ID   Z14_DORVU               Reviewed;          35 AA.
AC   P0DUS3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   23-FEB-2022, entry version 2.
DE   RecName: Full=Z-limacoditoxin(1)-Dv4 {ECO:0000303|PubMed:33893140};
DE            Short=Z-LCTX(1)-Dv4 {ECO:0000303|PubMed:33893140};
DE   AltName: Full=Vulnericin {ECO:0000303|PubMed:33893140};
DE   Flags: Precursor;
OS   Doratifera vulnerans (Mottled cup moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Zygaenoidea;
OC   Limacodidae; Doratifera.
OX   NCBI_TaxID=1372962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-32, FUNCTION,
RP   SUBCELLULAR LOCATION, PYROGLUTAMATE FORMATION AT GLN-23, AMIDATION AT
RP   PRO-32, SYNTHESIS OF 23-32, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=33893140; DOI=10.1073/pnas.2023815118;
RA   Walker A.A., Robinson S.D., Paluzzi J.V., Merritt D.J., Nixon S.A.,
RA   Schroeder C.I., Jin J., Goudarzi M.H., Kotze A.C., Dekan Z., Sombke A.,
RA   Alewood P.F., Fry B.G., Epstein M.E., Vetter I., King G.F.;
RT   "Production, composition, and mode of action of the painful defensive venom
RT   produced by a limacodid caterpillar, Doratifera vulnerans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC   -!- FUNCTION: Potently activates insect GPCR. More precisely, it activates
CC       the ACP receptor (ACPR) from the mosquito A.aegypti (EC(50)=3.07 nM)
CC       with a potency comparable to that of the endogenous ligand. Has no
CC       activity on receptors of the closely related neuropeptides adipokinetic
CC       hormone and corazonin. In vivo, does not reveal any observable effects
CC       when injected into crickets (A.domesticus). Does not induce increase in
CC       intracellular calcium in mouse DRG neurons, suggesting that it does not
CC       induce pain. {ECO:0000269|PubMed:33893140}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33893140}.
CC   -!- TISSUE SPECIFICITY: Expressed by the spine venom secretory cell. The
CC       spine is a cuticular structure containing at its base a single large
CC       nucleated venom secretory cell, as well as a central venom reservoir
CC       extending throughout the spine. It is an independent unit capable of
CC       producing, storing, and injecting venom. Spines are grouped by 50 to
CC       100 in each of the eight venom scoli on the back of D.vulnerans
CC       caterpillars. {ECO:0000269|PubMed:33893140}.
CC   -!- DEVELOPMENTAL STAGE: Only secreted by caterpillars. Adult moth do not
CC       have spines. {ECO:0000269|PubMed:33893140}.
CC   -!- MISCELLANEOUS: Extremely abundant peptide in the venom (almost one-
CC       quarter of all toxin-encoding transcripts, and the highest represented
CC       peptide by proteomics methods). {ECO:0000305|PubMed:33893140}.
CC   -!- SIMILARITY: Belongs to the limacoditoxin-1 (ACP-like) family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing;
KW   G-protein coupled receptor impairing toxin; Pyrrolidone carboxylic acid;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT   PEPTIDE         23..32
FT                   /note="Z-limacoditoxin(1)-Dv4"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453399"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT   MOD_RES         32
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:33893140"
SQ   SEQUENCE   35 AA;  4023 MW;  47C8A071228F85E8 CRC64;
     MKKTFLPIFL VILLASYALG NPQITFSKDW RPGKK