ID   SCN5A_MOUSE             Reviewed;        2019 AA.
AC   Q9JJV9; E9Q1D2; Q3UH91;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 160.
DE   RecName: Full=Sodium channel protein type 5 subunit alpha;
DE   AltName: Full=Sodium channel protein cardiac muscle subunit alpha;
DE   AltName: Full=Sodium channel protein type V subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.5;
DE   AltName: Full=mH1;
GN   Name=Scn5a;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RX   PubMed=11834499; DOI=10.1152/ajpheart.00644.2001;
RA   Zimmer T., Bollensdorff C., Haufe V., Birch-Hirschfeld E., Benndorf K.;
RT   "Mouse heart Na+ channels: primary structure and function of two isoforms
RT   and alternatively spliced variants.";
RL   Am. J. Physiol. 282:H1007-H1017(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   [4]
RP   INTERACTION WITH SNTA1; SNTB1 AND SNTB2.
RX   PubMed=9412493; DOI=10.1523/jneurosci.18-01-00128.1998;
RA   Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
RA   Froehner S.C.;
RT   "Interaction of muscle and brain sodium channels with multiple members of
RT   the syntrophin family of dystrophin-associated proteins.";
RL   J. Neurosci. 18:128-137(1998).
RN   [5]
RP   PHOSPHORYLATION BY CAMK2D.
RX   PubMed=17124532; DOI=10.1172/jci26620;
RA   Wagner S., Dybkova N., Rasenack E.C., Jacobshagen C., Fabritz L.,
RA   Kirchhof P., Maier S.K., Zhang T., Hasenfuss G., Brown J.H., Bers D.M.,
RA   Maier L.S.;
RT   "Ca2+/calmodulin-dependent protein kinase II regulates cardiac Na+
RT   channels.";
RL   J. Clin. Invest. 116:3127-3138(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457; SER-484 AND SER-539, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   INTERACTION WITH FGF13.
RX   PubMed=21817159; DOI=10.1161/circresaha.111.247957;
RA   Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V., Puranam R.S.,
RA   Rosenberg P.B., Bursac N., Pitt G.S.;
RT   "Fibroblast growth factor homologous factor 13 regulates Na+ channels and
RT   conduction velocity in murine hearts.";
RL   Circ. Res. 109:775-782(2011).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23420830; DOI=10.1161/circep.111.000206;
RA   Chakrabarti S., Wu X., Yang Z., Wu L., Yong S.L., Zhang C., Hu K.,
RA   Wang Q.K., Chen Q.;
RT   "MOG1 rescues defective trafficking of Na(v)1.5 mutations in Brugada
RT   syndrome and sick sinus syndrome.";
RL   Circ. Arrhythm. Electrophysiol. 6:392-401(2013).
RN   [9]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-526, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: This protein mediates the voltage-dependent sodium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a sodium-selective channel through which
CC       Na(+) ions may pass in accordance with their electrochemical gradient
CC       (PubMed:11834499, PubMed:23420830). It is a tetrodotoxin-resistant
CC       Na(+) channel isoform. This channel is responsible for the initial
CC       upstroke of the action potential. Channel inactivation is regulated by
CC       intracellular calcium levels (By similarity).
CC       {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:11834499,
CC       ECO:0000269|PubMed:23420830}.
CC   -!- SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1
CC       and SNTB2 (PubMed:9412493). Interacts with NEDD4, NEDD4L, WWP2 and
CC       GPD1L (By similarity). Interacts with CALM (By similarity). Interacts
CC       with FGF13; the interaction is direct and may regulate SNC5A density at
CC       membranes and function (PubMed:21817159). Interacts with FGF12 and
CC       FGF14 (By similarity). Interacts with ANK3 (By similarity). Interacts
CC       with PKP2 (via N-terminus) (By similarity). Interacts with TMEM233 (By
CC       similarity). {ECO:0000250|UniProtKB:P15389,
CC       ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:21817159,
CC       ECO:0000269|PubMed:9412493}.
