Target Information

General Information of This Target
Target ID
BTDT00010
Target Name
Sodium channel protein type 9 subunit alpha (Scn9a)
Target Bioclass
Transporter and channel
Uniprot ID
O08562
3D Structure
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2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Scn9a
Gene ID
78956
Synonym
Peripheral sodium channel 1; Sodium channel protein type IX subunit alpha; Voltage-gated sodium channel subunit alpha Nav1.7
Sequence
MAMLPPPGPQSFVHFTKQSLALIEQRISEEKAKEHKDEKKDDEEEGPKPSSDLEAGKQLP
FIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKAIFRFNATPALYMLSPFSPLRRISI
KILVHSLFSMLIMCTILTNCIFMTLSNPPEWTKNVEYTFTGIYTFESLIKILARGFCVGE
FTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQ
SVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRKELEENETLESIMNTAESEEELK
KYFYYLEGSKDALLCGFSTDSGQCPEGYICVKAGRNPDYGYTSFDTFSWAFLALFRLMTQ
DYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKE
LEFQQMLDRLKKEQEEAEAIAAAAAEFTSIGRSRIMGLSESSSETSRLSSKSAKERRNRR
KKKKQKMSSGEEKGDDEKLSKSGSEESIRKKSFHLGVEGHHRTREKRLSTPNQSPLSIRG
SLFSARRSSRTSLFSFKGRGRDLGSETEFADDEHSIFGDNESRRGSLFVPHRPRERRSSN
ISQASRSPPVLPVNGKMHSAVDCNGVVSLVDGPSALMLPNGQLLPEVIIDKATSDDSGTT
NQMRKKRLSSSYFLSEDMLNDPHLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHTF
LIWNCSPYWIKFKKLIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTEEFKNVLAVGNL
IFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLIELFLADVEGLSVLRSFRLLR
VFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINV
DCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVYMMVMVIGNLVVLN
LFLALLLSSFSSDNLTAIEEDTDANNLQIAVARIKRGINYVKQTLREFILKSFSKKPKGS
KDTKRTADPNNKKENYISNRTLAEMSKDHNFLKEKDRISGYGSSLDKSFMDENDYQSFIH
NPSLTVTVPIAPGESDLEIMNTEELSSDSDSDYSKEKRNRSSSSECSTVDNPLPGEEEAE
AEPVNADEPEACFTDGCVRRFPCCQVNVDSGKGKVWWTIRKTCYRIVEHSWFESFIVLMI
LLSSGALAFEDIYIEKKKTIKIILEYADKIFTYIFILEMLLKWVAYGYKTYFTNAWCWLD
FLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPSIM
NVLLVCLIFWLIFSIMGVNLFAGKFYECVNTTDGSRFPTSQVANRSECFALMNVSGNVRW
KNLKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSVNVNEQPKYEYSLYMYIYFVIFII
FGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGN
KFQGCIFDLVTNQAFDITIMVLICLNMVTMMVEKEGQTEYMDYVLHWINMVFIILFTGEC
VLKLISLRHYYFTVGWNIFDFVVVILSIVGMFLAEMIEKYFVSPTLFRVIRLARIGRILR
LIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGINDMFNFE
TFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPKKVHPGSSVEGDCGNPSVGIFYFVS
YIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFCKL
SDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGEGGEMDSLRSQ
MEERFMSANPSKVSYEPITTTLKRKQEEVSATIIQRAYRRYRLRQHVKNISSIYIKDGDR
DDDLPNKEDTVFDNVNENSSPEKTDVTASTISPPSYDSVTKPDQEKYETDKTEKEDKEKD
ESRK

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Family
the sodium channel (TC 1.A.1.10) family
Function
Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin- sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain.

