ID   U5928_DORVU             Reviewed;          66 AA.
AC   P0DUT6;
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=U-limacoditoxin(59)-Dv128 {ECO:0000303|PubMed:33893140};
DE            Short=U-LCTX(59)-Dv128 {ECO:0000303|PubMed:33893140};
DE   AltName: Full=Vulnericin {ECO:0000303|PubMed:33893140};
DE   Contains:
DE     RecName: Full=U-LCTX(59)-Dv128 peptide 1 {ECO:0000305};
DE   Contains:
DE     RecName: Full=U-LCTX(59)-Dv128 peptide 2 {ECO:0000305};
DE   Contains:
DE     RecName: Full=U-LCTX(59)-Dv128 peptide 3 {ECO:0000305};
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 21-31, FUNCTION,
RP   SUBCELLULAR LOCATION, AMIDATION AT GLY-31 AND GLY-47, AND IDENTIFICATION BY
RP   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: Probable toxin. {ECO:0000305}.
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   -!- SIMILARITY: Belongs to the limacoditoxin-59 family. {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; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Repeat; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT   PEPTIDE         21..31
FT                   /note="U-LCTX(59)-Dv128 peptide 1"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453417"
FT   PROPEP          33..37
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453418"
FT   PEPTIDE         38..47
FT                   /note="U-LCTX(59)-Dv128 peptide 2"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453419"
FT   PROPEP          49..53
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453420"
FT   PEPTIDE         54..66
FT                   /note="U-LCTX(59)-Dv128 peptide 3"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453421"
FT   REPEAT          22..37
FT                   /note="1"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   REPEAT          38..53
FT                   /note="2"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   REPEAT          54..64
FT                   /note="3; half-length"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   REGION          21..66
FT                   /note="3 X 16 AA tandem repeats of [FI]-G-G-G-L-G-G-A-V-G-
FT                   G-R-R-R-R-D"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   MOD_RES         31
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT   MOD_RES         47
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:33893140"
SQ   SEQUENCE   66 AA;  6427 MW;  0103EE5034CD7629 CRC64;
     MRHLLVLLLI CLSVIAMAQA TFGGGLGGAV GGRRRRDIGG GLGGAVGGRR RRDIGGGLGG
     AVGGKS