ID   SCNAA_MOUSE             Reviewed;        1958 AA.
AC   Q6QIY3; Q62243; Q6EWG7; Q6KCH7; Q703F9;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Sodium channel protein type 10 subunit alpha;
DE   AltName: Full=Peripheral nerve sodium channel 3;
DE            Short=PN3;
DE   AltName: Full=Sensory neuron sodium channel;
DE   AltName: Full=Sodium channel protein type X subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.8;
GN   Name=Scn10a {ECO:0000312|MGI:MGI:108029}; Synonyms=Sns;
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 [GENOMIC DNA / MRNA] OF 943-1090 (ISOFORMS 1 AND 2).
RC   STRAIN=129P2; TISSUE=Spinal ganglion, and Trigeminal ganglion;
RX   PubMed=15047701; DOI=10.1074/jbc.m401281200;
RA   Kerr N.C.H., Holmes F.E., Wynick D.;
RT   "Novel isoforms of the sodium channels Nav1.8 and Nav1.5 are produced by a
RT   conserved mechanism in mouse and rat.";
RL   J. Biol. Chem. 279:24826-24833(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 3).
RC   STRAIN=C3H/HeJ;
RA   Jover E., Shah V.;
RT   "Mouse sodium channel clone BC in pSB+.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC   STRAIN=CD-1; TISSUE=Spinal ganglion;
RA   Puhl H.L. III, King M.M., Ikeda S.R.;
RT   "cDNA cloning of the mouse sensory neuron specific sodium channel Nav1.8
RT   (Scn10a).";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH NEDD4 AND NEDD4L, PROBABLE UBIQUITINATION, AND MUTAGENESIS
RP   OF TYR-1922.
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, TRANSPORTER ACTIVITY, AND MUTAGENESIS OF GLN-861.
RX   PubMed=24159039; DOI=10.1126/science.1236451;
RA   Rowe A.H., Xiao Y., Rowe M.P., Cummins T.R., Zakon H.H.;
RT   "Voltage-gated sodium channel in grasshopper mice defends against bark
RT   scorpion toxin.";
RL   Science 342:441-446(2013).
CC   -!- FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-
CC       dependent sodium ion permeability of excitable membranes. Assuming
CC       opened or closed conformations in response to the voltage difference
CC       across the membrane, the protein forms a sodium-selective channel
CC       through which sodium ions may pass in accordance with their
CC       electrochemical gradient. Plays a role in neuropathic pain mechanisms.
CC       {ECO:0000269|PubMed:24159039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:24159039};
CC   -!- SUBUNIT: The channel consists of an ion conducting pore forming alpha-
CC       subunit regulated by one or more associated auxiliary subunits SCN1B,
CC       SCN2B and SCN3B; electrophysiological properties may vary depending on
CC       the type of the associated beta subunits. Found in a number of
CC       complexes with PRX, DYNLT1 and PDZD2. Interacts with proteins such as
CC       FSTL1, PRX, DYNLT1, PDZD2, S100A10 and many others (By similarity).
CC       Interacts with NEDD4 and NEDD4L. {ECO:0000250,
CC       ECO:0000269|PubMed:15123669}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Note=It can
CC       be translocated to the cell membrane through association with S100A10.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6QIY3-1; Sequence=Displayed;
CC       Name=2; Synonyms=Nav1.8c;
CC         IsoId=Q6QIY3-2; Sequence=VSP_012257;
CC       Name=3;
CC         IsoId=Q6QIY3-3; Sequence=VSP_012256;
CC   -!- TISSUE SPECIFICITY: Expressed in dorsal root ganglion and trigeminal
CC       ganglion.
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 promotes its endocytosis.
CC       {ECO:0000305}.
CC   -!- PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and reduces
CC       peak sodium currents. {ECO:0000250}.
CC   -!- PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ.
CC       This cysteine (position 815) is speculated in other sodium channel
CC       subunits alpha to be implied in covalent binding with the sodium
CC       channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}.
CC   -!- MISCELLANEOUS: Mus musculus is sensitive to the pain-inducing
CC       components of the bark scorpion (Centruroides sculpturatus) venom while
CC       Onychomys torridus is not. Gln-861 may account for the difference
CC       between both rodents and its replacement by a glutamate, the
CC       corresponding amino acid found in the Onychomys torridus ortholog,
CC       allows inhibition of Snc10a by the venom, which in turn, inhibits
CC       sodium currents, blocks action potential propagation and may induce
CC       analgesia (PubMed:24159039). {ECO:0000305|PubMed:24159039}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.8/SCN10A subfamily. {ECO:0000305}.
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DR   EMBL; AJ622906; CAF22039.1; -; Genomic_DNA.
DR   EMBL; AJ623269; CAF25039.1; -; mRNA.
DR   EMBL; AJ623270; CAF25040.1; -; mRNA.
