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Sodium channel protein type 1 subunit alpha (Sodium channel protein brain I subunit alpha) (Sodium channel protein type I subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.1)

 SCN1A_RAT               Reviewed;        2009 AA.
P04774;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
07-NOV-2018, entry version 156.
RecName: Full=Sodium channel protein type 1 subunit alpha;
AltName: Full=Sodium channel protein brain I subunit alpha;
AltName: Full=Sodium channel protein type I subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.1;
Name=Scn1a;
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]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2442385; DOI=10.3109/10799898709054998;
Noda M., Numa S.;
"Structure and function of sodium channel.";
J. Recept. Res. 7:467-497(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 177-253.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1658739; DOI=10.1093/nar/19.20.5673;
Sarao R., Gupta S.K., Auld V.J., Dunn R.J.;
"Developmentally regulated alternative RNA splicing of rat brain
sodium channel mRNAs.";
Nucleic Acids Res. 19:5673-5679(1991).
[4]
PHOSPHORYLATION AT SER-470; SER-551 AND SER-607.
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-525; SER-550;
SER-551 AND SER-730, 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).
[6]
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. Plays
a key role in brain, probably by regulating the moment when
neurotransmitters are released in neurons. Involved in sensory
perception of mechanical pain: activation in somatosensory neurons
induces pain without neurogenic inflammation and produces
hypersensitivity to mechanical, but not thermal stimuli.
{ECO:0000250|UniProtKB:A2APX8}.
-!- ACTIVITY REGULATION: Inactivation of this channel is specifically
inhibited by the spider toxins Hm1a and Hm1b (H.maculata, AC
P60992 and AC P0DOC5) in somatosensory neurons to elicit acute
pain and mechanical allodynia. {ECO:0000250|UniProtKB:A2APX8}.
-!- 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 FGF13.
Interacts with the conotoxin GVIIJ (PubMed:24497506).
{ECO:0000250|UniProtKB:P04775, ECO:0000250|UniProtKB:P35498,
ECO:0000269|PubMed:24497506}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P35498}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:D0E0C2}.
-!- 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}.
-!- DOMAIN: The S3b-S4 and S1-S2 loops of repeat IV are targeted by
H.maculata toxins Hm1a and Hm1b, leading to inhibit fast
inactivation of Nav1.1/SCN1A. Selectivity for H.maculata toxins
Hm1a and Hm1b depends on S1-S2 loops of repeat IV.
{ECO:0000250|UniProtKB:A2APX8}.
-!- PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000250|UniProtKB:P04775}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.1/SCN1A subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X03638; CAA27286.1; -; mRNA.
EMBL; M22253; AAA79965.1; -; mRNA.
PIR; A25019; A25019.
RefSeq; NP_110502.1; NM_030875.1.
UniGene; Rn.32079; -.
ProteinModelPortal; P04774; -.
BioGrid; 249530; 1.
CORUM; P04774; -.
STRING; 10116.ENSRNOP00000008026; -.
BindingDB; P04774; -.
ChEMBL; CHEMBL4906; -.
GuidetoPHARMACOLOGY; 578; -.
iPTMnet; P04774; -.
PhosphoSitePlus; P04774; -.
SwissPalm; P04774; -.
PaxDb; P04774; -.
PRIDE; P04774; -.
GeneID; 81574; -.
KEGG; rno:81574; -.
UCSC; RGD:69364; rat.
CTD; 6323; -.
RGD; 69364; Scn1a.
eggNOG; ENOG410INF8; Eukaryota.
eggNOG; COG1226; LUCA.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG053100; -.
InParanoid; P04774; -.
KO; K04833; -.
PhylomeDB; P04774; -.
PRO; PR:P04774; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
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:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISS:UniProtKB.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
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; IBA:GO_Central.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR008051; Na_channel_a1su.
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.
PRINTS; PR01664; NACHANNEL1.
1: Evidence at protein level;
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; Voltage-gated channel.
CHAIN 1 2009 Sodium channel protein type 1 subunit
alpha.
/FTId=PRO_0000048490.
TOPO_DOM 1 128 Cytoplasmic. {ECO:0000305}.
TRANSMEM 129 147 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 148 154 Extracellular. {ECO:0000305}.
TRANSMEM 155 175 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 176 189 Cytoplasmic. {ECO:0000305}.
TRANSMEM 190 207 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 208 213 Extracellular. {ECO:0000305}.
TRANSMEM 214 230 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 231 249 Cytoplasmic. {ECO:0000305}.
TRANSMEM 250 269 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 270 367 Extracellular. {ECO:0000305}.
