ID   SCXL_ANDAU              Reviewed;          66 AA.
AC   P80950;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Neurotoxin-like protein STR1;
DE   AltName: Full=Anatoxin AaH STR1;
DE            Short=AaHSTR1;
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.
RC   STRAIN=Hector; TISSUE=Venom;
RA   Mansuelle P., Hassani O., Cestele S., Loret E.P., van Dorsselaer A.,
RA   Rochat H., Sampieri F.;
RL   Submitted (AUG-1997) to UniProtKB.
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RC   STRAIN=Hector;
RX   PubMed=9288938; DOI=10.1111/j.1432-1033.1997.01118.x;
RA   Blanc E., Hassani O., Meunier S., Mansuelle P., Sampieri F., Rochat H.,
RA   Darbon H.;
RT   "1H-NMR-derived secondary structure and overall fold of a natural anatoxin
RT   from the scorpion Androctonus australis hector.";
RL   Eur. J. Biochem. 247:1118-1126(1997).
CC   -!- FUNCTION: This protein is not toxic.
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   -!- 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; P80950; -.
DR   SMR; P80950; -.
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:InterPro.
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; 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; Secreted.
FT   CHAIN           1..66
FT                   /note="Neurotoxin-like protein STR1"
FT                   /id="PRO_0000066829"
FT   DOMAIN          2..65
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        13..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:9288938"
FT   DISULFID        17..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:9288938"
FT   DISULFID        26..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:9288938"
FT   DISULFID        30..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:9288938"
SQ   SEQUENCE   66 AA;  7641 MW;  D1B64B7C4E8467E3 CRC64;
     ARDGYIVHDG TNCKYSCEFG SEYKYCGPLC EKKKAKTGYC YLFACWCIEV PDEVRVWGED
     GFMCWS