Z11_DORVU
ID Z11_DORVU Reviewed; 35 AA.
AC P0DUS2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 25-MAY-2022, entry version 3.
DE RecName: Full=Z-limacoditoxin(1)-Dv1 {ECO:0000303|PubMed:33893140};
DE Short=Z-LCTX(1)-Dv1 {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 G protein-coupled receptor. It
CC activates the ACP receptor (ACPR) from the mosquito A.aegypti
CC (EC(50)=0.55 nM) with a potency comparable to that of the endogenous
CC ligand. Has no activity on receptors of the closely related
CC neuropeptides adipokinetic hormone and corazonin. In vivo, does not
CC reveal any observable effects when injected into crickets
CC (A.domesticus). Does not induce increase in intracellular calcium in
CC mouse DRG neurons, suggesting that it does not induce pain.
CC {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:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR002047; Adipokinetic_hormone_CS.
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)-Dv1"
FT /evidence="ECO:0000269|PubMed:33893140"
FT /id="PRO_0000453398"
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; 3952 MW; A1E8A0699DFF85F8 CRC64;
MKKTFLPIFL VILLASYALA NPQVTFSRDW GPGKK