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Sodium channel protein type 8 subunit alpha (Peripheral nerve protein type 4) (PN4) (Sodium channel 6) (NaCh6) (Sodium channel protein type VIII subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.6)

 SCN8A_RAT               Reviewed;        1978 AA.
O88420; O88421;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
07-NOV-2018, entry version 124.
RecName: Full=Sodium channel protein type 8 subunit alpha;
AltName: Full=Peripheral nerve protein type 4;
Short=PN4;
AltName: Full=Sodium channel 6;
Short=NaCh6;
AltName: Full=Sodium channel protein type VIII subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.6;
Name=Scn8a;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Spinal ganglion;
PubMed=9603190;
Dietrich P.S., McGivern J.G., Delgado S.G., Koch B.D., Eglen R.M.,
Hunter J.C., Sangameswaran L.;
"Functional analysis of a voltage-gated sodium channel and its splice
variant from rat dorsal root ganglia.";
J. Neurochem. 70:2262-2272(1998).
[2]
INTERACTION WITH FGF13.
PubMed=15282281; DOI=10.1523/JNEUROSCI.1628-04.2004;
Wittmack E.K., Rush A.M., Craner M.J., Goldfarb M., Waxman S.G.,
Dib-Hajj S.D.;
"Fibroblast growth factor homologous factor 2B: association with
Nav1.6 and selective colocalization at nodes of Ranvier of dorsal root
axons.";
J. Neurosci. 24:6765-6775(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-520, 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).
[4]
INTERACTION WITH THE CONOTOXIN GVIIJ.
PubMed=24497506; DOI=10.1073/pnas.1324189111;
Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
"A disulfide tether stabilizes the block of sodium channels by the
conotoxin muO[section sign]-GVIIJ.";
Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
-!- 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:9603190}.
-!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
conducting pore forming alpha-subunit regulated by one or more
beta-1 (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4
(SCN4B). Beta-1 (SCN1B) and beta-3 (SCN3B) are non-covalently
associated with alpha, while beta-2 (SCN2B) and beta-4 (SCN4B) are
covalently linked by disulfide bonds. Interacts with NEDD4 and
NEDD4L (By similarity). Interacts with FGF13 (PubMed:15282281).
Interacts with FGF14, GBG3, GBB2 and SCN1B (By similarity).
Interacts with the conotoxin GVIIJ (PubMed:24497506).
{ECO:0000250|UniProtKB:Q9UQD0, ECO:0000250|UniProtKB:Q9WTU3,
ECO:0000269|PubMed:15282281, ECO:0000269|PubMed:24497506}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9603190};
Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PN4;
IsoId=O88420-1; Sequence=Displayed;
Name=2; Synonyms=PN4a;
IsoId=O88420-2; Sequence=VSP_038652;
Note=May be due to competing donor splice site.;
-!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in brain,
moderately in spinal cord, and at low levels in dorsal root
ganglia, nodose ganglia and superior cervical ganglia. Not
detected in sciatic nerve and non-neuronal tissues. Isoform 2 is
hardly detectable, if at all, in brain, expressed at low levels in
spinal cord and at highest levels in dorsal root ganglia.
{ECO:0000269|PubMed:9603190}.
-!- 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. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-1495 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.6/SCN8A subfamily. {ECO:0000305}.
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EMBL; AF049239; AAC26014.1; -; mRNA.
EMBL; AF049240; AAC26015.1; -; mRNA.
RefSeq; NP_062139.2; NM_019266.2. [O88420-1]
UniGene; Rn.91216; -.
ProteinModelPortal; O88420; -.
SMR; O88420; -.
BioGrid; 248327; 1.
STRING; 10116.ENSRNOP00000008160; -.
BindingDB; O88420; -.
ChEMBL; CHEMBL2752; -.
GuidetoPHARMACOLOGY; 583; -.
CarbonylDB; O88420; -.
iPTMnet; O88420; -.
PhosphoSitePlus; O88420; -.
PaxDb; O88420; -.
PRIDE; O88420; -.
GeneID; 29710; -.
KEGG; rno:29710; -.
UCSC; RGD:3638; rat. [O88420-1]
CTD; 6334; -.
RGD; 3638; Scn8a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG053100; -.
InParanoid; O88420; -.
KO; K04840; -.
PhylomeDB; O88420; -.
PRO; PR:O88420; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0016021; C:integral component of membrane; IDA:RGD.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:RGD.
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:0007422; P:peripheral nervous system development; IEP:BHF-UCL.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
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; IPR008054; Na_channel_a8su.
