ID   SCX2_TITPA              Reviewed;          65 AA.
AC   P84631;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Beta-mammal toxin Tpa2;
DE   AltName: Full=TpNNX;
OS   Tityus pachyurus (Colombian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=288781;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:16309982};
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. This toxin is lethal to mice.
CC       {ECO:0000269|PubMed:16309982}.
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=7522.0; 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. {ECO:0000255}.
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DR   AlphaFoldDB; P84631; -.
DR   SMR; P84631; -.
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..65
FT                   /note="Beta-mammal toxin Tpa2"
FT                   /id="PRO_0000239432"
FT   DOMAIN          2..64
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        24..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   65 AA;  7531 MW;  8A8E932683BC2BAE CRC64;
     KKEGYLVGND GCKYSCFTRP AQYCVHECEL RKGTDGYCYA WLACYCYNMP DHVRTWSRAT
     NRCGS