ID SCN9A_MOUSE Reviewed; 1984 AA.
AC Q62205; A2ASI7; Q5DTI0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=Sodium channel protein type 9 subunit alpha {ECO:0000250|UniProtKB:Q15858};
DE AltName: Full=Peripheral sodium channel 1;
DE Short=PN1 {ECO:0000250|UniProtKB:O08562};
DE AltName: Full=Sodium channel protein type IX subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.7;
GN Name=Scn9a {ECO:0000312|MGI:MGI:107636};
GN Synonyms=Kiaa4197 {ECO:0000303|Ref.3};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1675-1983.
RC TISSUE=Brain;
RA Jover E., Shah V.;
RT "Mouse sodium channel 25 in m13mp19.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1740-1983.
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEDD4 AND NEDD4L, AND
RP UBIQUITINATION.
RX PubMed=15123669; DOI=10.1074/jbc.m402820200;
RA Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
RT "Regulation of neuronal voltage-gated sodium channels by the ubiquitin-
RT protein ligases Nedd4 and Nedd4-2.";
RL J. Biol. Chem. 279:28930-28935(2004).
RN [5]
RP FUNCTION IN INFLAMMATORY PAIN.
RX PubMed=15314237; DOI=10.1073/pnas.0404915101;
RA Nassar M.A., Stirling L.C., Forlani G., Baker M.D., Matthews E.A.,
RA Dickenson A.H., Wood J.N.;
RT "Nociceptor-specific gene deletion reveals a major role for Nav1.7 (PN1) in
RT acute and inflammatory pain.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12706-12711(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=31647222; DOI=10.1021/acs.bioconjchem.9b00612;
RA Gonzales J., Demetrio de Souza Franca P., Jiang Y., Pirovano G.,
RA Kossatz S., Guru N., Yarilin D., Agwa A.J., Schroeder C.I., Patel S.G.,
RA Ganly I., King G.F., Reiner T.;
RT "Fluorescence imaging of peripheral nerves by a Nav1.7-targeted inhibitor
RT cystine knot peptide.";
RL Bioconj. Chem. 30:2879-2888(2019).
RN [7]
RP SUBUNIT.
RX PubMed=37117223; DOI=10.1038/s41467-023-37963-2;
RA Jami S., Deuis J.R., Klasfauseweh T., Cheng X., Kurdyukov S., Chung F.,
RA Okorokov A.L., Li S., Zhang J., Cristofori-Armstrong B., Israel M.R.,
RA Ju R.J., Robinson S.D., Zhao P., Ragnarsson L., Andersson A., Tran P.,
RA Schendel V., McMahon K.L., Tran H.N.T., Chin Y.K., Zhu Y., Liu J.,
RA Crawford T., Purushothamvasan S., Habib A.M., Andersson D.A., Rash L.D.,
RA Wood J.N., Zhao J., Stehbens S.J., Mobli M., Leffler A., Jiang D.,
RA Cox J.J., Waxman S.G., Dib-Hajj S.D., Gregory Neely G., Durek T.,
RA Vetter I.;
RT "Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7
RT function.";
RL Nat. Commun. 14:2442-2442(2023).
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 (PubMed:15123669). It is
CC a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain
CC mechanisms, especially in the development of inflammatory pain
CC (PubMed:15314237). {ECO:0000250|UniProtKB:Q15858,
CC ECO:0000269|PubMed:15123669, ECO:0000269|PubMed:15314237}.
CC -!- SUBUNIT: The sodium channel complex consists of a large, channel-
CC forming alpha subunit (SCN9A) regulated by one or more beta subunits
CC (SCN1B, SCN2B, SCN3B and SCN4B) (By similarity). SCN1B and SCN3B are
CC non-covalently associated with SCN2A. SCN2B and SCN4B are disulfide-
CC linked to SCN2A (By similarity). Interacts with NEDD4 and NEDD4L
CC (PubMed:15123669). Interacts with TMEM233 (PubMed:37117223). Interacts
CC with the conotoxin GVIIJ (By similarity).
CC {ECO:0000250|UniProtKB:O08562, ECO:0000250|UniProtKB:Q15858,
CC ECO:0000269|PubMed:15123669, ECO:0000305|PubMed:37117223}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15123669};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cell
CC projection, neuron projection {ECO:0000250|UniProtKB:O08562}. Note=In
CC neurite terminals. {ECO:0000250|UniProtKB:O08562}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in sciatic nerves, with moderate
CC levels in kidney (PubMed:31647222). Not detected in liver, brain and
CC muscle (PubMed:31647222). {ECO:0000269|PubMed:31647222}.
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 -!- PTM: Ubiquitinated by NEDD4L; which may promote its endocytosis. Does
CC not seem to be ubiquitinated by NEDD4. {ECO:0000269|PubMed:15123669}.
