ID   SCX39_CENSU             Reviewed;          87 AA.
AC   B7FDP2; P85522;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Toxin Css39.8;
DE   Flags: Precursor;
OS   Centruroides suffusus (Durango bark scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-85, STRUCTURE BY NMR OF
RP   20-85, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, TOXIC DOSE, AND DISULFIDE BONDS.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=19631296; DOI=10.1016/j.bbapap.2009.07.006;
RA   Corzo G., Prochnicka-Chalufour A., Garcia B.I., Possani L.D.,
RA   Delepierre M.;
RT   "Solution structure of Cn5, a crustacean toxin found in the venom of the
RT   scorpions Centruroides noxius and Centruroides suffusus suffusus.";
RL   Biochim. Biophys. Acta 1794:1591-1598(2009).
CC   -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC       channels (Nav) and shift the voltage of activation toward more negative
CC       potentials thereby affecting sodium channel activation and promoting
CC       spontaneous and repetitive firing. This toxin is lethal to crustaceans
CC       (freshwater crayfish (Cambarellus montezumae spp.)), it provokes a
CC       reversible paralysis to insects (crickets (Achaeta spp.)), but is not
CC       toxic to mice. At high concentrations, it does displace the (beta)
CC       mammal-specific toxin Cn2 from rat brain synaptosomes.
CC       {ECO:0000269|PubMed:19631296}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19631296}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:19631296}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=7136.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19631296};
CC   -!- TOXIC DOSE: LD(50) is 28.5 mg/g body weight of crayfish.
CC       {ECO:0000269|PubMed:19631296}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR   EMBL; AM981271; CAQ37795.1; -; mRNA.
DR   AlphaFoldDB; B7FDP2; -.
DR   SMR; B7FDP2; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR018218; Scorpion_toxinL.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   PRINTS; PR00285; SCORPNTOXIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:19631296"
FT   CHAIN           20..85
FT                   /note="Toxin Css39.8"
FT                   /id="PRO_5000417205"
FT   DOMAIN          20..85
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:19631296"
FT   DISULFID        35..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:19631296"
FT   DISULFID        44..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:19631296"
FT   DISULFID        48..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:19631296"
SQ   SEQUENCE   87 AA;  9514 MW;  6673259B9DACE88F CRC64;
     MNSLLMITAC FFLIGTVWAK EGYLVNKSTG CKYGCLLLGK NEGCDKECKA KNQGGSYGYC
     YAFGCWCEGL PESTPTYPLP NKSCSKK