;
"Crystallographic insights into sodium-channel modulation by the beta4
subunit.";
Proc. Natl. Acad. Sci. U.S.A. 110:E5016-E5024(2013).
[9]
MUTAGENESIS OF CYS-910, INTERACTION WITH THE CONOTOXIN GVIIJ, AND
DISULFIDE BOND.
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).
[10]
MUTAGENESIS OF PHE-385.
PubMed=26039939; DOI=10.1021/acs.biochem.5b00390;
Zhang M.M., Gajewiak J., Azam L., Bulaj G., Olivera B.M.,
Yoshikami D.;
"Probing the redox states of sodium channel cysteines at the binding
site of muO[section sign]-conotoxin GVIIJ.";
Biochemistry 54:3911-3920(2015).
[11]
STRUCTURE BY NMR OF 1474-1526, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF PHE-1489.
PubMed=9893979; DOI=10.1021/bi9823380;
Rohl C.A., Boeckman F.A., Baker C., Scheuer T., Catterall W.A.,
Klevit R.E.;
"Solution structure of the sodium channel inactivation gate.";
Biochemistry 38:855-861(1999).
[12]
STRUCTURE BY NMR OF 1901-1927 IN COMPLEX WITH CALM, AND INTERACTION
WITH CALM.
PubMed=21439835; DOI=10.1016/j.str.2011.02.009;
Feldkamp M.D., Yu L., Shea M.A.;
"Structural and energetic determinants of apo calmodulin binding to
the IQ motif of the Na(V)1.2 voltage-dependent sodium channel.";
Structure 19:733-747(2011).
-!- 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.
{ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:9893979}.
-!- SUBUNIT: Heterooligomer of a large alpha subunit and a smaller
beta subunit. Heterooligomer with SCN2B or SCN4B; disulfide-
linked. Interacts with NEDD4L. Interacts with CALM. Interacts with
the conotoxin GVIIJ (PubMed:24497506).
{ECO:0000269|PubMed:15548568, ECO:0000269|PubMed:21439835,
ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:24497506}.
-!- INTERACTION:
P07463:CAM (xeno); NbExp=2; IntAct=EBI-2619448, EBI-15916571;
P21707:Syt1; NbExp=2; IntAct=EBI-2619448, EBI-458098;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24297919,
ECO:0000269|PubMed:9893979}; Multi-pass membrane protein
{ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:9893979}.
-!- 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-1506 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000269|PubMed:1322892,
ECO:0000269|PubMed:1658937, ECO:0000269|PubMed:20131913}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.2/SCN2A subfamily. {ECO:0000305}.
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EMBL; X03639; CAA27287.1; -; mRNA.
RefSeq; NP_036779.1; NM_012647.1.
UniGene; Rn.89192; -.
PDB; 1BYY; NMR; -; A=1474-1526.
PDB; 2KXW; NMR; -; B=1901-1927.
PDB; 2M5E; NMR; -; B=1901-1927.
PDBsum; 1BYY; -.
PDBsum; 2KXW; -.
PDBsum; 2M5E; -.
ProteinModelPortal; P04775; -.
SMR; P04775; -.
BioGrid; 246890; 4.
CORUM; P04775; -.
DIP; DIP-57088N; -.
IntAct; P04775; 2.
STRING; 10116.ENSRNOP00000007069; -.
BindingDB; P04775; -.
ChEMBL; CHEMBL3399; -.
GuidetoPHARMACOLOGY; 579; -.
iPTMnet; P04775; -.
PhosphoSitePlus; P04775; -.
SwissPalm; P04775; -.
PaxDb; P04775; -.
PRIDE; P04775; -.
GeneID; 24766; -.
KEGG; rno:24766; -.
UCSC; RGD:3632; rat.
CTD; 6326; -.
RGD; 3632; Scn2a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG053100; -.
InParanoid; P04775; -.
KO; K04834; -.
PhylomeDB; P04775; -.
EvolutionaryTrace; P04775; -.
PRO; PR:P04775; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043194; C:axon initial segment; IDA:RGD.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
GO; GO:0034706; C:sodium channel complex; IDA:UniProtKB.
GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
GO; GO:0043522; F:leucine zipper domain binding; IPI:RGD.
GO; GO:0031402; F:sodium ion binding; IDA:RGD.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:UniProtKB.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0042552; P:myelination; IEP:BHF-UCL.
GO; GO:0019228; P:neuronal action potential; IDA:RGD.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006814; P:sodium ion transport; IDA:RGD.
Gene3D; 1.20.120.350; -; 4.
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.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
SMART; SM00015; IQ; 1.
PROSITE; PS50096; IQ; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 2005 Sodium channel protein type 2 subunit
alpha.
/FTId=PRO_0000048492.
TOPO_DOM 1 129 Cytoplasmic. {ECO:0000305}.
TRANSMEM 130 148 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 149 155 Extracellular. {ECO:0000305}.
