SIXC_ODODO
ID SIXC_ODODO Reviewed; 64 AA.
AC A0A0U4AHC3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Beta-insect excitatory toxin OdTx12 {ECO:0000303|PubMed:32442468};
DE AltName: Full=Sodium channel toxin NaTx12 {ECO:0000303|PubMed:27426055};
DE Flags: Fragment;
OS Odontobuthus doriae (Yellow Iranian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Odontobuthus.
OX NCBI_TaxID=342590;
RN [1] {ECO:0000312|EMBL:ALY87543.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=27426055; DOI=10.1016/j.toxicon.2016.07.010;
RA Soorki M.N., Galehdari H., Baradaran M., Jalali A.;
RT "First venom gland transcriptomic analysis of Iranian yellow scorpion
RT 'Odonthubuthus doriae' with some new findings.";
RL Toxicon 120:69-77(2016).
RN [2]
RP ERRATUM OF PUBMED:27426055.
RX PubMed=29397194; DOI=10.1016/j.toxicon.2018.01.014;
RA Soorki M.N., Galehdari H., Baradaran M., Jalali A.;
RL Toxicon 143:118-118(2018).
RN [3]
RP FUNCTION, RECOMBINANT EXPRESSION, BIOASSAY, TOXIC DOSE, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=32442468; DOI=10.1016/j.toxicon.2020.05.003;
RA Khoshdel Nezamiha F., Imani S., Shahbazzadeh D., Tirgari S.,
RA Arabi Mianroodi R.;
RT "Cloning and expression of OdTx12, a beta excitatory toxin from
RT Odontobuthus doriae, in Escherichia coli and evaluation of its bioactivity
RT in Locusta migratoria.";
RL Toxicon 183:20-28(2020).
RN [4]
RP BIOTECHNOLOGY, AND RECOMBINANT EXPRESSION AS A CHIMERIC VARIANT.
RX PubMed=34537212; DOI=10.1016/j.toxicon.2021.09.001;
RA Khoshdel Nezamiha F., Imani S., Arabi Mianroodi R., Tirgari S.,
RA Shahbazzadeh D.;
RT "OdTx12/GNA, a chimeric variant of a beta excitatory toxin from
RT Odontobuthus doriae, reveals oral toxicity towards Locusta migratoria and
RT Tenebrio molitor.";
RL Toxicon 202:13-19(2021).
CC -!- FUNCTION: Excitatory insect beta-toxins induce a spastic paralysis
CC (PubMed:32442468). They 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 (By similarity). In vivo, this
CC recombinant protein is lethal to Locusta migratoria larvae after
CC injection, but has no significant effect when orally administered. Is
CC not toxic to mice after intracerebroventricular injection
CC (PubMed:32442468). {ECO:0000250|UniProtKB:O61668,
CC ECO:0000269|PubMed:32442468}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:27426055,
CC ECO:0000305|PubMed:32442468}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:27426055, ECO:0000305|PubMed:32442468}.
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 -!- TOXIC DOSE: LD(50) is 0.4 ug/100 mg of insect (after 48 hours) and 0.2
CC ug/100 mg of insect (after 72 hours) by injection into Locusta
CC migratoria larvae. {ECO:0000269|PubMed:32442468}.
CC -!- BIOTECHNOLOGY: Could be considered as a biological insecticide
CC candidate, when fused to Galanthus nivalis agglutinin (GNA), a protein
CC with the potential to cross the insect gut. This chimeric OdTx12/GNA
CC variant shows a gain in toxicity against insects when administered
CC orally, while maintaining similar effects as the wild-type toxin when
CC injected (toxic to insects and non-toxic to mammals).
CC {ECO:0000269|PubMed:34537212}.
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; KU295411; ALY87543.1; -; mRNA.
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 Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN <1..64
FT /note="Beta-insect excitatory toxin OdTx12"
FT /id="PRO_0000455071"
FT DOMAIN 1..59
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 10..31
FT /evidence="ECO:0000250|UniProtKB:P56637"
FT DISULFID 16..36
FT /evidence="ECO:0000250|UniProtKB:P56637"
FT DISULFID 20..38
FT /evidence="ECO:0000250|UniProtKB:P56637"
FT DISULFID 32..58
FT /evidence="ECO:0000250|UniProtKB:P56637"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ALY87543.1"
SQ SEQUENCE 64 AA; 7217 MW; E899DA473DDCE9B7 CRC64;
QSTGGKAPEC LLSNYCNNEC TKVHYADKGY CCLLSCYCFG LSDDKKVLEI SDSRKKYCDY
TIIN
