ID   SC52_CENOR              Reviewed;          65 AA.
AC   C0HLF8;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Toxin Co52 {ECO:0000303|PubMed:31734253};
OS   Centruroides ornatus (Scorpion) (Centruroides infamatus ornatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=2338500 {ECO:0000303|PubMed:31734253};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:31734253};
RX   PubMed=31734253; DOI=10.1016/j.toxicon.2019.11.004;
RA   Garcia-Guerrero I.A., Carcamo-Noriega E., Gomez-Lagunas F.,
RA   Gonzalez-Santillan E., Zamudio F.Z., Gurrola G.B., Possani L.D.;
RT   "Biochemical characterization of the venom from the Mexican scorpion
RT   Centruroides ornatus, a dangerous species to humans.";
RL   Toxicon 173:27-38(2020).
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). Not toxic to mice,
CC       chicks, crickets or woodlice (at 5ug) (PubMed:31734253).
CC       {ECO:0000250|UniProtKB:C0HLF2, ECO:0000269|PubMed:31734253}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31734253}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31734253}.
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=7343.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:31734253};
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   AlphaFoldDB; C0HLF8; -.
DR   SMR; C0HLF8; -.
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   Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..65
FT                   /note="Toxin Co52"
FT                   /id="PRO_0000450098"
FT   DOMAIN          2..65
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        25..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        29..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   65 AA;  7351 MW;  0A5CDAE424623F36 CRC64;
     KEDGYLVDKT GCKKSCYKLG ENDYCNRECK WKHVGGSYGY CYGFGCYCEG LSDSTPTWPL
     PNKTC