ID   SCX6_CENTE              Reviewed;          85 AA.
AC   P0DUH8;
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 Ct6 {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 19-31, PROBABLE AMIDATION
RP   AT CYS-83, 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).
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. {ECO:0000250|UniProtKB:P60266}.
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=7288; 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; JZ122270; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DUH8; -.
DR   SMR; P0DUH8; -.
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..18
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT   CHAIN           19..83
FT                   /note="Beta-toxin Ct6"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT                   /id="PRO_0000452424"
FT   DOMAIN          19..84
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         83
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT   DISULFID        30..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        34..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        43..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        47..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   85 AA;  9450 MW;  3E7E8590CE7B6C39 CRC64;
     MKTFVLALCL VLIGMVYAKD GYLVSKHTGC KLGCSPKIGD RYCHIECTSM NHKGDEGYCY
     WLACYCKGMP ENAEVYPLPN KSCGK