SIX6_BUTOC
ID SIX6_BUTOC Reviewed; 62 AA.
AC P59864;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Beta-insect depressant toxin BotIT6;
DE Short=Insect toxin 6;
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, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=12565735; DOI=10.1016/s0041-0101(02)00246-5;
RA Mejri T., Borchani L., Srairi-Abid N., Ben khalifa R., Cestele S.,
RA Regaya I., Karoui H., Pelhate M., Rochat H., el Ayeb M.;
RT "BotIT6: a potent depressant insect toxin from Buthus occitanus tunetanus
RT venom.";
RL Toxicon 41:163-171(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16216259; DOI=10.1016/j.jinsphys.2005.08.008;
RA Bel Haj Rhouma R., Cerutti-Duonor M., Benkhadir K., Goudey-Perriere F.,
RA el Ayeb M., Lopez-Ferber M., Karoui H.;
RT "Insecticidal effects of Buthus occitanus tunetanus BotIT6 toxin expressed
RT in Escherichia coli and baculovirus/insect cells.";
RL J. Insect Physiol. 51:1376-1383(2005).
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.
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 -!- TOXIC DOSE: LD(50) is 0.1 mg/kg in Blattella germanica.
CC {ECO:0000269|PubMed:12565735}.
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; P59864; -.
DR SMR; P59864; -.
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 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..62
FT /note="Beta-insect depressant toxin BotIT6"
FT /id="PRO_0000066717"
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 62 AA; 7323 MW; 062EF238BFB517FC CRC64;
DGYPKQKNGC KYDCIINNKW CNGICKMHGG YYGYCWGWGL ACWCEGLPED KKWWYETNKC
GR
