ID   SCXA_CENNO              Reviewed;          81 AA.
AC   Q94435; P91591;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Insect-toxin Cn10;
DE   AltName: Full=CngtVIII;
DE   Flags: Precursor; Fragment;
OS   Centruroides noxius (Mexican scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 14-80.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=8973638; DOI=10.1111/j.1432-1033.1996.0235r.x;
RA   Selisko B., Garcia C., Becerril B., Delepierre M., Possani L.D.;
RT   "An insect-specific toxin from Centruroides noxius Hoffmann. cDNA, primary
RT   structure three-dimensional model and electrostatic surface potentials in
RT   comparison with other toxin variants.";
RL   Eur. J. Biochem. 242:235-242(1996).
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 (By similarity). Is toxic on insects
CC       and crustaceans, but not on mammals. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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   -!- 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; Y08270; CAA69595.1; -; mRNA.
DR   AlphaFoldDB; Q94435; -.
DR   SMR; Q94435; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          <1..13
FT                   /evidence="ECO:0000269|PubMed:8973638"
FT   CHAIN           14..80
FT                   /note="Insect-toxin Cn10"
FT                   /id="PRO_0000035286"
FT   PROPEP          81
FT                   /note="Removed by a carboxypeptidase"
FT                   /id="PRO_0000035287"
FT   DOMAIN          14..79
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        25..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        29..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        38..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        42..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   NON_TER         1
SQ   SEQUENCE   81 AA;  8812 MW;  C7D4757A93962C74 CRC64;
     ITACLVLIGT VCAKEGYLVN KSTGCKYNCL ILGENKNCDM ECKAKNQGGS YGYCYKLACW
     CEGLPESTPT YPIPGKTCRT K