SCN4A_RAT
ID SCN4A_RAT Reviewed; 1840 AA.
AC P15390; O70611;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Sodium channel protein type 4 subunit alpha;
DE AltName: Full=Mu-1;
DE AltName: Full=SkM1 {ECO:0000303|PubMed:9613589};
DE AltName: Full=Sodium channel protein skeletal muscle subunit alpha;
DE AltName: Full=Sodium channel protein type IV subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.4;
GN Name=Scn4a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2559760; DOI=10.1016/0896-6273(89)90113-x;
RA Trimmer J.S., Cooperman S.S., Tomiko S.A., Zhou J., Crean S.M., Boyle M.B.,
RA Kallen R.G., Sheng Z., Barchi R.L., Sigworth F.J., Goodman R.H.,
RA Agnew W.S., Mandel G.;
RT "Primary structure and functional expression of a mammalian skeletal muscle
RT sodium channel.";
RL Neuron 3:33-49(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS ILE-120;
RP HIS-916; CYS-1202; ASP-1257; GLY-1755 AND LYS-1803.
RC STRAIN=COP; TISSUE=Prostate;
RX PubMed=9613589; DOI=10.1016/s0014-5793(98)00378-0;
RA Diss J.K.J., Stewart D., Fraser S.P., Black J.A., Dibb-Hajj S.,
RA Waxman S.G., Archer S.N., Djamgoz M.B.A.;
RT "Expression of skeletal muscle-type voltage-gated Na+ channel in rat and
RT human prostate cancer cell lines.";
RL FEBS Lett. 427:5-10(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP TYR-401.
RX PubMed=16303569; DOI=10.1016/j.cub.2005.10.068;
RA Venkatesh B., Lu S.Q., Dandona N., See S.L., Brenner S., Soong T.W.;
RT "Genetic basis of tetrodotoxin resistance in pufferfishes.";
RL Curr. Biol. 15:2069-2072(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF 1240-MET-ILE-1241.
RX PubMed=23077250; DOI=10.1073/pnas.1206952109;
RA Walker J.R., Novick P.A., Parsons W.H., McGregor M., Zablocki J.,
RA Pande V.S., Du Bois J.;
RT "Marked difference in saxitoxin and tetrodotoxin affinity for the human
RT nociceptive voltage-gated sodium channel (Nav1.7) [corrected].";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18102-18107(2012).
RN [6]
RP ERRATUM OF PUBMED:23077250.
RA Walker J.R., Novick P.A., Parsons W.H., McGregor M., Zablocki J.,
RA Pande V.S., Du Bois J.;
RL Proc. Natl. Acad. Sci. U.S.A. 109:21551-21551(2012).
RN [7]
RP INTERACTION WITH THE CONOTOXIN GVIIJ.
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., Wickenden A.D.,
RA 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 [8]
RP FUNCTION, INTERACTION WITH SCN1B, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP 1303-ILE--MET-1305.
RX PubMed=28012039; DOI=10.1007/s00249-016-1193-3;
RA Sanchez-Solano A., Islas A.A., Scior T., Paiz-Candia B.,
RA Millan-PerezPena L., Salinas-Stefanon E.M.;
RT "Characterization of specific allosteric effects of the Na+ channel beta1
RT subunit on the Nav1.4 isoform.";
RL Eur. Biophys. J. 46:485-494(2017).
RN [9]
RP MUTAGENESIS OF TYR-1379 AND ASN-1380.
RX PubMed=28428547; DOI=10.1038/s41598-017-01129-0;
RA Wingerd J.S., Mozar C.A., Ussing C.A., Murali S.S., Chin Y.K.,
RA Cristofori-Armstrong B., Durek T., Gilchrist J., Vaughan C.W., Bosmans F.,
RA Adams D.J., Lewis R.J., Alewood P.F., Mobli M., Christie M.J., Rash L.D.;
RT "The tarantula toxin beta/delta-TRTX-Pre1a highlights the importance of the
RT S1-S2 voltage-sensor region for sodium channel subtype selectivity.";
RL Sci. Rep. 7:974-988(2017).
RN [10]
RP STRUCTURE BY NMR OF 1567-1594.