DR   EMBL; L42342; AAA68000.1; -; mRNA.
DR   EMBL; AY538273; AAS45602.1; -; mRNA.
DR   CCDS; CCDS57716.1; -. [Q6QIY3-1]
DR   CCDS; CCDS90682.1; -. [Q6QIY3-2]
DR   RefSeq; NP_033160.2; NM_009134.3. [Q6QIY3-2]
DR   RefSeq; XP_017168712.1; XM_017313223.1. [Q6QIY3-1]
DR   AlphaFoldDB; Q6QIY3; -.
DR   SMR; Q6QIY3; -.
DR   BioGRID; 203097; 8.
DR   STRING; 10090.ENSMUSP00000081845; -.
DR   BindingDB; Q6QIY3; -.
DR   ChEMBL; CHEMBL5158; -.
DR   GlyCosmos; Q6QIY3; 9 sites, No reported glycans.
DR   GlyGen; Q6QIY3; 9 sites.
DR   iPTMnet; Q6QIY3; -.
DR   PhosphoSitePlus; Q6QIY3; -.
DR   PaxDb; 10090-ENSMUSP00000081845; -.
DR   ProteomicsDB; 256752; -. [Q6QIY3-1]
DR   ProteomicsDB; 256753; -. [Q6QIY3-2]
DR   ProteomicsDB; 256754; -. [Q6QIY3-3]
DR   ABCD; Q6QIY3; 1 sequenced antibody.
DR   Antibodypedia; 28790; 266 antibodies from 29 providers.
DR   DNASU; 20264; -.
DR   Ensembl; ENSMUST00000213392.2; ENSMUSP00000148987.2; ENSMUSG00000034533.11. [Q6QIY3-2]
DR   GeneID; 20264; -.
DR   KEGG; mmu:20264; -.
DR   UCSC; uc009sbf.2; mouse. [Q6QIY3-3]
DR   UCSC; uc009sbg.3; mouse. [Q6QIY3-2]
DR   AGR; MGI:108029; -.
DR   CTD; 6336; -.
DR   MGI; MGI:108029; Scn10a.
DR   VEuPathDB; HostDB:ENSMUSG00000034533; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000154992; -.
DR   InParanoid; Q6QIY3; -.
DR   OrthoDB; 1110761at2759; -.
DR   PhylomeDB; Q6QIY3; -.
DR   BioGRID-ORCS; 20264; 1 hit in 78 CRISPR screens.
DR   PRO; PR:Q6QIY3; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q6QIY3; Protein.
DR   Bgee; ENSMUSG00000034533; Expressed in dorsal root ganglion and 15 other cell types or tissues.
DR   ExpressionAtlas; Q6QIY3; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0044299; C:C-fiber; IDA:MGI.
DR   GO; GO:0071439; C:clathrin complex; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0099508; F:voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR   GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; IBA:GO_Central.
DR   GO; GO:0086016; P:AV node cell action potential; ISO:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR   GO; GO:0086043; P:bundle of His cell action potential; ISO:MGI.
DR   GO; GO:0061337; P:cardiac conduction; 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:0051649; P:establishment of localization in cell; IDA:MGI.
DR   GO; GO:0086010; P:membrane depolarization during action potential; ISS:UniProtKB.
DR   GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR   GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IMP:MGI.
DR   GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:MGI.
DR   GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR   GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; ISO:MGI.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IDA:MGI.
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; IPR001696; Na_channel_asu.
DR   InterPro; IPR044564; Na_chnl_inactivation_gate.
DR   InterPro; IPR010526; Na_trans_assoc_dom.
DR   InterPro; IPR043203; VGCC_Ca_Na.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF208; SODIUM CHANNEL PROTEIN TYPE 10 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   PRINTS; PR00170; NACHANNEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT   CHAIN           1..1958
FT                   /note="Sodium channel protein type 10 subunit alpha"
FT                   /id="PRO_0000048508"
FT   TOPO_DOM        1..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        126..149
FT                   /note="Helical; Name=S1 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..154
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        155..174
FT                   /note="Helical; Name=S2 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..187
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        188..206
FT                   /note="Helical; Name=S3 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..212
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        213..232
FT                   /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..248
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        249..272
FT                   /note="Helical; Name=S5 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..340
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        341..365
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        366..372
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        373..398
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..658
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        659..683
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        684..694
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        695..718
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        719..726
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        727..746
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        747..752
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        753..772
FT                   /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        773..788
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        789..809
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        810..833
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        834..854
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        855..863
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        864..889
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        890..1148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1149..1172
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1173..1185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1186..1211
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1212..1217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1218..1239
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1240..1243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1244..1265
FT                   /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1266..1284
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1285..1312
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1313..1354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1355..1376
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1377..1392
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1393..1419
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1420..1472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1473..1496
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1497..1507
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1508..1531
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1532..1537
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1538..1561
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1562..1573
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1574..1595
FT                   /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1596..1610
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1611..1633
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1634..1647
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1648..1670
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1671..1698
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1699..1723
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1724..1958
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REPEAT          116..404
FT                   /note="I"
FT                   /evidence="ECO:0000305"
FT   REPEAT          646..910
FT                   /note="II"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1141..1450
FT                   /note="III"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1459..1758
FT                   /note="IV"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1852..1881
FT                   /note="IQ"
FT   REGION          27..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1006..1094
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1901..1958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1042
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1076
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1907..1945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         611
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         614
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         1452
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1687
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        276..318
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   DISULFID        856..865
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   VAR_SEQ         1..1435
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_012256"
FT   VAR_SEQ         1030
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15047701"
FT                   /id="VSP_012257"
FT   MUTAGEN         861
FT                   /note="Q->E: Sensitive to inhibition by some components of
FT                   the venom of Centruroides sculpturatus."
