D212_DORVU
ID D212_DORVU Reviewed; 60 AA.
AC P0DUS6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=DELTA-limacoditoxin(2)-Dv12 {ECO:0000303|PubMed:33893140};
DE Short=DELTA-LCTX(2)-Dv12 {ECO:0000303|PubMed:33893140};
DE AltName: Full=Cecropin-like peptide {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 25-60, SUBCELLULAR
RP LOCATION, TOXIC DOSE, AND 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: Peptide that induces pain in mammals and has insecticidal,
CC antimicrobial and antiparasitic activities. Induces irreversible
CC paralysis in D.melanogaster when tested at high doses. Shows a moderate
CC antiparasitic activity against the major pathogenic nematode of
CC ruminants (H.contortus, EC(50)=24.5 uM). Has moderate to potent
CC antimicrobial activities against all Gram-positive and -negative
CC bacteria tested, and against the fungus C.neoformans (var. grubii), but
CC has no activity against the fungus C.albicans. Strongly induces the
CC increase of intracellular calcium in mice DRG neurons, which is a proxy
CC for neuronal activation that would occur during nociception. This
CC increase is due to influx of extracellular calcium, suggesting that the
CC peptide forms pore or channel in neuronal cell membranes. In addition,
CC intraplantar injection in mice provokes nocifensive behavior,
CC suggesting a pain-inducing activity. {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 -!- MASS SPECTROMETRY: Mass=3992.4; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:33893140};
CC -!- TOXIC DOSE: PD(50) is 4.01 nmol/g when injected into D.melanogaster.
CC {ECO:0000269|PubMed:33893140}.
CC -!- SIMILARITY: Belongs to the limacoditoxin-2 (cecropin-like) family.
CC {ECO:0000305}.
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DR SMR; P0DUS6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:33893140"
FT PEPTIDE 25..60
FT /note="DELTA-limacoditoxin(2)-Dv12"
FT /evidence="ECO:0000269|PubMed:33893140"
FT /id="PRO_0000453402"
SQ SEQUENCE 60 AA; 6714 MW; 701F6397684BC877 CRC64;
MKLIKTFLFL FVVLLVLSEV SAEPRFGRLI RLIVKIARRA HRARSAVKAA SNVAELAHGE