RX PubMed=30389410; DOI=10.1016/j.bmc.2018.10.012;
RA Niitsu A., Egawa A., Ikeda K., Tachibana K., Fujiwara T.;
RT "Veratridine binding to a transmembrane helix of sodium channel Nav1.4
RT determined by solid-state NMR.";
RL Bioorg. Med. Chem. 26:5644-5653(2018).
CC -!- FUNCTION: Pore-forming subunit of a voltage-gated sodium channel
CC complex through which Na(+) ions pass in accordance with their
CC electrochemical gradient (PubMed:2559760, PubMed:16303569,
CC PubMed:28012039). Alternates between resting, activated and inactivated
CC states (PubMed:28012039). Required for normal muscle fiber
CC excitability, normal muscle contraction and relaxation cycles, and
CC constant muscle strength in the presence of fluctuating K(+) levels (By
CC similarity). {ECO:0000250|UniProtKB:P35499,
CC ECO:0000269|PubMed:16303569, ECO:0000269|PubMed:2559760,
CC ECO:0000269|PubMed:28012039}.
CC -!- ACTIVITY REGULATION: Channel activity is regulated by the ancillary
CC beta subunit SCN1B (PubMed:28012039). SCN1B strongly enhances the
CC presence of the pore-forming alpha subunit at the cell surface (By
CC similarity). Interaction with SCN1B is required for rapid channel
CC inactivation and rapid recovery after inactivation, and prevents
CC decrease of channel activity in response to repetitive, high-frequency
CC depolarizations (PubMed:28012039). Potently inhibited by tetrodotoxin
CC and saxitoxin (PubMed:16303569, PubMed:23077250).
CC {ECO:0000250|UniProtKB:P35499, ECO:0000269|PubMed:16303569,
CC ECO:0000269|PubMed:23077250, ECO:0000269|PubMed:28012039}.
CC -!- SUBUNIT: Component of a voltage-sensitive sodium channel complex that
CC consists of a pore-forming alpha subunit and one or more regulatory
CC beta subunits. Interacts with SCN1B (PubMed:28012039). Heterooligomer
CC with SCN2B or SCN4B; disulfide-linked (By similarity). Interacts with
CC the PDZ domain of the syntrophins SNTA1, SNTB1 and SNTB2 (By
CC similarity). Interacts with the conotoxin GVIIJ (PubMed:24497506).
CC {ECO:0000250|UniProtKB:P04775, ECO:0000250|UniProtKB:Q9ER60,
CC ECO:0000250|UniProtKB:Q9JJV9, ECO:0000269|PubMed:24497506,
CC ECO:0000269|PubMed:28012039}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16303569,
CC ECO:0000269|PubMed:2559760, ECO:0000269|PubMed:28012039}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P35499}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle.
CC {ECO:0000269|PubMed:9613589}.
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:0000250|UniProtKB:P35499}.
CC -!- PTM: Phosphorylation at Ser-1321 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.4/SCN4A subfamily. {ECO:0000305}.
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DR EMBL; M26643; AAA41682.1; -; mRNA.
DR EMBL; Y17153; CAA76659.1; -; mRNA.
DR PIR; JN0007; CHRTM1.
DR RefSeq; NP_037310.1; NM_013178.1.
DR PDB; 5JR0; NMR; -; A=1567-1594.
DR PDB; 6MUE; X-ray; 1.90 A; B=1716-1744.
DR PDBsum; 5JR0; -.
DR PDBsum; 6MUE; -.
DR AlphaFoldDB; P15390; -.
DR SMR; P15390; -.
DR BioGRID; 247751; 2.
DR STRING; 10116.ENSRNOP00000016841; -.
DR BindingDB; P15390; -.
DR ChEMBL; CHEMBL3509; -.
DR GuidetoPHARMACOLOGY; 581; -.
DR GlyGen; P15390; 9 sites.
DR iPTMnet; P15390; -.
DR PhosphoSitePlus; P15390; -.
DR PaxDb; P15390; -.
DR PRIDE; P15390; -.
DR ABCD; P15390; 1 sequenced antibody.
DR GeneID; 25722; -.
DR KEGG; rno:25722; -.
DR UCSC; RGD:3636; rat.
DR CTD; 6329; -.
DR RGD; 3636; Scn4a.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; P15390; -.
DR PhylomeDB; P15390; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:P15390; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISS:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:UniProtKB.
