ID SCN8A_RAT Reviewed; 1978 AA.
AC O88420; O88421;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Sodium channel protein type 8 subunit alpha;
DE AltName: Full=Peripheral nerve protein type 4;
DE Short=PN4;
DE AltName: Full=Sodium channel 6;
DE Short=NaCh6;
DE AltName: Full=Sodium channel protein type VIII subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.6;
GN Name=Scn8a;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Spinal ganglion;
RX PubMed=9603190; DOI=10.1046/j.1471-4159.1998.70062262.x;
RA Dietrich P.S., McGivern J.G., Delgado S.G., Koch B.D., Eglen R.M.,
RA Hunter J.C., Sangameswaran L.;
RT "Functional analysis of a voltage-gated sodium channel and its splice
RT variant from rat dorsal root ganglia.";
RL J. Neurochem. 70:2262-2272(1998).
RN [2]
RP INTERACTION WITH FGF13.
RX PubMed=15282281; DOI=10.1523/jneurosci.1628-04.2004;
RA Wittmack E.K., Rush A.M., Craner M.J., Goldfarb M., Waxman S.G.,
RA Dib-Hajj S.D.;
RT "Fibroblast growth factor homologous factor 2B: association with Nav1.6 and
RT selective colocalization at nodes of Ranvier of dorsal root axons.";
RL J. Neurosci. 24:6765-6775(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-520, AND
RP IDENTIFICATION BY 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 [4]
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).
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.
CC {ECO:0000269|PubMed:9603190}.
CC -!- ACTIVITY REGULATION: Inhibited by tetrodotoxin and, more weakly, by its
CC metabolite 4,9-ah-tetrodotoxin. {ECO:0000250|UniProtKB:Q9UQD0}.
CC -!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion-
CC conducting pore-forming alpha subunit regulated by one or more beta-1
CC (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4 (SCN4B) subunits.
CC Beta-1 (SCN1B) and beta-3 (SCN3B) are non-covalently associated with
CC alpha, while beta-2 (SCN2B) and beta-4 (SCN4B) are covalently linked by
CC disulfide bonds. Interacts with NEDD4 and NEDD4L (By similarity).
CC Interacts with FGF13 (PubMed:15282281). Interacts with FGF14, GBG3,
CC GBB2 and SCN1B (By similarity). Interacts with TMEM233 (By similarity).
CC Interacts with the conotoxin GVIIJ (PubMed:24497506). Interacts with
CC CALM1; the interaction modulates the inactivation rate of SCN8A (By
CC similarity). {ECO:0000250|UniProtKB:Q9UQD0,
CC ECO:0000250|UniProtKB:Q9WTU3, ECO:0000269|PubMed:15282281,
CC ECO:0000269|PubMed:24497506}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9603190};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q9WTU3}. Note=Mainly localizes
CC to the axon initial segment. {ECO:0000250|UniProtKB:Q9WTU3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PN4;
CC IsoId=O88420-1; Sequence=Displayed;
CC Name=2; Synonyms=PN4a;
CC IsoId=O88420-2; Sequence=VSP_038652;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in brain, moderately
CC in spinal cord, and at low levels in dorsal root ganglia, nodose
CC ganglia and superior cervical ganglia. Not detected in sciatic nerve
CC and non-neuronal tissues. Isoform 2 is hardly detectable, if at all, in
CC brain, expressed at low levels in spinal cord and at highest levels in
CC dorsal root ganglia. {ECO:0000269|PubMed:9603190}.
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: May be ubiquitinated by NEDD4L; which would promote its
CC endocytosis. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-1495 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing donor splice site.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.6/SCN8A subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF049239; AAC26014.1; -; mRNA.
DR EMBL; AF049240; AAC26015.1; -; mRNA.
DR RefSeq; NP_062139.2; NM_019266.2. [O88420-1]
DR AlphaFoldDB; O88420; -.
DR BMRB; O88420; -.
DR SMR; O88420; -.
DR BioGRID; 248327; 2.
DR STRING; 10116.ENSRNOP00000008160; -.
DR BindingDB; O88420; -.
DR ChEMBL; CHEMBL2752; -.
DR GuidetoPHARMACOLOGY; 583; -.
DR CarbonylDB; O88420; -.
DR GlyCosmos; O88420; 8 sites, No reported glycans.
DR GlyGen; O88420; 8 sites.
DR iPTMnet; O88420; -.
DR PhosphoSitePlus; O88420; -.
DR PaxDb; 10116-ENSRNOP00000008160; -.
DR ABCD; O88420; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000080923.2; ENSRNOP00000075703.2; ENSRNOG00000005309.8. [O88420-2]
DR Ensembl; ENSRNOT00055048321; ENSRNOP00055039731; ENSRNOG00055027400. [O88420-1]
DR Ensembl; ENSRNOT00065037782; ENSRNOP00065030555; ENSRNOG00065021763. [O88420-1]
DR GeneID; 29710; -.
DR KEGG; rno:29710; -.
DR UCSC; RGD:3638; rat. [O88420-1]
DR AGR; RGD:3638; -.
DR CTD; 6334; -.
DR RGD; 3638; Scn8a.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000156263; -.
DR InParanoid; O88420; -.
DR OMA; ECSPMWI; -.
DR PhylomeDB; O88420; -.
DR PRO; PR:O88420; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0034706; C:sodium channel complex; ISO:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031402; F:sodium ion binding; IDA:RGD.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:0042552; P:myelination; IEP:BHF-UCL.
DR GO; GO:0021675; P:nerve development; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR GO; GO:0021554; P:optic nerve development; IEP:RGD.
DR GO; GO:0007422; P:peripheral nervous system development; IEP:BHF-UCL.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
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; IPR008054; Na_channel_a8su.
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:SF23; SODIUM CHANNEL PROTEIN TYPE 8 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PRINTS; PR01667; NACHANNEL8.
DR SMART; SM00015; IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..1978
FT /note="Sodium channel protein type 8 subunit alpha"
FT /id="PRO_0000390890"
FT TOPO_DOM 1..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 133..151
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 152..158
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 180..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..211
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 212..217
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..234
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 235..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..273
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 274..355
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 356..380
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 381..387
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 388..408
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 409..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 752..770
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 771..781
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 782..801
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 802..815
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 816..835
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 836..837
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 838..855
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 856..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 872..890
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 891..919
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 920..940
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 941..953
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 954..974
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 975..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1198..1215
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1216..1228
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1229..1247
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1248..1261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1262..1280
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1281..1288
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1289..1307
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1308..1324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1325..1344
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1345..1397
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1398..1419
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1420..1436
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1437..1458
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1459..1521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1522..1539
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1540..1550
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1551..1569
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1570..1581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1582..1599
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1600..1612
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1613..1629
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1630..1648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1649..1666
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1667..1688
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1689..1711
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1712..1740
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1741..1763
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1764..1978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 114..442
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 733..1005
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1178..1493
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1502..1799
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1893..1922
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1923..1978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1948..1978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 371
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQD0"
FT BINDING 373
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQD0"
FT BINDING 891..898
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 937
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQD0"
FT BINDING 1411
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQD0"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1495
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 281..333
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 902
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 902
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 904..910
FT /evidence="ECO:0000250|UniProtKB:Q9UQD0"
FT DISULFID 942..951
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 1354..1374
FT /evidence="ECO:0000250|UniProtKB:Q9UQD0"
FT DISULFID 1719..1734
FT /evidence="ECO:0000250|UniProtKB:Q9UQD0"
FT VAR_SEQ 664
FT /note="E -> EVKIDKAATDS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9603190"
FT /id="VSP_038652"
SQ 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
//
