SIX1_ANDAU
ID SIX1_ANDAU Reviewed; 88 AA.
AC P01497;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Beta-insect excitatory toxin 1 {ECO:0000305};
DE AltName: Full=AaH IT1 {ECO:0000303|PubMed:2808423};
DE Short=AaH IT {ECO:0000303|PubMed:2808423};
DE Short=AaHIT;
DE Short=AaHIT1;
DE Short=AaIT {ECO:0000303|PubMed:25641865};
DE Short=AaIT1;
DE Flags: Precursor;
OS Androctonus australis (Sahara scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6858;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hector; TISSUE=Venom gland;
RX PubMed=2808423; DOI=10.1016/s0021-9258(19)47295-5;
RA Bougis P.E., Rochat H., Smith L.A.;
RT "Precursors of Androctonus australis scorpion neurotoxins. Structures of
RT precursors, processing outcomes, and expression of a functional recombinant
RT toxin II.";
RL J. Biol. Chem. 264:19259-19265(1989).
RN [2]
RP PROTEIN SEQUENCE OF 19-88, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC STRAIN=Hector; TISSUE=Venom;
RX PubMed=2334710; DOI=10.1021/bi00458a021;
RA Loret E.P., Mansuelle P., Rochat H., Granier C.;
RT "Neurotoxins active on insects: amino acid sequences, chemical
RT modifications, and secondary structure estimation by circular dichroism of
RT toxins from the scorpion Androctonus australis hector.";
RL Biochemistry 29:1492-1501(1990).
RN [3]
RP PROTEIN SEQUENCE OF 19-88, AND SUBCELLULAR LOCATION.
RC STRAIN=Hector; TISSUE=Venom;
RA Darbon H., Rochat H., Kopeyan C., van Rietschoten J., Zlotkin E.;
RT "Covalent structure of the insect toxin of Androctonus australis hector.";
RL Toxicon 20:64-64(1982).
RN [4]
RP BIOTECHNOLOGY, AND REVIEW.
RX PubMed=11086217; DOI=10.1016/s0300-9084(00)01177-9;
RA Zlotkin E., Fishman Y., Elazar M.;
RT "AaIT: from neurotoxin to insecticide.";
RL Biochimie 82:869-881(2000).
RN [5]
RP BIOTECHNOLOGY, AND RECOMBINANT EXPRESSION AS A CHIMERIC VARIANT IN
RP TRANSGENIC PLANTS.
RX PubMed=25641865; DOI=10.1111/1744-7917.12203;
RA Liu S.M., Li J., Zhu J.Q., Wang X.W., Wang C.S., Liu S.S., Chen X.X.,
RA Li S.;
RT "Transgenic plants expressing the AaIT/GNA fusion protein show increased
RT resistance and toxicity to both chewing and sucking pests.";
RL Insect Sci. 23:265-276(2016).
RN [6]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RC STRAIN=Hector;
RX PubMed=1993198; DOI=10.1021/bi00221a016;
RA Darbon H., Weber C., Braun W.;
RT "Two-dimensional 1H nuclear magnetic resonance study of AaH IT, an anti-
RT insect toxin from the scorpion Androctonus australis hector. Sequential
RT resonance assignments and folding of the polypeptide chain.";
RL Biochemistry 30:1836-1845(1991).
CC -!- FUNCTION: Excitatory insect beta-toxins induce a spastic paralysis.
CC They bind voltage-independently at site-4 of sodium channels (Nav) and
CC shift the voltage of activation toward more negative potentials thereby
CC affecting sodium channel activation and promoting spontaneous and
CC repetitive firing. This toxin is active only on insects.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2334710,
CC ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2334710, ECO:0000305|Ref.3}.
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: PD(50) is 0.099 ng/mg of insects.
CC {ECO:0000269|PubMed:2334710}.
CC -!- BIOTECHNOLOGY: Could be used to reinforce the natural insecticidal
CC ability of baculoviruses. The insertion of the gene coding for AaHIT
CC causes a higher killing speed of insects by the baculovirus
CC (particularly against lepidopterans). {ECO:0000269|PubMed:11086217}.
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 AaIT/GNA
CC variant shows increased resistance and toxicity to both chewing and
CC sucking pests (the cotton bollworm Helicoverpa armigera, the whitefly
CC Bemisia tabaci, and the rice brown planthopper Nilaparvata lugens),
CC when expressed in transgenic plants. {ECO:0000269|PubMed:25641865}.
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; M27706; AAA29951.1; -; mRNA.
DR EMBL; M27705; AAA29950.1; -; mRNA.
DR AlphaFoldDB; P01497; -.
DR BMRB; P01497; -.
DR SMR; P01497; -.
DR ABCD; P01497; 12 sequenced antibodies.
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 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; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
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; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000305|PubMed:2334710, ECO:0000305|Ref.3"
FT CHAIN 19..88
FT /note="Beta-insect excitatory toxin 1"
FT /evidence="ECO:0000269|PubMed:2334710, ECO:0000269|Ref.3"
FT /id="PRO_0000035187"
FT DOMAIN 20..83
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 34..55
FT /evidence="ECO:0000269|PubMed:1993198"
FT DISULFID 40..60
FT /evidence="ECO:0000269|PubMed:1993198"
FT DISULFID 44..62
FT /evidence="ECO:0000269|PubMed:1993198"
FT DISULFID 56..82
FT /evidence="ECO:0000269|PubMed:1993198"
FT VARIANT 17
FT /note="F -> L"
FT CONFLICT 43
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 88 AA; 9852 MW; E6FF097B3277748F CRC64;
MKFLLLFLVV LPIMGVFGKK NGYAVDSSGK APECLLSNYC NNECTKVHYA DKGYCCLLSC
YCFGLNDDKK VLEISDTRKS YCDTTIIN