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Taxonomy ID
10116
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Rattus
Species: Rattus norvegicus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Mu-conotoxin SmIIIA Dissociation constant
260 nM
 [1- 5]
 Toxin Info    Mu-conotoxin SrVA Inhibition rate
7 %
 [6], [7], [8]
 Toxin Info    Kappa-actitoxin-Avd4a Effective concentration 50
300 nM
 [9- 13]
 Toxin Info    DeltaKappa-actitoxin-Avd4b Effective concentration 50
300 nM
 [14], [15], [12]
 Toxin Info    Delta-conotoxin PVIA Effective concentration 50
6.4 μM
 [16], [17], [18], [19]
 Toxin Info    Mu-conotoxin MrVIA IC50
345 nM
 [18- 24]
 Toxin Info    Mu-conotoxin PIIIA IC50
>100 μM
 [2- 29]
 Toxin Info    PnCS2 IC50
0.9 ± 0.1 μM
 [30]
 Toxin Info    Mu-conotoxin SmIIIA IC50
1.3 μM
 [1- 5]
 Toxin Info    PnCS4 IC50
3.1 ± 0.2 μM
 [30]
 Toxin Info    PnCS3 IC50
5.7 ± 0.2 μM
 [30]
References
Ref 1 Mu-conotoxin SmIIIA, a potent inhibitor of tetrodotoxin-resistant sodium channels in amphibian sympathetic and sensory neurons. Biochemistry. 2002 Dec 24;41(51):15388-93. doi: 10.1021/bi0265628.
Ref 2 -Conotoxins that differentially block sodium channels NaV1.1 through 1.8 identify those responsible for action potentials in sciatic nerve. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10302-7. doi: 10.1073/pnas.1107027108. Epub 2011 Jun 7.
Ref 3 A novel -conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors. Br J Pharmacol. 2012 Jul;166(5):1654-68. doi: 10.1111/j.1476-5381.2012.01837.x.
Ref 4 Co-expression of Na(V) subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking -conotoxins. Br J Pharmacol. 2013 Apr;168(7):1597-610. doi: 10.1111/bph.12051.
Ref 5 Structural basis for tetrodotoxin-resistant sodium channel binding by mu-conotoxin SmIIIA. J Biol Chem. 2003 Nov 21;278(47):46805-13. doi: 10.1074/jbc.M309222200. Epub 2003 Sep 10.
Ref 6 Identification, by RT-PCR, of four novel T-1-superfamily conotoxins from the vermivorous snail Conus spurius from the Gulf of Mexico. Peptides. 2009 Aug;30(8):1396-404. doi: 10.1016/j.peptides.2009.05.003. Epub 2009 May 15.
Ref 7 A biologically active hydrophobic T-1-conotoxin from the venom of Conus spurius. Peptides. 2006 Mar;27(3):500-5. doi: 10.1016/j.peptides.2005.07.020. Epub 2005 Nov 16.
Ref 8 The T-1 conotoxin -SrVA from the worm hunting marine snail Conus spurius preferentially blocks the human Na(V)1.5 channel. Peptides. 2022 Oct;156:170859. doi: 10.1016/j.peptides.2022.170859. Epub 2022 Aug 5.
Ref 9 Comprehensive EST analysis of the symbiotic sea anemone, Anemonia viridis. BMC Genomics. 2009 Jul 23;10:333. doi: 10.1186/1471-2164-10-333.
Ref 10 A Low Molecular Weight Protein from the Sea Anemone Anemonia viridis with an Anti-Angiogenic Activity. Mar Drugs. 2018 Apr 19;16(4):134. doi: 10.3390/md16040134.
Ref 11 The mining of toxin-like polypeptides from EST database by single residue distribution analysis. BMC Genomics. 2011 Jan 31;12:88. doi: 10.1186/1471-2164-12-88.
Ref 12 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 13 Evidence of accelerated evolution and ectodermal-specific expression of presumptive BDS toxin cDNAs from Anemonia viridis. Mar Drugs. 2013 Oct 30;11(11):4213-31. doi: 10.3390/md11114213.
Ref 14 Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J Biol Chem. 1998 Mar 20;273(12):6744-9. doi: 10.1074/jbc.273.12.6744.
Ref 15 Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies. J Neurosci. 2005 Sep 21;25(38):8735-45. doi: 10.1523/JNEUROSCI.2119-05.2005.
Ref 16 Purification, characterization, synthesis, and cloning of the lockjaw peptide from Conus purpurascens venom. Biochemistry. 1995 Apr 18;34(15):4913-8. doi: 10.1021/bi00015a002.
Ref 17 Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 1996 May 9;381(6578):148-51. doi: 10.1038/381148a0.
Ref 18 Distinction among neuronal subtypes of voltage-activated sodium channels by mu-conotoxin PIIIA. J Neurosci. 2000 Jan 1;20(1):76-80. doi: 10.1523/JNEUROSCI.20-01-00076.2000.
Ref 19 Delta-conotoxin structure/function through a cladistic analysis. Biochemistry. 2001 Nov 6;40(44):13201-8. doi: 10.1021/bi010683a.
Ref 20 Diversity and evolution of conotoxins in Conus virgo, Conus eburneus, Conus imperialis and Conus marmoreus from the South China Sea. Toxicon. 2012 Nov;60(6):982-9. doi: 10.1016/j.toxicon.2012.06.011. Epub 2012 Jul 7.
Ref 21 New sodium channel-blocking conotoxins also affect calcium currents in Lymnaea neurons. Biochemistry. 1995 Apr 25;34(16):5364-71. doi: 10.1021/bi00016a007.
Ref 22 A new family of conotoxins that blocks voltage-gated sodium channels. J Biol Chem. 1995 Jul 14;270(28):16796-802. doi: 10.1074/jbc.270.28.16796.
Ref 23 MicroO-conotoxin MrVIA inhibits mammalian sodium channels, but not through site I. J Neurophysiol. 1996 Sep;76(3):1423-9. doi: 10.1152/jn.1996.76.3.1423.
Ref 24 The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3. FEBS Lett. 2006 Feb 20;580(5):1360-4. doi: 10.1016/j.febslet.2006.01.057. Epub 2006 Jan 26.
Ref 25 Definition of the M-conotoxin superfamily: characterization of novel peptides from molluscivorous Conus venoms. Biochemistry. 2005 Jun 7;44(22):8176-86. doi: 10.1021/bi047541b.
Ref 26 mu-Conotoxin PIIIA, a new peptide for discriminating among tetrodotoxin-sensitive Na channel subtypes. J Neurosci. 1998 Jun 15;18(12):4473-81. doi: 10.1523/JNEUROSCI.18-12-04473.1998.
Ref 27 Pruning nature: Biodiversity-derived discovery of novel sodium channel blocking conotoxins from Conus bullatus. Toxicon. 2009 Jan;53(1):90-8. doi: 10.1016/j.toxicon.2008.10.017. Epub 2008 Nov 20.
Ref 28 Structurally diverse -conotoxin PIIIA isomers block sodium channel NaV 1.4. Angew Chem Int Ed Engl. 2012 Apr 23;51(17):4058-61. doi: 10.1002/anie.201107011. Epub 2012 Mar 12.
Ref 29 Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels. J Biol Chem. 2002 Jul 26;277(30):27247-55. doi: 10.1074/jbc.M201611200. Epub 2002 May 2.
Ref 30 Where cone snails and spiders meet: design of small cyclic sodium-channel inhibitors. FASEB J. 2019 Mar;33(3):3693-3703. doi: 10.1096/fj.201801909R. Epub 2018 Dec 3.
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