ID   SCXB_CENNO              Reviewed;          63 AA.
AC   P58296;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Toxin Cn11 {ECO:0000303|PubMed:11914394};
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   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=11914394; DOI=10.1242/jeb.205.6.869;
RA   Ramirez-Dominguez M.E., Olamendi-Portugal T., Garcia U., Garcia C.,
RA   Arechiga H., Possani L.D.;
RT   "Cn11, the first example of a scorpion toxin that is a true blocker of
RT   Na(+) currents in crayfish neurons.";
RL   J. Exp. Biol. 205:869-876(2002).
CC   -!- FUNCTION: First blocker of sodium channels (Nav) found in scorpions. Is
CC       lethal to crustaceans (Cambarellus montezumae), less toxic to insects
CC       (crickets) and non-toxic to mammals (mice) at the doses assayed.
CC       {ECO:0000269|PubMed:11914394}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11914394}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11914394}.
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. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P58296; -.
DR   SMR; P58296; -.
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   CDD; cd00107; Knot1; 1.
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; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..63
FT                   /note="Toxin Cn11"
FT                   /evidence="ECO:0000269|PubMed:11914394"
FT                   /id="PRO_0000066771"
FT   DOMAIN          2..63
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        23..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   63 AA;  6982 MW;  D482413D0FB66FFE CRC64;
     ARDGYPVDEK GCKLSCLIND KWCNSACHSR GGKYGYCYTG GLACYCEAVP DNVKVWTYET
     NTC