DR GO; GO:0006812; P:cation transport; IMP:RGD.
DR GO; GO:0015871; P:choline transport; IMP:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IMP:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0100001; P:regulation of skeletal muscle contraction by action potential; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR008052; Na_channel_a4su_mammal.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PRINTS; PR01665; NACHANNEL4.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1840
FT /note="Sodium channel protein type 4 subunit alpha"
FT /id="PRO_0000048496"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..150
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 151..157
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 179..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..210
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 211..216
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..233
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 234..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..272
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 273..385
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 386..410
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 411..417
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 418..438
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 439..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 573..591
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 592..602
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 603..622
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 623..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 637..656
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 657..658
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 659..676
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 677..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 693..711
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 712..740
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 741..761
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 762..772
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 773..791
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 792..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1026..1043
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1044..1056
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1057..1075
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1076..1089
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1090..1108
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1109..1116
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1117..1135
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1136..1152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1153..1172
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1173..1223
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1224..1245
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1246..1262
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1263..1284
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1285..1347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1348..1365
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1366..1376
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1377..1395
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1396..1407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1408..1425
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1426..1438
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1439..1455
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1456..1474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1475..1492
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1493..1514
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1515..1537
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1538..1567
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1568..1590
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1591..1840
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 113..448
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 554..826
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1006..1319
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1328..1626
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1720..1749
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 36..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1305
FT /note="Important for rapid channel inactivation"
FT /evidence="ECO:0000269|PubMed:28012039"
FT REGION 1775..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..983
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1827
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 401
FT /note="Important for inhibition by tetrodotoxin"
FT /evidence="ECO:0000269|PubMed:16303569"
FT MOD_RES 56
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 251
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1321
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 1321
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..354
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 363..369
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 723
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 723
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 725..731
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 763..772
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1546..1561
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT VARIANT 120
FT /note="V -> I (in strain: COP; prostatic cancer cell
FT lines)"
FT /evidence="ECO:0000269|PubMed:9613589"
FT VARIANT 916
FT /note="Q -> H (in strain: COP; prostatic cancer cell
FT lines)"
FT /evidence="ECO:0000269|PubMed:9613589"
FT VARIANT 1202
FT /note="S -> C (in strain: COP; prostatic cancer cell
FT lines)"
FT /evidence="ECO:0000269|PubMed:9613589"
FT VARIANT 1257
FT /note="H -> D (in strain: COP; prostatic cancer cell
FT lines)"
FT /evidence="ECO:0000269|PubMed:9613589"
FT VARIANT 1755
FT /note="D -> G (in strain: COP; prostatic cancer cell
FT lines)"
FT /evidence="ECO:0000269|PubMed:9613589"
FT VARIANT 1803
FT /note="E -> K (in strain: COP; prostatic cancer cell
FT lines)"
FT /evidence="ECO:0000269|PubMed:9613589"
FT MUTAGEN 401
FT /note="Y->C,N: Strongly reduced sensitivity to
FT tetrodotoxin."
FT /evidence="ECO:0000269|PubMed:16303569"
FT MUTAGEN 1240..1241
FT /note="MD->TI: Strongly reduced sensitivity to saxitoxin."
FT /evidence="ECO:0000269|PubMed:23077250"
FT MUTAGEN 1303..1305
FT /note="Missing: Loss of rapid channel inactivation."
FT /evidence="ECO:0000269|PubMed:28012039"
FT MUTAGEN 1379
FT /note="Y->S: Become sensitive to the spider beta/delta-
FT theraphotoxin-Pre1a, which inhibits inactivation of the
FT channel."
FT /evidence="ECO:0000269|PubMed:28428547"
FT MUTAGEN 1380
FT /note="N->R: No change in sensitivity to the spider
FT beta/delta-theraphotoxin-Pre1a."