CC -!- PTM: Phosphorylation at Ser-1488 by PKC in a highly conserved
CC cytoplasmic loop increases peak sodium currents.
CC {ECO:0000250|UniProtKB:Q15858}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.7/SCN9A subfamily. {ECO:0000305}.
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DR EMBL; AL928623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L42338; AAA67106.1; -; mRNA.
DR EMBL; AK220540; BAD90315.1; -; mRNA.
DR CCDS; CCDS71063.1; -.
DR RefSeq; NP_001277603.1; NM_001290674.1.
DR AlphaFoldDB; Q62205; -.
DR SMR; Q62205; -.
DR BioGRID; 203104; 14.
DR IntAct; Q62205; 1.
DR MINT; Q62205; -.
DR STRING; 10090.ENSMUSP00000097642; -.
DR BindingDB; Q62205; -.
DR ChEMBL; CHEMBL3414411; -.
DR DrugCentral; Q62205; -.
DR GuidetoPHARMACOLOGY; 584; -.
DR iPTMnet; Q62205; -.
DR PhosphoSitePlus; Q62205; -.
DR MaxQB; Q62205; -.
DR PaxDb; 10090-ENSMUSP00000097642; -.
DR ProteomicsDB; 256751; -.
DR ABCD; Q62205; 1 sequenced antibody.
DR Antibodypedia; 33781; 562 antibodies from 39 providers.
DR DNASU; 20274; -.
DR Ensembl; ENSMUST00000100064.9; ENSMUSP00000097642.3; ENSMUSG00000075316.13.
DR GeneID; 20274; -.
DR KEGG; mmu:20274; -.
DR UCSC; uc008jxe.4; mouse.
DR AGR; MGI:107636; -.
DR CTD; 6335; -.
DR MGI; MGI:107636; Scn9a.
DR VEuPathDB; HostDB:ENSMUSG00000075316; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000161368; -.
DR InParanoid; Q62205; -.
DR OMA; NCSPFWI; -.
DR OrthoDB; 1110761at2759; -.
DR PhylomeDB; Q62205; -.
DR TreeFam; TF323985; -.
DR BioGRID-ORCS; 20274; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Scn9a; mouse.
DR PRO; PR:Q62205; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q62205; Protein.
DR Bgee; ENSMUSG00000075316; Expressed in lumbar dorsal root ganglion and 73 other cell types or tissues.
DR ExpressionAtlas; Q62205; baseline and differential.
DR Genevisible; Q62205; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
DR GO; GO:0005272; F:sodium channel activity; TAS:Reactome.
DR GO; GO:0031402; F:sodium ion binding; ISO:MGI.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:UniProtKB.
DR GO; GO:0061368; P:behavioral response to formalin induced pain; ISO:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0007623; P:circadian rhythm; IMP:MGI.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:MGI.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0045759; P:negative regulation of action potential; ISO:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0009636; P:response to toxic substance; IDA:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
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; IPR000048; IQ_motif_EF-hand-BS.
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:SF221; SODIUM CHANNEL PROTEIN TYPE 9 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 SMART; SM00015; IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Coiled coil; Disulfide bond; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..1984
FT /note="Sodium channel protein type 9 subunit alpha"
FT /id="PRO_0000048503"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..145
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 146..152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 174..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..205
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 206..211
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..228
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 229..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..267
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 268..346
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 347..371
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 372..378
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 400..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 744..762
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 763..773
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 774..793
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 794..807
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 808..827
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 828..829
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 830..847
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 848..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 864..882
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 883..911
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 912..932
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 933..945
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 946..966
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 967..1191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1192..1209
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1210..1222
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1223..1241
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1242..1255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1256..1274
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1275..1282
