ID   SIX4_ANDAU              Reviewed;          65 AA.
AC   P21150;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Toxin AaHIT4;
DE            Short=AaH IT4 {ECO:0000303|PubMed:1846301};
DE            Short=AaIT4;
DE   AltName: Full=Insect toxin 4;
OS   Androctonus australis (Sahara scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=6858;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=Hector; TISSUE=Venom;
RX   PubMed=1846301; DOI=10.1021/bi00217a007;
RA   Loret E.P., Martin-Eauclaire M.-F., Mansuelle P., Sampieri F., Granier C.,
RA   Rochat H.;
RT   "An anti-insect toxin purified from the scorpion Androctonus australis
RT   hector also acts on the alpha- and beta-sites of the mammalian sodium
RT   channel: sequence and circular dichroism study.";
RL   Biochemistry 30:633-640(1991).
CC   -!- FUNCTION: Has a toxic effect on insects and mammals and is capable of
CC       competing with anti-insect scorpion toxins for binding to the sodium
CC       channel (Nav) of insects. It also modulates the binding of alpha-type
CC       and beta-type anti-mammal scorpion toxins to the mammal sodium channel.
CC       It may act on both site 3 and site 4 of voltage-gated sodium channels.
CC       {ECO:0000269|PubMed:1846301}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1846301}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:1846301}.
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. {ECO:0000305}.
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DR   PIR; A38394; A38394.
DR   AlphaFoldDB; P21150; -.
DR   SMR; P21150; -.
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; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
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="Toxin AaHIT4"
FT                   /evidence="ECO:0000269|PubMed:1846301"
FT                   /id="PRO_0000066708"
FT   DOMAIN          1..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        23..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   65 AA;  7786 MW;  D3E32722C3411A1C CRC64;
     EHGYLLNKYT GCKVWCVINN EECGYLCNKR RGGYYGYCYF WKLACYCQGA RKSELWNYKT
     NKCDL