ID   SCX2_CENOR              Reviewed;          66 AA.
AC   C0HLF3;
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=Beta-mammal toxin Co2 {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 (PubMed:31734253). This toxin acts on
CC       human Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.4/SCN4A and Nav1.6/SCN8A
CC       voltage-gated sodium channels (PubMed:31734253). Also, it reduces the
CC       peak of sodium currents in Nav1.5/SCN5A at all potentials
CC       (PubMed:31734253). In vivo, is lethal to mice when intraperitoneally
CC       injected at a dose of 5ug (PubMed:31734253). No activity is observed
CC       when injected into crickets or woodlice (PubMed:31734253).
CC       {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=7614.3; 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; C0HLF3; -.
DR   SMR; C0HLF3; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   GO; GO:0044493; P:envenomation resulting in negative regulation of voltage-gated sodium channel activity in 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   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..66
FT                   /note="Beta-mammal toxin Co2"
FT                   /id="PRO_0000450096"
FT   DOMAIN          1..66
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   66 AA;  7623 MW;  C86556D167C9E502 CRC64;
     KEGYIVNYHD GCKYACVKLG DNDYCLRECK LRYGKGAGGY CYAFGCWCTH LYEQAVVWPL
     PKKRCN