ID   SCX9_CENLI              Reviewed;          84 AA.
AC   Q8WRY4;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Toxin Cll9;
DE   Flags: Precursor;
OS   Centruroides limpidus (Mexican scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-82, MASS
RP   SPECTROMETRY, AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=12818191; DOI=10.1016/s1570-9639(03)00155-9;
RA   Corona M., Coronas F.V., Merino E., Becerril B., Gutierrez R.,
RA   Rebolledo-Antunez S., Garcia D.E., Possani L.D.;
RT   "A novel class of peptide found in scorpion venom with neurodepressant
RT   effects in peripheral and central nervous system of the rat.";
RL   Biochim. Biophys. Acta 1649:58-67(2003).
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). Has some action on
CC       peripheral ganglia, but not on other sodium channels such as those from
CC       cerebellum granular cells in culture. Induces sleep, suggesting a
CC       strong antiepileptic action. {ECO:0000250,
CC       ECO:0000269|PubMed:12818191}.
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   -!- MASS SPECTROMETRY: Mass=6888.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12818191};
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; AF387171; AAL57291.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8WRY4; -.
DR   SMR; Q8WRY4; -.
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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
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   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:12818191"
FT   CHAIN           20..82
FT                   /note="Toxin Cll9"
FT                   /id="PRO_0000035278"
FT   DOMAIN          20..83
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        44..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        48..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   84 AA;  9198 MW;  21018F12E2ECC26E CRC64;
     MNSLLMITAC LILIGTVWAE DGYLFDKRKR CTLACIDKTG DKNCDRNCKK EGGSFGHCSY
     SACWCKGLPG STPISRTPGK TCKK