ID   SCX3A_ANDCR             Reviewed;          69 AA.
AC   D5HR52;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Alpha-toxin Ac3;
DE   AltName: Full=Neurotoxin 3;
DE   Flags: Precursor; 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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=20018978; DOI=10.1093/molbev/msp310;
RA   Weinberger H., Moran Y., Gordon D., Turkov M., Kahn R., Gurevitz M.;
RT   "Positions under positive selection--key for selectivity and potency of
RT   scorpion alpha-toxins.";
RL   Mol. Biol. Evol. 27:1025-1034(2010).
CC   -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC       channels (Nav) and inhibit the inactivation of the activated channels,
CC       thereby blocking neuronal transmission. {ECO:0000250|UniProtKB:P01485}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01485}.
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   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR   EMBL; GQ335452; ADE42761.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5HR52; -.
DR   SMR; D5HR52; -.
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   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   3: Inferred from homology;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          <1..3
FT                   /evidence="ECO:0000250|UniProtKB:P01485"
FT   CHAIN           4..67
FT                   /note="Alpha-toxin Ac3"
FT                   /id="PRO_5000585059"
FT   DOMAIN          5..67
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         67
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P01485"
FT   DISULFID        15..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        19..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        25..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        29..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   NON_TER         1
FT                   /evidence="ECO:0000305|PubMed:20018978"
SQ   SEQUENCE   69 AA;  7815 MW;  DDF835AA62BD470B CRC64;
     VESIKDGYIV DDRNCTYFCG RNAYCNEECT KLKGESGYCQ WASPYGNACY CYKLPDHVRT
     KAPGKCNGR