ID   SCXS_TITPA              Reviewed;          38 AA.
AC   P0DL23;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Putative beta-neurotoxin;
DE   Flags: Fragment;
OS   Tityus pachyurus (Colombian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=288781;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16309982; DOI=10.1016/j.bbapap.2005.08.010;
RA   Barona J., Batista C.V.F., Zamudio F.Z., Gomez-Lagunas F., Wanke E.,
RA   Otero R., Possani L.D.;
RT   "Proteomic analysis of the venom and characterization of toxins specific
RT   for Na+ - and K+ -channels from the Colombian scorpion Tityus pachyurus.";
RL   Biochim. Biophys. Acta 1764:76-84(2006).
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}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16309982}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16309982}.
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=7066.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16309982};
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   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; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 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..>38
FT                   /note="Putative beta-neurotoxin"
FT                   /id="PRO_0000422255"
FT   DOMAIN          2..>38
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        24..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         38
SQ   SEQUENCE   38 AA;  4195 MW;  E2EB1F05429F2005 CRC64;
     NKDGYLMEHD GCKLSCLMKK GTFCAEXCAR LXGXDGYC