FT                   /evidence="ECO:0000269|PubMed:24159039"
FT   MUTAGEN         1922
FT                   /note="Y->A: No regulation by NEDD4L."
FT                   /evidence="ECO:0000269|PubMed:15123669"
SQ   SEQUENCE   1958 AA;  220552 MW;  24830634E86490FF CRC64;
     MEFPFGSVGT TNFRRFTPES LAEIEKQIAA HRAAKKGRPK QRGQKDKSEK PRPQLDLKAC
     NQLPRFYGEL PAELVGEPLE DLDPFYSTHR TFIVLDKSRT ISRFSATWAL WLFSPFNLIR
     RTAIKVSVHS WFSIFITVTI LVNCVCMTRT DLPEKLEYAF TVVYTFEALI KILARGFCLN
     EFTYLRDPWN WLDFSVITLA YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
     HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCIKNG TDPHKADNLS SEMAGDIFIK
     PGTTDPLLCG NGSDAGHCPN DYVCRKTSDN PDFNYTSFDS FAWAFLSLFR LMTQDSWERL
     YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQSQATIAEI EAKEKKFKEA
     LEVLQKEQEV LAALGIDTTS LYSHNGSPLA PKNANERRPR VKSRMSEGST DDNRSLQSDP
     YNQRRMSFLG LSSGRRRASH SSVFHFRAPS QDVSFPDGIL DDGVFHGDQE SRRSSILLGR
     GAGQAGPLPR SPLPQSPNPG PRRGEEGQRG VPTGELATGA PEGPALDAAG QKNFLSADYL
     NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISLAQK YLIWECCPKW KKFKMVLFEL
     VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN IVFTVFFTME MAFKIIAFDP
     YYYFQKKWNI FDCVIVTVSL LELSTSKKGS LSVLRTFRLL RVFKLAKSWP TLNMLIKIIG
     NSVGALGNLT FILAIIVFIF ALVGKQLLSE NYGCRRDGIS VWNGERLRWH MCDFFHSFLV
     VFRILCGEWI ENMWVCMEVS QDYICLTLFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP
     EDDGEVNNLQ VALARIQVFG HRASRAITSY IRSHCRLRWP KVETQLGMKP PLTSCKAENH
     IATDAVNAAV GNLAKPALGG PKENHGDFIT DPNVWVSVPI AEGESDLDEL EEDVEHASQS
     SWQEESPKGQ QELLQQVQKC EDHQAARSPP SGMSSEDLAP YLGERWQREE SPRVPAEGVD
     DTSSSEGSTV DCPDPEEILR KIPELAEELD EPDDCFPEGC TRRCPCCKVN TSKFPWATGW
     QVRKTCYRIV EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF
     EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL RTLRALRPLR
     ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFSR CVDTRSNPFS
     VVNSTFVTNK SDCYNQNNTG HFFWVNVKVN FDNVAMGYLA LLQVATFKGW MDIMYAAVDS
     RDINSQPNWE ESLYMYLYFV VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ
     KKYYNAMKKL GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMALICLN MITMMVETDN
     QSEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL SISSLLFSAI
     LSSLESYFSP TLLRVIRLAR IGRILRLIRA AKGIRTLLFA LMMSLPALFN IGLLLFLVMF
     IYSIFGMASF ANVIDEAGID DMFNFKTFGN SMLCLFQITT SAGWDGLLSP ILNTGPPYCD
     PNRPNSNGSK GNCGSPAVGI LFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED
     DFDMFYETWE KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH
     CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRCK QEDISATIIQ
     KAYRNYMLQR SLMLSNPLHV PRAEEDGVSL PREGYVTFMA NDNGGLPDKS ETASATSFPP
     SYDSVTRGLS DRANISTSSS MQNEDEVTAK EGKSPGPQ
//