ID   SCX7_CENTE              Reviewed;          83 AA.
AC   P0DUH9;
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 Ct7 {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 19-46, PROBABLE AMIDATION
RP   AT GLY-81, 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 toxic to
CC       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=6817; 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; JZ122271; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DUH9; -.
DR   SMR; P0DUH9; -.
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   CDD; cd00107; Knot1; 1.
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..81
FT                   /note="Beta-toxin Ct7"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT                   /id="PRO_0000452425"
FT   PROPEP          82
FT                   /evidence="ECO:0000250|UniProtKB:E7CLP2"
FT                   /id="PRO_0000452426"
FT   DOMAIN          19..81
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         81
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT   DISULFID        29..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        33..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        40..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        44..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   83 AA;  8920 MW;  8FB56F424BAB0EA0 CRC64;
     MKVLILIIAS VLLIGVECKD GYPMNSEGCK ISCVIGNTFC DTECKMLKAS SGYCWTLGLA
     CYCEGLPENV EVWDSATNKC GGK