SIX1_BUTOC
ID SIX1_BUTOC Reviewed; 65 AA.
AC P55902;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alpha-insect toxin BotIT1;
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, TOXIC DOSE, AND MASS 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: 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. This contractive toxin is
CC highly toxic to insects and barely toxic to mammals.
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=7334.93; Mass_error=0.23; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9080593};
CC -!- TOXIC DOSE: LD(50) is 50 ug/kg in mouse by intracerebroventricular
CC injection and 600 ng/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. Alpha subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P55902; -.
DR SMR; P55902; -.
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..65
FT /note="Alpha-insect toxin BotIT1"
FT /id="PRO_0000066713"
FT DOMAIN 2..64
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
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"
SQ SEQUENCE 65 AA; 7343 MW; 93A1371D877D7123 CRC64;
VRDAYIAQNY NCVYFCMKDD YCNDLCTKNG ASSGYCQWAG KYGNACWCYA LPDNVPIRIP
GKCHS