CC   -!- INTERACTION:
CC       Q9JJV9; Q4U4S6: Xirp2; NbExp=2; IntAct=EBI-8313814, EBI-10768169;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834499,
CC       ECO:0000269|PubMed:23420830}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule
CC       {ECO:0000250|UniProtKB:P15389}. Cell junction
CC       {ECO:0000250|UniProtKB:P15389}. Note=RANGRF promotes trafficking to the
CC       cell membrane. Colocalizes with PKP2 at intercalated disks in the heart
CC       (By similarity). {ECO:0000250|UniProtKB:P15389,
CC       ECO:0000269|PubMed:23420830}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q9JJV9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JJV9-2; Sequence=VSP_037444;
CC   -!- TISSUE SPECIFICITY: Expressed in the myocardium.
CC       {ECO:0000269|PubMed:11834499}.
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   -!- DOMAIN: The IQ domain mediates association with calmodulin.
CC       {ECO:0000250|UniProtKB:Q14524}.
CC   -!- PTM: Phosphorylation at Ser-1505 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and reduces
CC       peak sodium currents (By similarity). Regulated through phosphorylation
CC       by CaMK2D (PubMed:17124532). {ECO:0000250|UniProtKB:Q14524,
CC       ECO:0000269|PubMed:17124532}.
CC   -!- PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. Does not
CC       seem to be ubiquitinated by NEDD4 or WWP2.
CC       {ECO:0000250|UniProtKB:Q14524}.
CC   -!- PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ.
CC       This cysteine (position 868) 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   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.5/SCN5A subfamily. {ECO:0000305}.
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DR   EMBL; AJ271477; CAB70096.1; -; mRNA.
DR   EMBL; AK147254; BAE27800.1; -; mRNA.
DR   EMBL; AK147517; BAE27966.1; -; mRNA.
DR   EMBL; AC121922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC171201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001240789.1; NM_001253860.1.
DR   RefSeq; NP_067519.2; NM_021544.4.
DR   AlphaFoldDB; Q9JJV9; -.
DR   BMRB; Q9JJV9; -.
DR   SMR; Q9JJV9; -.
DR   BioGRID; 203101; 14.
DR   DIP; DIP-46142N; -.
DR   IntAct; Q9JJV9; 4.
DR   MINT; Q9JJV9; -.
DR   STRING; 10090.ENSMUSP00000112838; -.
DR   BindingDB; Q9JJV9; -.
DR   ChEMBL; CHEMBL4630764; -.
DR   GlyCosmos; Q9JJV9; 13 sites, No reported glycans.
DR   GlyGen; Q9JJV9; 13 sites.
DR   iPTMnet; Q9JJV9; -.
DR   PhosphoSitePlus; Q9JJV9; -.
DR   CPTAC; non-CPTAC-4004; -.
DR   PaxDb; 10090-ENSMUSP00000112838; -.
DR   ProteomicsDB; 253414; -. [Q9JJV9-1]
DR   ProteomicsDB; 253415; -. [Q9JJV9-2]
DR   ABCD; Q9JJV9; 2 sequenced antibodies.
DR   Antibodypedia; 6411; 364 antibodies from 32 providers.
DR   DNASU; 20271; -.
DR   Ensembl; ENSMUST00000120420.2; ENSMUSP00000113272.2; ENSMUSG00000032511.18. [Q9JJV9-1]
DR   GeneID; 20271; -.
DR   KEGG; mmu:20271; -.
DR   UCSC; uc009sbc.2; mouse. [Q9JJV9-2]
DR   AGR; MGI:98251; -.
DR   CTD; 6331; -.
DR   MGI; MGI:98251; Scn5a.
DR   VEuPathDB; HostDB:ENSMUSG00000032511; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000161691; -.
DR   InParanoid; Q9JJV9; -.
DR   OrthoDB; 1110761at2759; -.
DR   TreeFam; TF323985; -.
DR   BioGRID-ORCS; 20271; 2 hits in 78 CRISPR screens.
DR   PRO; PR:Q9JJV9; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9JJV9; Protein.