TRANSMEM 156 176 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 177 190 Cytoplasmic. {ECO:0000305}.
TRANSMEM 191 208 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 209 214 Extracellular. {ECO:0000305}.
TRANSMEM 215 231 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 232 250 Cytoplasmic. {ECO:0000305}.
TRANSMEM 251 270 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 271 369 Extracellular. {ECO:0000305}.
INTRAMEM 370 394 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 395 401 Extracellular. {ECO:0000305}.
TRANSMEM 402 422 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 423 759 Cytoplasmic. {ECO:0000305}.
TRANSMEM 760 778 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 779 789 Extracellular. {ECO:0000305}.
TRANSMEM 790 809 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 810 823 Cytoplasmic. {ECO:0000305}.
TRANSMEM 824 843 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 844 845 Extracellular. {ECO:0000305}.
TRANSMEM 846 863 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 864 879 Cytoplasmic. {ECO:0000305}.
TRANSMEM 880 898 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 899 927 Extracellular. {ECO:0000305}.
INTRAMEM 928 948 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 949 961 Extracellular. {ECO:0000305}.
TRANSMEM 962 982 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 983 1209 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1210 1227 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1228 1240 Extracellular. {ECO:0000305}.
TRANSMEM 1241 1259 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1260 1273 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1274 1292 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1293 1300 Extracellular. {ECO:0000305}.
TRANSMEM 1301 1319 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1320 1336 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1337 1356 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1357 1408 Extracellular. {ECO:0000305}.
INTRAMEM 1409 1430 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1431 1447 Extracellular. {ECO:0000305}.
TRANSMEM 1448 1469 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1470 1532 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1533 1550 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1551 1561 Extracellular. {ECO:0000305}.
TRANSMEM 1562 1580 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1581 1592 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1593 1610 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1611 1623 Extracellular. {ECO:0000305}.
TRANSMEM 1624 1640 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1641 1659 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1660 1677 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1678 1699 Extracellular. {ECO:0000305}.
INTRAMEM 1700 1722 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1723 1752 Extracellular. {ECO:0000305}.
TRANSMEM 1753 1775 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1776 2005 Cytoplasmic. {ECO:0000305}.
REPEAT 111 456 I. {ECO:0000305}.
REPEAT 741 1013 II. {ECO:0000305}.
REPEAT 1190 1504 III. {ECO:0000305}.
REPEAT 1513 1811 IV. {ECO:0000305}.
DOMAIN 1905 1934 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
SITE 1489 1489 Important for channel closure.
MOD_RES 4 4 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:20131913}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:20131913}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 553 553 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1322892,
ECO:0000269|PubMed:20131913}.
MOD_RES 554 554 Phosphoserine; by PKC; in vitro.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1322892,
ECO:0000269|PubMed:20131913}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 573 573 Phosphoserine; by PKC; in vitro.
{ECO:0000269|PubMed:1322892}.
MOD_RES 576 576 Phosphoserine; by PKC; in vitro.
{ECO:0000269|PubMed:1322892}.
MOD_RES 589 589 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 721 721 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:20131913}.
MOD_RES 1506 1506 Phosphoserine; by PKC.
{ECO:0000269|PubMed:1322892,
ECO:0000269|PubMed:1658937}.
MOD_RES 1930 1930 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 1943 1943 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1963 1963 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 1966 1966 Phosphothreonine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 1971 1971 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1368 1368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1382 1382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1393 1393 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 278 347 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 910 910 Interchain; with SCN2B or SCN4B.
{ECO:0000305|PubMed:24497506}.
DISULFID 910 910 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:0000269|PubMed:24497506}.
DISULFID 950 959 {ECO:0000250|UniProtKB:D0E0C2}.
MUTAGEN 385 385 F->C: Sodium current is irreversibly
blocked by methanethiosulfonate (MTSET);
the mutated Cys residue has a free thiol
susceptible to reaction with MTSET, and
inhibition of current is due to the fact
that the residue is close to the
selectivity filter.
{ECO:0000250|UniProtKB:P15389,
ECO:0000269|PubMed:26039939}.
MUTAGEN 910 910 C->L: >1000-fold reduction of sensitivity
to the conotoxin GVIIJ(SSG).
{ECO:0000269|PubMed:24497506}.
MUTAGEN 1489 1489 F->Q: Strongly impairs channel
inactivation.
{ECO:0000269|PubMed:9893979}.
MUTAGEN 1506 1506 S->A: Blocks the reduction of Na+ current
and the slowing of inactivation caused by
PKC. {ECO:0000269|PubMed:1658937}.
MUTAGEN 1975 1975 Y->A: Abolishes interaction with NEDD4L.
{ECO:0000269|PubMed:15548568}.
HELIX 1492 1502 {ECO:0000244|PDB:1BYY}.
HELIX 1904 1922 {ECO:0000244|PDB:2KXW}.
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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