ID   SCX1_BUTOC              Reviewed;          65 AA.
AC   P01488;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Alpha-toxin Bot1 {ECO:0000303|PubMed:16274721};
DE   AltName: Full=Bot I;
DE            Short=BotI;
DE   AltName: Full=Neurotoxin 1;
DE   AltName: Full=Neurotoxin I {ECO:0000303|PubMed:6845379};
OS   Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=6871;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND AMIDATION AT PHE-65.
RC   TISSUE=Venom;
RX   PubMed=6845379; DOI=10.1016/0041-0101(83)90058-2;
RA   Gregoire J., Rochat H.;
RT   "Covalent structure of toxins I and II from the scorpion Buthus occitanus
RT   tunetanus.";
RL   Toxicon 21:153-162(1983).
RN   [2]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Vargas O., Gregoire J., Martin M.-F., Bechis G., Rochat H.;
RT   "Neurotoxins from the venoms of two scorpions: Buthus occitanus tunetanus
RT   and Buthus occitanus mardochei.";
RL   Toxicon 20:79-79(1982).
RN   [3]
RP   REVIEW.
RX   PubMed=16274721; DOI=10.1016/j.toxicon.2005.09.006;
RA   Rodriguez de la Vega R.C., Possani L.D.;
RT   "Overview of scorpion toxins specific for Na+ channels and related
RT   peptides: biodiversity, structure-function relationships and evolution.";
RL   Toxicon 46:831-844(2005).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6845379,
CC       ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:6845379, ECO:0000305|Ref.2}.
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   PIR; A01748; NTSR1B.
DR   AlphaFoldDB; P01488; -.
DR   SMR; P01488; -.
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   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..65
FT                   /note="Alpha-toxin Bot1"
FT                   /evidence="ECO:0000269|PubMed:6845379, ECO:0000269|Ref.2"
FT                   /id="PRO_0000066732"
FT   DOMAIN          2..64
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         65
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:6845379"
FT   DISULFID        12..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        22..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   CONFLICT        29
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   65 AA;  7268 MW;  6FCD8F69D36A4B8D CRC64;
     GRDAYIAQPE NCVYECAQNS YCNDLCTKNG ATSGYCQWLG KYGNACWCKD LPDNVPIRIP
     GKCHF