ID   TXA26_ANDAU             Reviewed;          80 AA.
AC   Q4LCS7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Toxin-like peptide AaF1CA26;
DE   Flags: Precursor;
GN   Name=aaF1CA26 {ECO:0000312|EMBL:CAH03781.1};
OS   Androctonus australis (Sahara scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=6858;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAH03781.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Venom gland {ECO:0000269|PubMed:15963953};
RX   PubMed=15963953; DOI=10.1016/j.bbrc.2005.05.148;
RA   Martin-Eauclaire M.-F., Ceard B., Bosmans F., Rosso J.-P., Tytgat J.,
RA   Bougis P.E.;
RT   "New 'birtoxin analogs' from Androctonus australis venom.";
RL   Biochem. Biophys. Res. Commun. 333:524-530(2005).
CC   -!- FUNCTION: Probable neurotoxin that inhibits ion channels.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01493}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15963953}.
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 (3 C-C) scorpion toxin superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ781835; CAH03781.1; -; mRNA.
DR   AlphaFoldDB; Q4LCS7; -.
DR   SMR; Q4LCS7; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0008200; F:ion channel inhibitor activity; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255, ECO:0000312|EMBL:CAH03781.1"
FT   CHAIN           23..80
FT                   /note="Toxin-like peptide AaF1CA26"
FT                   /evidence="ECO:0000312|EMBL:CAH03781.1"
FT                   /id="PRO_0000228822"
FT   DOMAIN          25..80
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        40..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        49..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        53..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   80 AA;  9019 MW;  88C3635721FD585B CRC64;
     MMKLMLFSII VILFSLIGSI HGADVPGNYP LDSSDDTYLC APLGENPSCI QICRKHGVKY
     GYCYAFQCWC EYLEDKNVKS