U332_DORVU
ID U332_DORVU Reviewed; 59 AA.
AC P0DUS8;
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(3)-Dv32a {ECO:0000303|PubMed:33893140};
DE Short=U-LCTX(3)-Dv32a {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 18-59, FUNCTION,
RP SUBCELLULAR LOCATION, 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: Probable toxin. Does not induce increase in intracellular
CC calcium in 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 -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000305|PubMed:33893140}.
CC -!- MASS SPECTROMETRY: Mass=4806.0; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:33893140};
CC -!- SIMILARITY: Belongs to the limacoditoxin-3 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 Direct protein sequencing; Disulfide bond; Knottin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:33893140"
FT PEPTIDE 18..59
FT /note="U-limacoditoxin(3)-Dv32a"
FT /evidence="ECO:0000269|PubMed:33893140"
FT /id="PRO_0000453404"
FT DISULFID 22..38
FT /evidence="ECO:0000305|PubMed:33893140"
FT DISULFID 29..44
FT /evidence="ECO:0000305|PubMed:33893140"
FT DISULFID 37..53
FT /evidence="ECO:0000305|PubMed:33893140"
SQ SEQUENCE 59 AA; 6624 MW; 5BDC2173E29160E1 CRC64;
MLRLIMIVTA LILLAAAEPE DCSWPDEHCN LFKTGQCCDR SMSCVVKNWK TVCSAGWFS