Target Information

General Information of This Target
Target ID
BTDT00080
Target Name
Sodium channel protein para (para)
Target Bioclass
Transporter and channel
Uniprot ID
P35500
3D Structure
Download
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
para
Gene ID
32619
Synonym
Protein paralytic; Sodium channel 1
Sequence
MTEDSDSISEEERSLFRPFTRESLVQIEQRIAAEHEKQKELERKRAEGEVPQYGRKKKQK
EIRYDDEDEDEGPQPDPTLEQGVPIPVRLQGSFPPELASTPLEDIDPYYSNVLTFVVVSK
GKDIFRFSASKAMWMLDPFNPIRRVAIYILVHPLFSLFIITTILVNCILMIMPTTPTVES
TEVIFTGIYTFESAVKVMARGFILCPFTYLRDAWNWLDFVVIALAYVTMGIDLGNLAALR
TFRVLRALKTVAIVPGLKTIVGAVIESVKNLRDVIILTMFSLSVFALMGLQIYMGVLTQK
CIKKFPLDGSWGNLTDENWDYHNRNSSNWYSEDEGISFPLCGNISGAGQCDDDYVCLQGF
GPNPNYGYTSFDSFGWAFLSAFRLMTQDFWEDLYQLVLRAAGPWHMLFFIVIIFLGSFYL
VNLILAIVAMSYDELQKKAEEEEAAEEEAIREAEEAAAAKAAKLEERANAQAQAAADAAA
AEEAALHPEMAKSPTYSCISYELFVGGEKGNDDNNKEKMSIRSVEVESESVSVIQRQPAP
TTAHQATKVRKVSTTSLSLPGSPFNIRRGSRSSHKYTIRNGRGRFGIPGSDRKPLVLSTY
QDAQQHLPYADDSNAVTPMSEENGAIIVPVYYGNLGSRHSSYTSHQSRISYTSHGDLLGG
MAVMGVSTMTKESKLRNRNTRNQSVGATNGGTTCLDTNHKLDHRDYEIGLECTDEAGKIK
HHDNPFIEPVQTQTVVDMKDVMVLNDIIEQAAGRHSRASDRGVSVYYFPTEDDDEDGPTF
KDKALEVILKGIDVFCVWDCCWVWLKFQEWVSLIVFDPFVELFITLCIVVNTMFMAMDHH
DMNKEMERVLKSGNYFFTATFAIEATMKLMAMSPKYYFQEGWNIFDFIIVALSLLELGLE
GVQGLSVLRSFRLLRVFKLAKSWPTLNLLISIMGRTMGALGNLTFVLCIIIFIFAVMGMQ
LFGKNYHDHKDRFPDGDLPRWNFTDFMHSFMIVFRVLCGEWIESMWDCMYVGDVSCIPFF
LATVVIGNLVVLNLFLALLLSNFGSSSLSAPTADNDTNKIAEAFNRIGRFKSWVKRNIAD
CFKLIRNKLTNQISDQPSGERTNQISWIWSEGKGVCRCISAEHGDNELELGHDEILADGL
IKKGIKEQTQLEVAIGDGMEFTIHGDMKNNKPKKSKYLNNATDDDTASINSYGSHKNRPF
KDESHKGSAETMEGEEKRDASKEDLGLDEELDEEGECEEGPLDGDIIIHAHDEDILDEYP
ADCCPDSYYKKFPILAGDDDSPFWQGWGNLRLKTFQLIENKYFETAVITMILMSSLALAL
EDVHLPQRPILQDILYYMDRIFTVIFFLEMLIKWLALGFKVYFTNAWCWLDFVIVMVSLI
NFVASLVGAGGIQAFKTMRTLRALRPLRAMSRMQGMRVVVNALVQAIPSIFNVLLVCLIF
WLIFAIMGVQLFAGKYFKCEDMNGTKLSHEIIPNRNACESENYTWVNSAMNFDHVGNAYL
CLFQVATFKGWIQIMNDAIDSREVDKQPIRETNIYMYLYFVFFIIFGSFFTLNLFIGVII
DNFNEQKKKAGGSLEMFMTEDQKKYYNAMKKMGSKKPLKAIPRPRWRPQAIVFEIVTDKK
FDIIIMLFIGLNMFTMTLDRYDASDTYNAVLDYLNAIFVVIFSSECLLKIFALRYHYFIE
PWNLFDVVVVILSILGLVLSDIIEKYFVSPTLLRVVRVAKVGRVLRLVKGAKGIRTLLFA
LAMSLPALFNICLLLFLVMFIFAIFGMSFFMHVKEKSGINDVYNFKTFGQSMILLFQMST
SAGWDGVLDAIINEEACDPPDNDKGYPGNCGSATVGITFLLSYLVISFLIVINMYIAVIL
ENYSQATEDVQEGLTDDDYDMYYEIWQQFDPEGTQYIRYDQLSEFLDVLEPPLQIHKPNK
YKIISMDIPICRGDLMYCVDILDALTKDFFARKGNPIEETGEIGEIAARPDTEGYEPVSS
TLWRQREEYCARLIQHAWRKHKARGEGGGSFEPDTDHGDGGDPDAGDPAPDEATDGDAPA
GGDGSVNGTAEGAADADESNVNSPGEDAAAAAAAAAAAAAAGTTTAGSPGAGSAGRQTAV
LVESDGFVTKNGHKVVIHSRSPSITSRTADV

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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.