DR   Bgee; ENSMUSG00000032511; Expressed in myocardium of ventricle and 114 other cell types or tissues.
DR   ExpressionAtlas; Q9JJV9; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0034706; C:sodium channel complex; IPI:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
DR   GO; GO:0030018; C:Z disc; ISO:MGI.
DR   GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR   GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR   GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR   GO; GO:0086060; F:voltage-gated sodium channel activity involved in AV node cell action potential; ISO:MGI.
DR   GO; GO:0086061; F:voltage-gated sodium channel activity involved in bundle of His cell action potential; ISO:MGI.
DR   GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; IMP:MGI.
DR   GO; GO:0086062; F:voltage-gated sodium channel activity involved in Purkinje myocyte action potential; ISO:MGI.
DR   GO; GO:0086063; F:voltage-gated sodium channel activity involved in SA node cell action potential; IMP:MGI.
DR   GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:0086016; P:AV node cell action potential; ISO:MGI.
DR   GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISO:MGI.
DR   GO; GO:0086043; P:bundle of His cell action potential; ISO:MGI.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR   GO; GO:0003231; P:cardiac ventricle development; IMP:MGI.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR   GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR   GO; GO:0086010; P:membrane depolarization during action potential; ISO:MGI.
DR   GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISO:MGI.
DR   GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISO:MGI.
DR   GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:MGI.
DR   GO; GO:0086046; P:membrane depolarization during SA node cell action potential; ISO:MGI.
DR   GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR   GO; GO:0045760; P:positive regulation of action potential; ISO:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR   GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR   GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; ISO:MGI.
DR   GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:MGI.
DR   GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:MGI.
DR   GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:MGI.
DR   GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; ISO:MGI.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
DR   GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISO:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; IMP:MGI.
DR   GO; GO:0086015; P:SA node cell action potential; ISO:MGI.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IDA:MGI.
DR   GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR   GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO: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; IPR008053; Na_channel_a5su.
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:SF206; SODIUM CHANNEL PROTEIN TYPE 5 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   PRINTS; PR01666; NACHANNEL5.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   Genevisible; Q9JJV9; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Cell junction; Cell membrane;
KW   Cytoplasm; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Membrane; Methylation; Phosphoprotein; Reference proteome; Repeat; Sodium;
KW   Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation; Voltage-gated channel.
FT   CHAIN           1..2019
FT                   /note="Sodium channel protein type 5 subunit alpha"
FT                   /id="PRO_0000376895"
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:D0E0C2"
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:D0E0C2"
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:D0E0C2"
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:D0E0C2"
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:D0E0C2"
FT   TOPO_DOM        273..357
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        358..382
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        383..389
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        390..410
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        411..717
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        718..736
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        737..747
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        748..767
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        768..781
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        782..801
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        802..803
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        804..821
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        822..837
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        838..856
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        857..885
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        886..906
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        907..919
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        920..940
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        941..1208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1209..1226
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1227..1239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1240..1258
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1259..1272
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1273..1291
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1292..1299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1300..1318
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1319..1335
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1336..1355
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1356..1407
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1408..1429
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1430..1446
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1447..1468
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1469..1531
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1532..1549
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1550..1560
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1561..1579
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1580..1591
