SIX2_BUTOC
ID SIX2_BUTOC Reviewed; 60 AA.
AC P59863;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Beta-toxin BotIT2;
DE Short=Bot IT2;
DE AltName: Full=Insect toxin 2;
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.
RC TISSUE=Venom;
RX PubMed=8917451; DOI=10.1111/j.1432-1033.1996.00525.x;
RA Borchani L., Mansuelle P., Stankiewicz M., Grolleau F., Cestele S.,
RA Karoui H., Lapied B., Rochat H., Pelhate M., el Ayeb M.;
RT "A new scorpion venom toxin paralytic to insects that affects Na+ channel
RT activation. Purification, structure, antigenicity and mode of action.";
RL Eur. J. Biochem. 241:525-532(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=15941066;
RA Bel Haj Rhouma R., Dkhil H., Benkhadir K., Borchani L., el Ayeb M.,
RA Karoui H.;
RT "Molecular cloning and nucleotide sequence analysis of encoded anti-insect
RT toxin BotIT2 from the scorpion Buthus occitanus tunetanus venom.";
RL Arch. Inst. Pasteur Tunis 80:35-41(2003).
RN [3]
RP FUNCTION.
RX DOI=10.1016/0022-1910(95)00120-4;
RA Stankiewicz M., Grolleau F., Lapied B., Borchani L., el Ayeb M.,
RA Pelhate M.;
RT "Bot IT2, a toxin paralytic to insects from the Buthus occitanus tunetanus
RT venom modifying the activity of insect sodium channels.";
RL J. Insect Physiol. 42:397-405(1996).
RN [4]
RP FUNCTION.
RX PubMed=9094428; DOI=10.1016/s0014-5793(97)00160-9;
RA Cestele S., Borchani L., el Ayeb M., Rochat H.;
RT "Bot IT2: a new scorpion toxin to study receptor site on insect sodium
RT channels.";
RL FEBS Lett. 405:77-80(1997).
CC -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC channels (Nav) and shift the voltage of activation toward more negative
CC potentials thereby affecting sodium channel activation and promoting
CC spontaneous and repetitive firing. This toxin specifically acts by
CC inducing a new current with very slow activation/deactivation kinetics
CC due to the transformation of normal fast channels into slow ones. It
CC possess properties of excitatory and depressant toxins. It is highly
CC active on insects and less active on mammals.
CC {ECO:0000269|PubMed:9094428, ECO:0000269|Ref.3}.
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; P59863; -.
DR SMR; P59863; -.
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..60
FT /note="Beta-toxin BotIT2"
FT /id="PRO_0000066714"
FT DOMAIN 1..60
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 60 AA; 6918 MW; 597A9A6D674AEEE7 CRC64;
DGYIKGYKGC KITCVINDDY CDTECKAEGG TYGYCWKWGL ACWCEDLPDE KRWKSETNTC