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Taxonomy ID
7227
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Kingdom: Metazoa
Phylum: Arthropoda
Class: Insecta
Order: Diptera
Family: Drosophilidae
Genus: Drosophila
Species: Drosophila melanogaster
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Venom peptide Sh41 Effect . [1]
 Toxin Info    Venom peptide Sh42 Effect . [1]
 Toxin Info    Neurotoxic enhancer CSTX-13 Inhibition rate . [2], [3], [4], [5]
 Toxin Info    Delta-actitoxin-Avd2b 2 Inhibition rate
100 %
 [6], [7]
 Toxin Info    Delta-actitoxin-Avd2b 4 Inhibition rate
100 %
 [6], [7]
 Toxin Info    Delta-actitoxin-Avd2b 1 Inhibition rate
100 %
 [6], [7]
 Toxin Info    Delta-actitoxin-Avd2b 3 Inhibition rate
100 %
 [6], [7]
 Toxin Info    Alpha-like toxin BmK M1 Effective concentration 50
30 nM
 [8- 21]
 Toxin Info    Sodium channel neurotoxin MeuNaTxalpha-4 Effective concentration 50
130 nM
 [22]
 Toxin Info    Sodium channel neurotoxin MeuNaTxalpha-2 Effective concentration 50
220 nM
 [22]
 Toxin Info    Sodium channel neurotoxin MeuNaTxalpha-5* Effective concentration 50
280 nM
 [22]
 Toxin Info    Sodium channel neurotoxin MeuNaTxalpha-5 Effective concentration 50
280 nM
 [22]
 Toxin Info    Sodium channel neurotoxin MeuNaTxalpha-1 Effective concentration 50
1.17 μM
 [22], [23], [24]
 Toxin Info    Mu-thomitoxin-Hme1c IC50
555 nM
 [25], [26]
References
Ref 1 Isolation and characterization of FMRFamide-like peptides in the venoms of solitary sphecid wasps. Peptides. 2021 Aug;142:170575. doi: 10.1016/j.peptides.2021.170575. Epub 2021 May 20.
Ref 2 The Dual Prey-Inactivation Strategy of Spiders-In-Depth Venomic Analysis of Cupiennius salei. Toxins (Basel). 2019 Mar 19;11(3):167. doi: 10.3390/toxins11030167.
Ref 3 CSTX-13, a highly synergistically acting two-chain neurotoxic enhancer in the venom of the spider Cupiennius salei (Ctenidae). Proc Natl Acad Sci U S A. 2004 Aug 3;101(31):11251-6. doi: 10.1073/pnas.0402226101. Epub 2004 Jul 22.
Ref 4 Spider venom: enhancement of venom efficacy mediated by different synergistic strategies in Cupiennius salei. J Exp Biol. 2005 Jun;208(Pt 11):2115-21. doi: 10.1242/jeb.01594.
Ref 5 Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider Cupiennius salei to Potentiate Toxicity on Insects. Toxins (Basel). 2020 Apr 12;12(4):250. doi: 10.3390/toxins12040250.
Ref 6 Fusion and retrotransposition events in the evolution of the sea anemone Anemonia viridis neurotoxin genes. J Mol Evol. 2009 Aug;69(2):115-24. doi: 10.1007/s00239-009-9258-x. Epub 2009 Jul 16.
Ref 7 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 8 The CDNA and genomic DNA sequences of a mammalian neurotoxin from the scorpion Buthus martensii Karsch. Toxicon. 1997 Jul;35(7):1025-31. doi: 10.1016/s0041-0101(96)00224-3.
Ref 9 Two neurotoxins (BmK I and BmK II) from the venom of the scorpion Buthus martensi Karsch: purification, amino acid sequences and assessment of specific activity. Toxicon. 1996 Sep;34(9):987-1001. doi: 10.1016/0041-0101(96)00065-7.
