SIXI_ORTSC
ID SIXI_ORTSC Reviewed; 64 AA.
AC O76963;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Insect toxin OsI1;
DE AltName: Full=Insecticidal toxin OsI-1;
OS Orthochirus scrobiculosus (Central Asian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Orthochirus.
OX NCBI_TaxID=6892;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-17, AMIDATION AT GLY-61,
RP TOXIC DOSE, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10669025; DOI=10.1016/s0041-0101(99)00164-6;
RA Kozlov S.A., Lipkin A.V., Nosyreva E.D., Blake A., Windass J.J.D.,
RA Grishin E.V.;
RT "Purification and cDNA cloning of an insecticidal protein from the venom of
RT the scorpion Orthochirus scrobiculosus.";
RL Toxicon 38:361-371(2000).
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 -!- MASS SPECTROMETRY: Mass=6994; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10669025};
CC -!- TOXIC DOSE: PD(50) is 12 mg/kg when injected into tobacco budworm
CC larvae (H.virescens). {ECO:0000269|PubMed:10669025}.
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 EMBL; AJ006866; CAA07277.1; -; mRNA.
DR AlphaFoldDB; O76963; -.
DR SMR; O76963; -.
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="Insect toxin OsI1"
FT /id="PRO_0000035297"
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:10669025"
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 64 AA; 7319 MW; F99EAA234E8EBA65 CRC64;
DGYPKQKDGC KYSCTINHKF CNSVCKSNGG DYGYCWFWGL ACWCEGLPDN KMWKYETNTC
GGKK