INTRAMEM 368 392 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 393 399 Extracellular. {ECO:0000305}.
TRANSMEM 400 420 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 421 768 Cytoplasmic. {ECO:0000305}.
TRANSMEM 769 787 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 788 798 Extracellular. {ECO:0000305}.
TRANSMEM 799 818 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 819 832 Cytoplasmic. {ECO:0000305}.
TRANSMEM 833 852 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 853 854 Extracellular. {ECO:0000305}.
TRANSMEM 855 872 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 873 888 Cytoplasmic. {ECO:0000305}.
TRANSMEM 889 907 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 908 936 Extracellular. {ECO:0000305}.
INTRAMEM 937 957 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 958 970 Extracellular. {ECO:0000305}.
TRANSMEM 971 991 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 992 1219 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1220 1237 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1238 1250 Extracellular. {ECO:0000305}.
TRANSMEM 1251 1269 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1270 1283 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1284 1302 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1303 1310 Extracellular. {ECO:0000305}.
TRANSMEM 1311 1329 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1330 1346 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1347 1366 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1367 1418 Extracellular. {ECO:0000305}.
INTRAMEM 1419 1440 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1441 1457 Extracellular. {ECO:0000305}.
TRANSMEM 1458 1479 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1480 1542 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1543 1560 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1561 1571 Extracellular. {ECO:0000305}.
TRANSMEM 1572 1590 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1591 1602 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1603 1620 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1621 1633 Extracellular. {ECO:0000305}.
TRANSMEM 1634 1650 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1651 1669 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1670 1687 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1688 1709 Extracellular. {ECO:0000305}.
INTRAMEM 1710 1732 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1733 1762 Extracellular. {ECO:0000305}.
TRANSMEM 1763 1785 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1786 2009 Cytoplasmic. {ECO:0000305}.
REPEAT 110 454 I. {ECO:0000305}.
REPEAT 750 1022 II. {ECO:0000305}.
REPEAT 1200 1514 III. {ECO:0000305}.
REPEAT 1523 1821 IV. {ECO:0000305}.
DOMAIN 1915 1944 IQ.
REGION 1561 1571 S1-S2 loop of repeat IV.
{ECO:0000250|UniProtKB:A2APX8}.
REGION 1619 1636 S3b-S4 loop of repeat IV.
{ECO:0000250|UniProtKB:A2APX8}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:20131913}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000269|PubMed:20131913}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1516 1516 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P04775}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1378 1378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1392 1392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1403 1403 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 277 345 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 919 919 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 919 919 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 959 968 {ECO:0000250|UniProtKB:D0E0C2}.
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


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EIAAB37617 Mouse,Mus musculus,NaN,Nan,Nat,Scn11a,Sensory neuron sodium channel 2,Sns2,Sodium channel protein type 11 subunit alpha,Sodium channel protein type XI subunit alpha,Voltage-gated sodium channel subuni
EIAAB37615 Mouse,Mus musculus,Peripheral nerve sodium channel 3,PN3,Scn10a,Sensory neuron sodium channel,Sns,Sodium channel protein type 10 subunit alpha,Sodium channel protein type X subunit alpha,Voltage-gated
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
EIAAB37608 NaCh6,Peripheral nerve protein type 4,PN4,Rat,Rattus norvegicus,Scn8a,Sodium channel 6,Sodium channel protein type 8 subunit alpha,Sodium channel protein type VIII subunit alpha,Voltage-gated sodium c
EIAAB37613 Canis familiaris,Canis lupus familiaris,Dog,NaNG,SCN10A,Sodium channel protein type 10 subunit alpha,Sodium channel protein type X subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.8
EIAAB37611 hNE-Na,Homo sapiens,Human,NENA,Neuroendocrine sodium channel,Peripheral sodium channel 1,PN1,SCN9A,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gate


 

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