ID   SCXJ_TITBA              Reviewed;          62 AA.
AC   P60276;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Toxin Tb2-II;
DE   AltName: Full=P-Mice-Ins-beta* NaTx5.4;
OS   Tityus bahiensis (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=50343;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11223090; DOI=10.1016/s0041-0101(00)00240-3;
RA   Pimenta A.M.C., Martin-Eauclaire M.-F., Rochat H., Figueiredo S.G.,
RA   Kalapothakis E., Afonso L.C.C., De Lima M.E.;
RT   "Purification, amino-acid sequence and partial characterization of two
RT   toxins with anti-insect activity from the venom of the South American
RT   scorpion Tityus bahiensis (Buthidae).";
RL   Toxicon 39:1009-1019(2001).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22355312; DOI=10.1371/journal.pone.0030478;
RA   Guerrero-Vargas J.A., Mourao C.B., Quintero-Hernandez V., Possani L.D.,
RA   Schwartz E.F.;
RT   "Identification and phylogenetic analysis of Tityus pachyurus and Tityus
RT   obscurus novel putative Na+-channel scorpion toxins.";
RL   PLoS ONE 7:E30478-E30478(2012).
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). This toxin is active
CC       against both mammals and insects. {ECO:0000250}.
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=6953.73; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11223090};
CC   -!- TOXIC DOSE: LD(50) is 40.0 ng/house fly. {ECO:0000269|PubMed:11223090}.
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   AlphaFoldDB; P60276; -.
DR   SMR; P60276; -.
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   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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..62
FT                   /note="Toxin Tb2-II"
FT                   /id="PRO_0000066797"
FT   DOMAIN          1..62
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        11..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        15..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        23..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   62 AA;  6963 MW;  E1565EA557DED3E3 CRC64;
     KEGYAMDHEG CKFSCFIRPS GFCDGYCKTH LKASSGYCAW PACYCYGVPS NIKVWDYATN
     KC