LAIT1_LIOAU
ID LAIT1_LIOAU Reviewed; 36 AA.
AC P0C5F2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Insecticidal toxin LaIT1;
OS Liocheles australasiae (Dwarf wood scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae; Liocheles.
OX NCBI_TaxID=431266;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, BIOASSAY, TOXIC DOSE, MASS SPECTROMETRY, AND
RP DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=17681581; DOI=10.1016/j.toxicon.2007.06.014;
RA Matsushita N., Miyashita M., Sakai A., Nakagawa Y., Miyagawa H.;
RT "Purification and characterization of a novel short-chain insecticidal
RT toxin with two disulfide bridges from the venom of the scorpion Liocheles
RT australasiae.";
RL Toxicon 50:861-867(2007).
RN [2]
RP STRUCTURE BY NMR, DISULFIDE BONDS, FUNCTION, BIOASSAY, SYNTHESIS, AND
RP MUTAGENESIS OF ARG-13; ARG-15 AND LYS-16.
RX PubMed=21782787; DOI=10.1016/j.bbrc.2011.07.016;
RA Horita S., Matsushita N., Kawachi T., Ayabe R., Miyashita M., Miyakawa T.,
RA Nakagawa Y., Nagata K., Miyagawa H., Tanokura M.;
RT "Solution structure of a short-chain insecticidal toxin LaIT1 from the
RT venom of scorpion Liocheles australasiae.";
RL Biochem. Biophys. Res. Commun. 411:738-744(2011).
CC -!- FUNCTION: Affects the activity of both ryanodine-sensitive calcium-
CC release channels RyR1 and RyR2 with high potency. At lower
CC concentrations the toxin increases full openings of the RyRs, and at
CC higher concentrations it inhibits full openings and induce openings to
CC subconductance levels and reduces the number of full conductance
CC openings. The different actions may be attributed to the toxins binding
CC at different sites on the RyRs, with binding at a high-affinity site
CC mediating the increase in full openings and the induction of
CC subconductance states evoked upon binding to a lower-affinity site (By
CC similarity). Shows insect lethality against crickets and common
CC cutworms (only shows paralysis against cockroaches), but no toxicity is
CC observed in mice. {ECO:0000250, ECO:0000269|PubMed:17681581,
CC ECO:0000269|PubMed:21782787}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=4200.02; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17681581};
CC -!- TOXIC DOSE: LD(50) is 22 mg/kg when injected into crickets (Orthoptera)
CC and LD(50) is 52 mg/kg when injected into common cutworms
CC (Lepidoptera). PD(50) (irreversible paralysis) is 120 mg/kg when
CC injected into cockroaches (observed 48 hours post-injection).
CC {ECO:0000269|PubMed:17681581}.
CC -!- MISCELLANEOUS: This toxxin may reach its physiological target by
CC traversing membranes, which may be by slow permeation. Alternatively,
CC scorpion venoms are known to contain amphipathic helical peptides that
CC form pores in the cell membrane, and it is possible that these pores
CC would allow this toxin to enter the cell (By similarity).
CC {ECO:0000250}.
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DR PDB; 2LDS; NMR; -; A=1-36.
DR PDBsum; 2LDS; -.
DR AlphaFoldDB; P0C5F2; -.
DR BMRB; P0C5F2; -.
DR SMR; P0C5F2; -.
DR EvolutionaryTrace; P0C5F2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin;
KW Ryanodine-sensitive calcium-release channel impairing toxin; Secreted;
KW Toxin.
FT CHAIN 1..36
FT /note="Insecticidal toxin LaIT1"
FT /id="PRO_0000305106"
FT DISULFID 11..23
FT DISULFID 17..29
FT MUTAGEN 13
FT /note="R->A: 4.2-fold reduction in insecticidal activity."
FT /evidence="ECO:0000269|PubMed:21782787"
FT MUTAGEN 15
FT /note="R->A: 12-fold reduction in insecticidal activity."
FT /evidence="ECO:0000269|PubMed:21782787"
FT MUTAGEN 16
FT /note="K->A: No effect in insecticidal activity."
FT /evidence="ECO:0000269|PubMed:21782787"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:2LDS"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2LDS"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2LDS"
SQ SEQUENCE 36 AA; 4207 MW; 8C3BFFCAE2FBD123 CRC64;
DFPLSKEYET CVRPRKCQPP LKCNKAQICV DPKKGW
