ID   SCX17_CENTE             Reviewed;          87 AA.
AC   P0DUI2;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=Beta-toxin Ct17 {ECO:0000303|PubMed:23840487};
DE   Flags: Precursor;
OS   Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=1028682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-49, PROBABLE AMIDATION
RP   AT CYS-84, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23840487; DOI=10.1371/journal.pone.0066486;
RA   Valdez-Velazquez L.L., Quintero-Hernandez V., Romero-Gutierrez M.T.,
RA   Coronas F.I., Possani L.D.;
RT   "Mass fingerprinting of the venom and transcriptome of venom gland of
RT   scorpion Centruroides tecomanus.";
RL   PLoS ONE 8:e66486-e66486(2013).
RN   [2]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=27130039; DOI=10.1016/j.toxicon.2016.04.046;
RA   Valdez-Velazquez L.L., Romero-Gutierrez M.T., Delgado-Enciso I.,
RA   Dobrovinskaya O., Melnikov V., Quintero-Hernandez V., Ceballos-Magana S.G.,
RA   Gaitan-Hinojosa M.A., Coronas F.I., Puebla-Perez A.M., Zamudio F.,
RA   De la Cruz-Garcia I., Vazquez-Vuelvas O.F., Soriano-Hernandez A.D.,
RA   Possani L.D.;
RT   "Comprehensive analysis of venom from the scorpion Centruroides tecomanus
RT   reveals compounds with antimicrobial, cytotoxic, and insecticidal
RT   activities.";
RL   Toxicon 118:95-103(2016).
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 possibly lethal
CC       to mice, freshwater shrimp and crickets (PubMed:27130039).
CC       {ECO:0000250|UniProtKB:P60266, ECO:0000269|PubMed:27130039}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23840487}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23840487}.
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=7427; Method=Electrospray; Note=Average mass.;
CC       Evidence={ECO:0000269|PubMed:23840487};
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; JZ122281; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DUI2; -.
DR   SMR; P0DUI2; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT   CHAIN           20..84
FT                   /note="Beta-toxin Ct17"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT                   /id="PRO_0000452429"
FT   DOMAIN          20..85
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         84
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT   DISULFID        31..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        44..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        48..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   87 AA;  9780 MW;  69592082DC083078 CRC64;
     MNSLLMITAC LVLIGTVWAK KDGYLVDKTG CKKTCYKLGE NDFCNRECKW KHIGGSYGYC
     YGFGCYCEGM SDSTPTWPLP NKRCGKK