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; PF00612; IQ; 1.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
PRINTS; PR01667; NACHANNEL8.
SMART; SM00015; IQ; 1.
PROSITE; PS50096; IQ; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Sodium; Sodium channel; Sodium transport; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 1978 Sodium channel protein type 8 subunit
alpha.
/FTId=PRO_0000390890.
TOPO_DOM 1 132 Cytoplasmic. {ECO:0000305}.
TRANSMEM 133 151 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 152 158 Extracellular. {ECO:0000305}.
TRANSMEM 159 179 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 180 193 Cytoplasmic. {ECO:0000305}.
TRANSMEM 194 211 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 212 217 Extracellular. {ECO:0000305}.
TRANSMEM 218 234 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 235 253 Cytoplasmic. {ECO:0000305}.
TRANSMEM 254 273 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 274 355 Extracellular. {ECO:0000305}.
INTRAMEM 356 380 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 381 387 Extracellular. {ECO:0000305}.
TRANSMEM 388 408 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 409 751 Cytoplasmic. {ECO:0000305}.
TRANSMEM 752 770 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 771 781 Extracellular. {ECO:0000305}.
TRANSMEM 782 801 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 802 815 Cytoplasmic. {ECO:0000305}.
TRANSMEM 816 835 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 836 837 Extracellular. {ECO:0000305}.
TRANSMEM 838 855 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 856 871 Cytoplasmic. {ECO:0000305}.
TRANSMEM 872 890 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 891 919 Extracellular. {ECO:0000305}.
INTRAMEM 920 940 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 941 953 Extracellular. {ECO:0000305}.
TRANSMEM 954 974 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 975 1197 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1198 1215 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1216 1228 Extracellular. {ECO:0000305}.
TRANSMEM 1229 1247 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1248 1261 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1262 1280 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1281 1288 Extracellular. {ECO:0000305}.
TRANSMEM 1289 1307 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1308 1324 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1325 1344 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1345 1397 Extracellular. {ECO:0000305}.
INTRAMEM 1398 1419 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1420 1436 Extracellular. {ECO:0000305}.
TRANSMEM 1437 1458 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1459 1521 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1522 1539 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1540 1550 Extracellular. {ECO:0000305}.
TRANSMEM 1551 1569 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1570 1581 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1582 1599 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1600 1612 Extracellular. {ECO:0000305}.
TRANSMEM 1613 1629 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1630 1648 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1649 1666 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1667 1688 Extracellular. {ECO:0000305}.
INTRAMEM 1689 1711 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1712 1740 Extracellular. {ECO:0000305}.
TRANSMEM 1741 1763 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1764 1978 Cytoplasmic. {ECO:0000305}.
REPEAT 114 442 I. {ECO:0000305}.
REPEAT 733 1005 II. {ECO:0000305}.
REPEAT 1178 1493 III. {ECO:0000305}.
REPEAT 1502 1799 IV. {ECO:0000305}.
DOMAIN 1893 1922 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
NP_BIND 891 898 ATP. {ECO:0000255}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1495 1495 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q15858}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 326 326 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1356 1356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1370 1370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1381 1381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 281 333 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 902 902 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 902 902 Interchain; with the conotoxin GVIIJ
(when the channel is not linked to SCN2B
or SCN4B; the bond to SCN2B or SCN4B
protects the channel from the inhibition
by toxin).
{ECO:0000250|UniProtKB:P04775}.
DISULFID 942 951 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 664 664 E -> EVKIDKAATDS (in isoform 2).
{ECO:0000303|PubMed:9603190}.
/FTId=VSP_038652.