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1592..1609
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1610..1622
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1623..1639
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1640..1658
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1659..1676
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1677..1698
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1699..1721
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1722..1750
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1751..1773
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1774..2019
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REPEAT          113..420
FT                   /note="I"
FT                   /evidence="ECO:0000305"
FT   REPEAT          699..971
FT                   /note="II"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1189..1503
FT                   /note="III"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1512..1809
FT                   /note="IV"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1903..1932
FT                   /note="IQ"
FT   REGION          27..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1000..1144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1841..1903
FT                   /note="Interaction with FGF13"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   REGION          1963..2019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1977..1980
FT                   /note="Interaction with NEDD4, NEDD4L and WWP2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   COMPBIAS        480..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1039
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1071
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1963..1995
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         38
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         457
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         460
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         484
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         486
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15389"
FT   MOD_RES         497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         526
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         526
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         539
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         664
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         1505
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
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        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        740
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        803
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        864
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        280..335
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   DISULFID        908..917
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   VAR_SEQ         206..211
FT                   /note="TTEFVD -> VSENIK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_037444"
FT   CONFLICT        215
FT                   /note="V -> L (in Ref. 2; BAE27966/BAE27800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="S -> P (in Ref. 2; BAE27966/BAE27800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1008..1009
FT                   /note="AA -> TT (in Ref. 1; CAB70096)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1078
FT                   /note="K -> KQ (in Ref. 2; BAE27966/BAE27800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1133
FT                   /note="T -> S (in Ref. 1; CAB70096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2019 AA;  227576 MW;  5A3BC3C191859E79 CRC64;
     MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSATSQ ESREGLPEEE APRPQLDLQA
     SKKLPDLYGN PPRELIGEPL EDLDPFYSTQ KTFIVLNKGK TIFRFSATNA LYVLSPFHPV
     RRAAVKILVH SLFSMLIMCT ILTNCVFMAQ HDPPPWTKYV EYTFTAIYTF ESLVKILARG
     FCLHAFTFLR DPWNWLDFSV IVMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV
     GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTELNGT NGSVEADGIV
     WNSLDVYLND PANYLLKNGT TDVLLCGNSS DAGTCPEGYR CLKAGENPDH GYTSFDSFAW
     AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN
     QATIAETEEK EKRFQEAMEM LKKEHEALTI RGVDTVSRSS LEMSPLAPVT NHERRSKRRK
     RLSSGTEDGG DDRLPKSDSE DGPRALNQLS LTHGLSRTSM RPRSSRGSIF TFRRRDQGSE
     ADFADDENST AGESESHRTS LLVPWPLRRP STQGQPGFGT SAPGHVLNGK RNSTVDCNGV
     VSLLGAGDAE ATSPGSHLLR PIVLDRPPDT TTPSEEPGGP QMLTPQAPCA DGFEEPGARQ
     RALSAVSVLT SALEELEESH RKCPPCWNRF AQHYLIWECC PLWMSIKQKV KFVVMDPFAD
     LTITMCIVLN TLFMALEHYN MTAEFEEMLQ VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG
     WNIFDSIIVI LSLMELGLSR MGNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG
     NLTLVLAIIV FIFAVVGMQL FGKNYSELRH RISDSGLLPR WHMMDFFHAF LIIFRILCGE
     WIETMWDCME VSGQSLCLLV FLLVMVIGNL VVLNLFLALL LSSFSADNLT APDEDGEMNN
     LQLALARIQR GLRFVKRTTW DFCCGLLRRR PKKPAALATH SQLPSCIAAP RSPPPPEVEK
     APPARKETRF EEDKRPGQGT PGDTEPVCVP IAVAESDTDD QEEDEENSLG TEEEESSKQE
     SQVVSGGHEP PQEPRAWSQV SETTSSEAEA STSQADWQQE REAEPRAPGC GETPEDSYSE
     GSTADMTNTA DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQAPG KVWWRLRKTC
     YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY VFVLEMLLKW
     VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP IKSLRTLRAL RPLRALSRFE
     GMRVVVNALV GAIPSIMNVL LVCLIFWLIF SIMGVNLFAG KFGRCINQTE GDLPLNYTIV
     NNKSECESFN VTGELYWTKV KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP
     QWEDNLYMYI YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM
     KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE TDDQSPEKVN
     ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV VILSIVGTVL SDIIQKYFFS
     PTLFRVIRLA RIGRILRLIR GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIYSIFGMAN
     FAYVKWEAGI DDMFNFQTFA NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS
     RGNCGSPAVG ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW
     EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI HCMDILFAFT
     KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR KHEEVSATVI QRAFRRHLLQ
     RSVKHASFLF RQQAGSSGLS DEDAPEREGL IAYMMNENFS RRSGPLSSSS ISSTSFPPSY
     DSVTRATSDN LPVRASDYSR SEDLADFPPS PDRDRESIV
//