FT /evidence="ECO:0000269|PubMed:28428547"
FT HELIX 1569..1594
FT /evidence="ECO:0007829|PDB:5JR0"
FT HELIX 1722..1732
FT /evidence="ECO:0007829|PDB:6MUE"
SQ SEQUENCE 1840 AA; 208867 MW; C5DC09D93DD9FAD6 CRC64;
MASSSLPNLV PPGPHCLRPF TPESLAAIEQ RAVEEEARLQ RNKQMEIEEP ERKPRSDLEA
GKNLPLIYGD PPPEVIGIPL EDLDPYYSDK KTFIVLNKGK AIFRFSATPA LYLLSPFSIV
RRVAIKVLIH ALFSMFIMIT ILTNCVFMTM SNPPSWSKHV EYTFTGIYTF ESLIKMLARG
FCIDDFTFLR DPWNWLDFSV ITMAYVTEFV DLGNISALRT FRVLRALKTI TVIPGLKTIV
GALIQSVKKL SDVMILTVFC LSVFALVGLQ LFMGNLRQKC VRWPPPMNDT NTTWYGNDTW
YSNDTWYGND TWYINDTWNS QESWAGNSTF DWEAYINDEG NFYFLEGSND ALLCGNSSDA
GHCPEGYECI KAGRNPNYGY TSYDTFSWAF LALFRLMTQD YWENLFQLTL RAAGKTYMIF
FVVIIFLGSF YLINLILAVV AMAYAEQNEA TLAEDQEKEE EFQQMLEKYK KHQEELEKAK
AAQALESGEE ADGDPTHNKD CNGSLDASGE KGPPRPSCSA DSAISDAMEE LEEAHQKCPP
WWYKCAHKVL IWNCCAPWVK FKHIIYLIVM DPFVDLGITI CIVLNTLFMA MEHYPMTEHF
DNVLSVGNLV FTGIFTAEMV LKLIAMDPYE YFQQGWNIFD SFIVTLSLVE LGLANVQGLS
VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV VGMQLFGKSY
KECVCKIASD CNLPRWHMND FFHSFLIVFR ILCGEWIETM WDCMEVAGQA MCLTVFLMVM
VIGNLVVLNL FLALLLSSFS ADSLAASDED GEMNNLQIAI GRIKWGIGFA KTFLLGLLRG
KILSPKEIIL SLGEPGGAGE NAEESTPEDE KKEPPPEDKE LKDNHILNHV GLTDGPRSSI
ELDHLNFINN PYLTIQVPIA SEESDLEMPT EEETDAFSEP EDIKKPLQPL YDGNSSVCST
ADYKPPEEDP EEQAEENPEG EQPEECFTEA CVKRCPCLYV DISQGRGKMW WTLRRACFKI
VEHNWFETFI VFMILLSSGA LAFEDIYIEQ RRVIRTILEY ADKVFTYIFI LEMLLKWVAY
GFKVYFTNAW CWLDFLIVDV SIISLVANWL GYSELGPIKS LRTLRALRPL RALSRFEGMR
VVVNALLGAI PSIMNVLLVC LIFWLIFSIM GVNLFAGKFY YCVNTTTSER FDISVVNNKS
ESESLMYTGQ VRWMNVKVNY DNVGLGYLSL LQVATFKGWM DIMYAAVDSR EKEEQPHYEV
NLYMYLYFVI FIIFGSFFTL NLFIGVIIDN FNQQKKKFGG KDIFMTEEQK KYYNAMKKLG
SKKPQKPIPR PQNKIQGMVY DFVTKQVFDI SIMILICLNM VTMMVETDDQ SQLKVDILYN
INMVFIIIFT GECVLKMFAL RHYYFTIGWN IFDFVVVILS IVGLALSDLI QKYFVSPTLF
RVIRLARIGR VLRLIRGAKG IRTLLFALMM SLPALFNIGL LLFLVMFIYS IFGMSNFAYV
KKESGIDDMF NFETFGNSII CLFEITTSAG WDGLLNPILN SGPPDCDPTL ENPGTNVRGD
CGNPSIGICF FCSYIIISFL IVVNMYIAII LENFNVATEE SSEPLSEDDF EMFYETWEKF
DPDATQFIDY SRLSDFVDTL QEPLKIAKPN KIKLITLDLP MVPGDKIHCL DILFALTKEV
LGDSGEMDAL KQTMEEKFMA ANPSKVSYEP ITTTLKRKQE EVCAIKIQRA YRRHLLQRSV
KQASYMYRHS QDGNDDGAPE KEGLLANTMN KMYGHEKEGD GVQSQGEEEK ASTEDAGPTV
EPEPTSSSDT ALTPSPPPLP PSSSPPQGQT VRPGVKESLV
