D211_DORVU
ID D211_DORVU Reviewed; 57 AA.
AC P0DUS5;
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=DELTA-limacoditoxin(2)-Dv11 {ECO:0000303|PubMed:33893140};
DE Short=DELTA-LCTX(2)-Dv11 {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 25-57, FUNCTION,
RP SUBCELLULAR LOCATION, TOXIC DOSE, 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: Peptide that induces pain in mammals and has insecticidal,
CC antibacterial and antiparasitic activities. Induces partially
CC reversible paralysis in D.melanogaster when tested at high doses. Shows
CC a moderate antiparasitic activity against the major pathogenic nematode
CC of ruminants (H.contortus, EC(50)=30.5 uM). Has potent or moderate
CC antibacterial activities against A.baumannii (MIC<0.25 ug/mL) and
CC S.aureus (MIC=16 ug/mL). Has no activity on the other bacteria tested,
CC nor on the fungus C.albicans. Strongly induces the increase of
CC intracellular calcium in mice DRG neurons, which is a proxy for
CC neuronal activation that would occur during nociception. This increase
CC is due to influx of extracellular calcium, suggesting that the peptide
CC 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 -!- TOXIC DOSE: PD(50) is 4.73 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 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.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:33893140"
FT PEPTIDE 25..57
FT /note="DELTA-limacoditoxin(2)-Dv11"
FT /evidence="ECO:0000269|PubMed:33893140"
FT /id="PRO_0000453401"
SQ SEQUENCE 57 AA; 6154 MW; B823362B755DAC7D CRC64;
MKFAKTFLLL FVVLLLLSIV MAEPKRGFGK LLRKVFKVGR RVAGSAAEIS GSSGGEE