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0SCN4A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSCN4A
DescriptionSodium channel protein type iv alpha subunit (voltage-gated sodium channel alpha subunit nav1.4) (sodium channel protein, skeletal muscle alpha-subunit) (skm1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005248 voltage-gated sodium channel activity (TAS)
0006936 muscle contraction (TAS)
0006814 sodium ion transport (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Members of this entry contain a region found exclusively in eukaryotic sodium channels or their subunits.any of which are voltage-gated. Members very often also contain between one and four copies of and.ess often.ne copy of .
  IPR010526:Sodium ion transport-associated
This group of proteins is found in sodium.otassium.nd calcium ion channels proteins. The proteins have 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some Na channels proteins the domain is repeated four times.hereas in others (e.g. K channels) the protein forms a tetramer in the membrane. A bacterial structure of the protein is known for the last two helices but is not included in the Pfam family due to it lacking the first four helices.
  IPR005821:Ion transport
Calmodulin (CaM) is recognized as a major calcium sensor and orchestrator of regulatory events through its interaction with a diverse group of cellular proteins. Three classes of recognition motifs exist for many of the known CaM binding proteins; the IQ motif as a consensus for Ca2+-independent binding and two related motifs for Ca2+-dependent binding.ermed18-14 and 1-5-10 based on the position of conserved hydrophobic residues .The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca2+-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains.ccounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule .
  IPR000048:IQ calmodulin-binding region
Voltage-dependent sodium channels are transmembrane (TM) proteinsresponsible for the depolarising phase of the action potential in mostelectrically excitable cells . They may exist in 3 states : theresting state.here the channel is closed; the activated state.here thechannel is open; and the inactivated state.here the channel is closedand refractory to opening. Several different structurally and functionallydistinct isoforms are found in mammals.oded for by a multigene family.hese being responsible for the different types of sodium ion currentsfound in excitable tissues.The structure of sodium channels is based on 4 internal repeats of a 6-helixbundle (in which 5 of the membrane-spanning segments are hydrophobic andthe other is positively charged).orming a 24-helical bundle. The chargedsegments are believed to be localised within clusters formed by their 5 hydrophobic neighbours: it is postulated that the charged domain may be thevoltage sensor region.ossibly moving outward on depolarisation.ausing aconformational change. This model.roposed by Noda et al. .ontrastswith that of Sato and Matsumoto .n which the TM segments are juxtaposedoctagonally. The basic structural motif (the 6-helix bundle) is also found in potassium and calcium channel alpha subunits.Cation channels are transport proteins responsible for the movement of cations through the membrane. These proteins contain 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times.hereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
  IPR001696:Na+ channel
Voltage-dependent sodium channels are transmembrane (TM) proteinsresponsible for the depolarising phase of the action potential in mostelectrically excitable cells . They may exist in 3 states : theresting state.here the channel is closed; the activated state.here thechannel is open; and the inactivated state.here the channel is closedand refractory to opening. Several different structurally and functionallydistinct isoforms are found in mammals.oded for by a multigene family.hese being responsible for the different types of sodium ion currentsfound in excitable tissues.The structure of sodium channels is based on 4 internal repeats of a 6-helixbundle (in which 5 of the membrane-spanning segments are hydrophobic andthe other is positively charged).orming a 24-helical bundle. The chargedsegments are believed to be localised within clusters formed by their 5 hydrophobic neighbours: it is postulated that the charged domain may be thevoltage sensor region.ossibly moving outward on depolarisation.ausing aconformational change. This model.roposed by Noda et al. .ontrastswith that of Sato and Matsumoto .n which the TM segments are juxtaposedoctagonally. The basic structural motif (the 6-helix bundle) is also found in potassium and calcium channel alpha subunits.The SCN4A gene belongs to the Nav1 family.hich also includes SCN1A.CN2A.CN3A.CN5A and SCN8A. This family is typically expressed in the brain.pinal cord.keletal muscle.ardiac muscle and peripheral neurons .Mutations in SCN4A are associated with hyperkalaemic periodic paralysis.aramyotonia congenita and a diverse group of disorders collectively knownas potassium-aggravated myotonia. These are characterised by skeletal musclehyperexcitability or muscle weakness.hich is exacerbated by exposure tocold temperature .
  IPR008052:Na+ channel 4
IPR010526:Na_trans_assoc 
Evalue:-132.36653137207 
Location:816-1041IPR005821:Ion_trans 
Evalue:-70.9208221435547 
Location:1067-1294IPR005821:Ion_trans 
Evalue:-70.5376052856445 
Location:159-446IPR005821:Ion_trans 
Evalue:-62.9586067199707 
Location:1387-1597IPR005821:Ion_trans 
Evalue:-61.2757225036621 
Location:612-801IPR000048:IQ 
Evalue:-2.25181198120117 
Location:1728-1748IPR008052:NACHANNEL4 
Evalue:0 
Location:1-21IPR008052:NACHANNEL4 
Evalue:0 
Location:515-534IPR008052:NACHANNEL4 
Evalue:0 
Location:496-511IPR008052:NACHANNEL4 
Evalue:0 
Location:478-492IPR001696:NACHANNEL 
Evalue:0 
Location:1615-1628
SequencesProtein: SCN4A_HUMAN (1836 aa)
mRNA: NM_000334
Local Annotation
Synapse Ontology
Na channel plays an important role in the course of action potential.
sdb:0287 Na channel  (Evidence:keywords)
KO assignmentK04837
  Level 3 annotation:
    sodium channel, voltage-gated, type IV, alpha
  Level 2 annotation:
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1147 residues, 59369645-59373085Exon2: 92 residues, 59373917-59374188Exon3: 37 residues, 59374837-59374942Exon4: 48 residues, 59375764-59375902Exon5: 20 residues, 59376098-59376152Exon6: 95 residues, 59376451-59376730Exon7: 43 residues, 59378136-59378259Exon8: 60 residues, 59378981-59379155Exon9: 53 residues, 59379702-59379857Exon10: 47 residues, 59380484-59380620Exon11: 161 residues, 59382515-59382992Exon12: 121 residues, 59388253-59388610Exon13: 60 residues, 59390356-59390530Exon14: 81 residues, 59392284-59392523Exon15: 53 residues, 59394763-59394917Exon16: 72 residues, 59395559-59395769Exon17: 49 residues, 59397193-59397335Exon18: 23 residues, 59397572-59397636Exon19: 113 residues, 59399114-59399447Exon20: 32 residues, 59402253-59402345Exon21: 45 residues, 59402813-59402942Exon22: 32 residues, 59403227-59403317Exon23: 41 residues, 59403443-59403562Exon24: 118 residues, 59403660-59404010Exon25: 2 residues, -Jump to SCN4A_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3027 58954426-58977332 ~-23K 16390(KCNH6)(+)Loci: 4309 59369645-59404010 ~-34K 16427(SCN4A)(-)Loci: 4308 58863397-58877277 ~-14K 16385(CYB561)(-)Link out to UCSC