SIX4_BUTOC
ID SIX4_BUTOC Reviewed; 61 AA.
AC P55903;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Beta-insect depressant toxin BotIT4;
DE Short=Insect toxin 4;
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, AMIDATION AT GLY-61, FUNCTION, TOXIC DOSE, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=9080593; DOI=10.1016/s0041-0101(96)00173-0;
RA Borchani L., Stankiewicz M., Kopeyan C., Mansuelle P., Kharrat R.,
RA Cestele S., Karoui H., Rochat H., Pelhate M., el Ayeb M.;
RT "Purification, structure and activity of three insect toxins from Buthus
RT occitanus tunetanus venom.";
RL Toxicon 35:365-382(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:9080593}.
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 -!- MASS SPECTROMETRY: Mass=6836.25; Mass_error=0.89; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9080593};
CC -!- TOXIC DOSE: LD(50) is 1.1 ug/g in Blattella germanica.
CC {ECO:0000269|PubMed:9080593}.
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; P55903; -.
DR SMR; P55903; -.
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..61
FT /note="Beta-insect depressant toxin BotIT4"
FT /id="PRO_0000066715"
FT DOMAIN 1..61
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 61
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:9080593"
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