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1283..1301
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1302..1318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1319..1338
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1339..1390
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1391..1412
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1413..1429
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1430..1451
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1452..1514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1515..1532
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1533..1543
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1544..1562
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1563..1574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1575..1592
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1593..1605
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1606..1622
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1623..1641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1642..1659
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1660..1681
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1682..1704
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1705..1734
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1735..1757
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1758..1984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 112..410
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 725..988
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1178..1486
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1495..1793
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1887..1916
FT /note="IQ"
FT REGION 26..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1933..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 402..449
FT /evidence="ECO:0000255"
FT COILED 684..708
FT /evidence="ECO:0000255"
FT COMPBIAS 26..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 821
FT /note="Is directly targeted by the spider protoxin-II"
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT SITE 826
FT /note="Is directly targeted by the spider protoxin-II"
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT MOD_RES 1488
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT DISULFID 275..324
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 894
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 894
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 896..902
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT DISULFID 934..943
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 1348..1368
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT DISULFID 1713..1728
FT /evidence="ECO:0000250|UniProtKB:Q15858"
SQ SEQUENCE 1984 AA; 225813 MW; 51A8DBA38EC7EF38 CRC64;
MAMLPPPGPQ SFVHFTKQSL ALIEQRISEE KAKGHKDEKK DDEEEGPKPS SDLEAGKQLP
FIYGDIPPGM VSEPLEDLDP YYADKKTFIV LNKGKAIFRF NATPALYMLS PFSPLRRISI
KILVHSLFSM LIMCTILTNC IFMTMSNPPD WTKNVEYTFT GIYTFESLIK ILARGFCVGE
FTFLRDPWNW LDFVVIVFAY LTEFVNLGNV SALRTFRVLR ALKTISVIPG LKTIVGALIQ
SVKKLSDVMI LTVFCLSVFA LIGLQLFMGN LKHKCFRKDL EQNETLESIM STAESEEELK
RYFYYLEGSK DALLCGFSTD SGQCPEGYEC VTAGRNPDYG YTSFDTFGWA FLALFRLMTQ
DYWENLYQQT LRAAGKTYMI FFVVVIFLGS FYLINLILAV VAMAYEEQNQ ANIEEAKQKE
LEFQQMLDRL KKEQEEAEAI AAAAAEYTSL GRSRIMGLSE SSSETSRLSS KSAKERRNRR
KKKKQKLSSG EEKGDDEKLS KSGSEESIRK KSFHLGVEGH HRAREKRLST PNQSPLSIRG
SLFSARRSSR TSLFSFKGRG RDLGSETEFA DDEHSIFGDN ESRRGSLFVP HRPRERRSSN
ISQASRSPPV LPVNGKMHSA VDCNGVVSLV DGPSALMLPN GQLLPEVIID KATSDDSGTT
NQMRKKRLSS SYFLSEDMLN DPHLRQRAMS RASILTNTVE ELEESRQKCP PWWYRFAHTF
LIWNCSPYWI KFKKFIYFIV MDPFVDLAIT ICIVLNTLFM AMEHHPMTDE FKNVLAVGNL
VFTGIFAAEM VLKLIAMDPY EYFQVGWNIF DSLIVTLSLV ELFLADVEGL SVLRSFRLLR
VFKLAKSWPT LNMLIKIIGN SVGALGNLTL VLAIIVFIFA VVGMQLFGKS YKECVCKINE
NCKLPRWHMN DFFHSFLIVF RVLCGEWIET MWDCMEVAGQ TMCLIVYMMV MVIGNLVVLN
LFLALLLSSF SSDNLTAIEE DTDANNLQIA VARIKRGINY VKQTLREFIL KSFSKKPKGS
KDTKRTADPN NKRENYISNR TLAEISKDHN FLKEKDKISG FSSSLDKSFM DENDYQSFIH
NPSLTVTVPI APGESDLENM NTEELSSDSD SDYSKERRNR SSSSECSTVD NPLPGEEEAE
AEPINADEPE ACFTDGCVRR FPCCQVNIDS GKGKVWWTIR KTCYRIVEHS WFESFIVLMI
LLSSGALAFE DIYIEKKKTI KIILEYADKI FTYIFILEML LKWVAYGYKT YFTNAWCWLD
FLIVDVSLVT LVANTLGYSD LGPIKSLRTL RALRPLRALS RFEGMRVVVN ALIGAIPSIM
NVLLVCLIFW LIFSIMGVNL FAGKFYECVN TTDGSRFSVS QVANRSECFA LMNVSGNVRW
KNLKVNFDNV GLGYLSLLQV ATFKGWMDIM YAAVDSVNVN AQPIYEYNLY MYIYFVIFII
FGSFFTLNLF IGVIIDNFNQ QKKKLGGQDI FMTEEQKKYY NAMKKLGSKK PQKPIPRPGN
KFQGCIFDLV TNQAFDITIM VLICLNMVTM MVEKEGQTDY MSFVLYWINV VFIILFTGEC
VLKLISLRHY YFTVGWNIFD FVVVILSIVG MFLAEMIEKY FVSPTLFRVI RLARIGRILR
LIKGAKGIRT LLFALMMSLP ALFNIGLLLF LVMFIYAIFG MSNFAYVKKE AGINDMFNFE
TFGNSMICLF QITTSAGWDG LLAPILNSAP PDCDPKKVHP GSSVEGDCGN PSVGIFYFVS
YIIISFLVVV NMYIAVILEN FSVATEESTE PLSEDDFEMF YEVWEKFDPD ATQFIEFCKL
SDFAAALDPP LLIAKPNKVQ LIAMDLPMVS GDRIHCLDIL FAFTKRVLGE SGEMDSLRSQ
MEERFMSANP SKVSYEPITT TLKRKQEDVS ATIIQRAYRR YRLRQNVKNI SSIYIKDGDR
DDDLPNKEDI VFDNVNENSS PEKTDATAST ISPPSYDSVT KPDQEKYETD KTEKEDKEKD
ESRK
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