SCXB_BUTOC
ID SCXB_BUTOC Reviewed; 65 AA.
AC P01486;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-toxin Bot11;
DE AltName: Full=BotXI;
DE AltName: Full=Neurotoxin 11;
DE AltName: Full=Toxin XI;
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=6729843; DOI=10.1016/0041-0101(84)90028-x;
RA Martin M.-F., Rochat H.;
RT "Purification of thirteen toxins active on mice from the venom of the North
RT African scorpion Buthus occitanus tunetanus.";
RL Toxicon 22:279-291(1984).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=3570664; DOI=10.1111/j.1399-3011.1987.tb02249.x;
RA Sampieri F., Habersetzer-Rochat C., Martin M.-F., Kopeyan C., Rochat H.;
RT "Amino acid sequence of toxin XI of the scorpion Buthus occitanus
RT tunetanus. Evidence of a mutation having an important effect upon
RT neurotoxic activity.";
RL Int. J. Pept. Protein Res. 29:231-237(1987).
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.
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. Alpha subfamily. {ECO:0000305}.
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DR PIR; A01746; NTSREB.
DR AlphaFoldDB; P01486; -.
DR SMR; P01486; -.
DR PRIDE; P01486; -.
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-toxin Bot11"
FT /id="PRO_0000066738"
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; 7468 MW; 9B2342CEEA431A36 CRC64;
LKDGYIVDDR NCTYFCGTNA YCNEECVKLK GESGYCQWVG RYGNACWCYK LPDHVRTVQA
GRCRS
