ID   SIX5_ANDAU              Reviewed;          61 AA.
AC   P81504;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Insect toxin AaHIT5;
DE            Short=AaH IT5;
DE            Short=AaIT5;
DE            Short=Insect toxin 5;
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, AND FUNCTION.
RC   STRAIN=Hector; TISSUE=Venom;
RX   PubMed=9208943; DOI=10.1111/j.1432-1033.1997.t01-1-00496.x;
RA   Nakagawa Y., Lee Y.M., Lehmberg E., Herrmann R., Herrmann R., Moskowitz H.,
RA   Jones A.D., Hammock B.D.;
RT   "Anti-insect toxin 5 (AaIT5) from Androctonus australis.";
RL   Eur. J. Biochem. 246:496-501(1997).
RN   [2]
RP   3D-STRUCTURE MODELING, AND MASS SPECTROMETRY.
RX   PubMed=9627406;
RX   DOI=10.1002/(sici)1520-6327(1998)38:2<53::aid-arch1>3.0.co;2-w;
RA   Nakagawa Y., Sadilek M., Lehmberg E., Herrmann R., Herrmann R.,
RA   Moskowitz H., Lee Y.M., Thomas B.A., Shimizu R., Kuroda M., Jones A.D.,
RA   Hammock B.D.;
RT   "Rapid purification and molecular modeling of AaIT peptides from venom of
RT   Androctonus australis.";
RL   Arch. Insect Biochem. Physiol. 38:53-65(1998).
CC   -!- FUNCTION: Excitatory insect toxins induce a spastic paralysis. They
CC       bind voltage-independently to sodium channels (Nav) and shift the
CC       voltage of activation toward more negative potentials thereby affecting
CC       sodium channel activation and promoting spontaneous and repetitive
CC       firing (By similarity). This toxin elicits excitatory activity with no
CC       flaccid paralysis despite its high degree of sequence similarity with
CC       other depressant insect toxins. This toxin is active only on insects.
CC       {ECO:0000250, ECO:0000269|PubMed:9208943}.
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=6882; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9627406};
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; P81504; -.
DR   SMR; P81504; -.
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   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..61
FT                   /note="Insect toxin AaHIT5"
FT                   /id="PRO_0000066709"
FT   DOMAIN          1..61
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        10..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        14..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        21..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        25..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   61 AA;  6889 MW;  CCF5E269AFE346AA CRC64;
     DGYIKRHDGC KVTCLINDNY CDTECKREGG SYGYCYSVGF ACWCEGLPDD KAWKSETNTC
     D