ID   TX20_ANDCR              Reviewed;          23 AA.
AC   P0C2A0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Toxin Acra2;
DE   Flags: Fragment;
OS   Androctonus crassicauda (Arabian fat-tailed scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=122909;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16762386; DOI=10.1016/j.toxicon.2006.04.003;
RA   Caliskan F., Garcia B.I., Coronas F.I.V., Batista C.V.F., Zamudio F.Z.,
RA   Possani L.D.;
RT   "Characterization of venom components from the scorpion Androctonus
RT   crassicauda of Turkey: peptides and genes.";
RL   Toxicon 48:12-22(2006).
CC   -!- FUNCTION: Excitatory insect toxins induce a spastic paralysis. They
CC       bind voltage-independently at site-4 of sodium channels (Nav) and shift
CC       the voltage of activation toward more negative potentials thereby
CC       affecting sodium channel activation and promoting spontaneous and
CC       repetitive firing (By similarity). Is lethal to mice. Is about 1% of
CC       the total protein in the venom. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16762386}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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   -!- PTM: Contains 4 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=7848.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16762386};
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..>23
FT                   /note="Toxin Acra2"
FT                   /id="PRO_0000271327"
FT   DOMAIN          2..>23
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2430 MW;  91E5B25BD4EB093F CRC64;
     KKDGYIVDSN GCAPECFPTN XGC