Ref 10 Electrophysiological characterization of BmK M1, an alpha-like toxin from Buthus martensi Karsch venom. FEBS Lett. 2001 Apr 20;495(1-2):61-5. doi: 10.1016/s0014-5793(01)02365-1.
Ref 11 Exploration of the functional site of a scorpion alpha-like toxin by site-directed mutagenesis. Biochemistry. 2003 Apr 29;42(16):4699-708. doi: 10.1021/bi0270438.
Ref 12 Importance of the conserved aromatic residues in the scorpion alpha-like toxin BmK M1: the hydrophobic surface region revisited. J Biol Chem. 2003 Jun 27;278(26):24125-31. doi: 10.1074/jbc.M211931200. Epub 2003 Apr 13.
Ref 13 Fos expression in rat spinal cord induced by peripheral injection of BmK I, an alpha-like scorpion neurotoxin. Toxicol Appl Pharmacol. 2003 Oct 1;192(1):78-85. doi: 10.1016/s0041-008x(03)00260-6.
Ref 14 Molecular basis of the mammalian potency of the scorpion alpha-like toxin, BmK M1. FASEB J. 2005 Apr;19(6):594-6. doi: 10.1096/fj.04-2485fje. Epub 2005 Jan 27.
Ref 15 The epileptic seizures induced by BmK I, a modulator of sodium channels. Exp Neurol. 2006 Jan;197(1):167-76. doi: 10.1016/j.expneurol.2005.09.006. Epub 2005 Oct 17.
Ref 16 The alpha-like scorpion toxin BmK I enhances membrane excitability via persistent sodium current by preventing slow inactivation and deactivation of rNav1.2a expressed in Xenopus Oocytes. Toxicol In Vitro. 2009 Jun;23(4):561-8. doi: 10.1016/j.tiv.2008.12.022. Epub 2008 Dec 30.
Ref 17 Molecular determination of selectivity of the site 3 modulator (BmK I) to sodium channels in the CNS: a clue to the importance of Nav1.6 in BmK I-induced neuronal hyperexcitability. Biochem J. 2010 Oct 15;431(2):289-98. doi: 10.1042/BJ20100517.
Ref 18 A series of bioactivity-variant neurotoxins from scorpion Buthus martensii Karsch: purification, crystallization and crystallographic analysis. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):341-4. doi: 10.1107/S0907444998006593. Epub 1999 Jan 1.
Ref 19 Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel. J Mol Biol. 1999 Sep 10;292(1):125-35. doi: 10.1006/jmbi.1999.3036.
Ref 20 Structural mechanism governing cis and trans isomeric states and an intramolecular switch for cis/trans isomerization of a non-proline peptide bond observed in crystal structures of scorpion toxins. J Mol Biol. 2004 Aug 27;341(5):1189-204. doi: 10.1016/j.jmb.2004.06.067.
Ref 21 Structural basis for the voltage-gated Na+ channel selectivity of the scorpion alpha-like toxin BmK M1. J Mol Biol. 2005 Nov 4;353(4):788-803. doi: 10.1016/j.jmb.2005.08.068. Epub 2005 Sep 22.
Ref 22 Evolutionary diversification of Mesobuthus -scorpion toxins affecting sodium channels. Mol Cell Proteomics. 2012 Jan;11(1):M111.012054. doi: 10.1074/mcp.M111.012054. Epub 2011 Oct 3.
Ref 23 Scorpion toxin MeuNaTx-1 sensitizes primary nociceptors by selective modulation of voltage-gated sodium channels. FEBS J. 2021 Apr;288(7):2418-2435. doi: 10.1111/febs.15593. Epub 2020 Nov 5.
Ref 24 Structure of MeuNaTx-1 toxin from scorpion venom highlights the importance of the nest motif. Proteins. 2021 Mar 13. doi: 10.1002/prot.26074. Online ahead of print.
Ref 25 Structure of membrane-active toxin from crab spider Heriaeus melloteei suggests parallel evolution of sodium channel gating modifiers in Araneomorphae and Mygalomorphae. J Biol Chem. 2015 Jan 2;290(1):492-504. doi: 10.1074/jbc.M114.595678. Epub 2014 Oct 28.
Ref 26 Spider toxin inhibits gating pore currents underlying periodic paralysis. Proc Natl Acad Sci U S A. 2018 Apr 24;115(17):4495-4500. doi: 10.1073/pnas.1720185115. Epub 2018 Apr 10.
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