SEQUENCE 1978 AA; 225159 MW; 9160843C5935B88B CRC64;
MAARLLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED SKPKPNSDLE
AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG KTLFRFSATP ALYILSPFNL
IRRIAIKILI HSVFSMIIMC TILTNCVFMT FSNPPEWSKN VEYTFTGIYT FESLVKIIAR
GFCIDGFTFL RDPWNWLDFS VIMMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI
VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTRGF
DWEEYINNKT NFYMVPGMLE PLLCGNSSDA GQCPEGFQCM KAGRNPNYGY TSFDTFSWAF
LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF YLVNLILAVV AMAYEEQNQA
TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA MATSAGTVSE DAIEEEGEDG VGSPRSSSEL
SKLSSKSAKE RRNRRKKRKQ KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF
SIMNQSLLSI PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS
LFIPIRARER RSSYSGYSGY SQCSRSSRIF PSLRRSVKRN STVDCNGVVS LIGPGSHIGR
LLPEATTEVE IKKKGPGSLL VSMDQLASYG RKDRINSIMS VVTNTLVEEL EESQRKCPPC
WYKFANTFLI WECHPYWIKL KEIVNLIVMD PFVDLAITIC IVLNTLFMAM EHHPMTPQFE
HVLAVGNLVF TGIFTAEMFL KLIAMDPYYY FQEGWNIFDG FIVSLSLMEL SLADVEGLSV
LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL AIIVFIFAVV GMQLFGKSYK
ECVCKINQEC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW DCMEVAGQAM CLIVFMMVMV
IGNLVVLNLF LALLLSSFSA DNLAATDDDG EMNNLQISVI RIKKGVAWTK VKVHAFMQAH
FKQREADEVK PLDELYEKKA NCIANHTGVD IHRNGDFQKN GNGTTSGIGS SVEKYIIDED
HMSFINNPNL TVRVPIAVGE SDFENLNTED VSSESDPEGS KDKLDDTSSS EGSTIDIKPE
VEEVPVEQPE EYLDPDACFT EGCVQRFKCC QVNIEEGLGK SWWILRKTCF LIVEHNWFET
FIIFMILLSS GALAFEDIYI EQRKTIRTIL EYADKVFTYI FILEMLLKWT AYGFVKFFTN
AWCWLDFLIV AVSLVSLIAN ALGYSELGAI KSLRTLRALR PLRALSRFEG MRVVVNALVG
AIPSIMNVLL VCLIFWLIFS IMGVNLFAGK YHYCFNETSE IRFEIDIVNN KTDCEKLMEG
NSTEIRWKNV KINFDNVGAG YLALLQVATF KGWMDIMYAA VDSRKPDEQP DYEGNIYMYI
YFVIFIIFGS FFTLNLFIGV IIDNFNQQKK KFGGQDIFMT EEQKKYYNAM KKLGSKKPQK
PIPRPLNKIQ GIVFDFVTQQ AFDIVIMMLI CLNMVTMMVE TDTQSKQMEN ILYWINLVFV
IFFTCECVLK MFALRHYYFT IGWNIFDFVV VILSIVGMFL ADIIEKYFVS PTLFRVIRLA
RIGRILRLIK GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIFSIFGMSN FAYVKHEAGI
DDMFNFETFG NSMICLFQIT TSAGWDGLLL PILNRPPDCS LDKEHPGSGF KGDCGNPSVG
IFFFVSYIII SFLIVVNMYI AIILENFSVA TEESADPLSE DDFETFYEIW EKFDPDATQF
IEYCKLADFA DALEHPLRVP KPNTIELIAM DLPMVSGDRI HCLDILFAFT KRVLGDSGEL
DILRQQMEER FVASNPSKVS YEPITTTLRR KQEEVSAVVL QRAYRGHLAR RGFICRKMAS
NKLENGGTHR DKKESTPSTA SLPSYDSVTK PDKEKQQRAE EGRRERAKRQ KEVRESKC


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EIAAB37603 Rat,Rattus norvegicus,Scn5a,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel sub
EIAAB37583 Rat,Rattus norvegicus,Scn2a,Scn2a1,Sodium channel protein brain II subunit alpha,Sodium channel protein type 2 subunit alpha,Sodium channel protein type II subunit alpha,Voltage-gated sodium channel s
EIAAB37602 mH1,Mouse,Mus musculus,Scn5a,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel su
EIAAB37589 Rat,Rattus norvegicus,Scn3a,Sodium channel protein brain III subunit alpha,Sodium channel protein type 3 subunit alpha,Sodium channel protein type III subunit alpha,Voltage-gated sodium channel subtyp
EIAAB37584 HBSC II,Homo sapiens,Human,NAC2,SCN2A,SCN2A1,SCN2A2,Sodium channel protein brain II subunit alpha,Sodium channel protein type 2 subunit alpha,Sodium channel protein type II subunit alpha,Voltage-gated
EIAAB37605 Homo sapiens,Human,Putative voltage-gated sodium channel subunit alpha Nax,SCN6A,SCN7A,Sodium channel protein cardiac and skeletal muscle subunit alpha,Sodium channel protein type 7 subunit alpha,Sodi
EIAAB37597 Mu-1,Rat,Rattus norvegicus,Scn4a,SkM1,Sodium channel protein skeletal muscle subunit alpha,Sodium channel protein type 4 subunit alpha,Sodium channel protein type IV subunit alpha,Voltage-gated sodium


 

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