ID   SIX2_BUTAR              Reviewed;          61 AA.
AC   P80962;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Beta-insect depressant toxin BaIT2;
DE            Short=BaIT2;
DE            Short=BarIT2;
DE            Short=Toxin 2;
OS   Buthacus arenicola (North African scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthacus.
OX   NCBI_TaxID=70335;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=9030726; DOI=10.1111/j.1432-1033.1997.93_1a.x;
RA   Cestele S., Kopeyan C., Oughideni R., Mansuelle P., Granier C., Rochat H.;
RT   "Biochemical and pharmacological characterization of a depressant insect
RT   toxin from the venom of the scorpion Buthacus arenicola.";
RL   Eur. J. Biochem. 243:93-99(1997).
CC   -!- FUNCTION: Depressant insect beta-toxins cause a transient contraction
CC       paralysis followed by a slow flaccid paralysis. They bind voltage-
CC       independently at site-4 of sodium channels (Nav) and shift the voltage
CC       of activation toward more negative potentials thereby affecting sodium
CC       channel activation and promoting spontaneous and repetitive firing.
CC       This toxin is active only on insects. {ECO:0000269|PubMed:9030726}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P80962; -.
DR   SMR; P80962; -.
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="Beta-insect depressant toxin BaIT2"
FT                   /id="PRO_0000066712"
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;  6845 MW;  4143435560DCFAEB CRC64;
     DGYIRRRDGC KVSCLFGNEG CDKECKAYGG SYGYCWTWGL ACWCEGLPDD KTWKSETNTC
     G