ID   U866_DORVU              Reviewed;         158 AA.
AC   P0DUT2;
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=U-limacoditoxin(8)-Dv66 {ECO:0000303|PubMed:33893140};
DE            Short=U-LCTX(8)-Dv66 {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 33-63; 79-109 AND 125-155,
RP   FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT PRO-63; PRO-109 AND PRO-155,
RP   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: Probable toxin. Does not show insecticidal, antimicrobial and
CC       antiparasitic activities. 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   -!- MISCELLANEOUS: Is also classified in the limacoditoxin-8 (DH31) family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the diuretic hormone class 2 family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008613; F:diuretic hormone activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007589; P:body fluid secretion; IEA:InterPro.
DR   InterPro; IPR034439; DH2-like.
DR   PANTHER; PTHR41146; PTHR41146; 3.
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..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..32
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT                   /id="PRO_0000453408"
FT   PEPTIDE         33..63
FT                   /note="U-limacoditoxin(8)-Dv66"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453409"
FT   PROPEP          64..78
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453410"
FT   PEPTIDE         79..109
FT                   /note="U-limacoditoxin(8)-Dv66"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453411"
FT   PROPEP          110..124
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453412"
FT   PEPTIDE         125..155
FT                   /note="U-limacoditoxin(8)-Dv66"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT                   /id="PRO_0000453413"
FT   REPEAT          33..78
FT                   /note="1"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   REPEAT          79..124
FT                   /note="2"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   REPEAT          125..158
FT                   /note="3; half-length"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   REGION          33..158
FT                   /note="3 X 46 AA tandem repeats"
FT                   /evidence="ECO:0000305|PubMed:33893140"
FT   REGION          101..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         63
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT   MOD_RES         109
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:33893140"
FT   MOD_RES         155
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:33893140"
SQ   SEQUENCE   158 AA;  17547 MW;  1E34CFE4F60DC6BA CRC64;
     MALRAPWIAL CCVLAVLFVV PAATRDEERQ KRGVDFGLQR GFSGSELAKL KLALARAQDP
     HGPGRKRRDA YEMERQKRGV DFGLQRGFSG SELAKLKLAL ARAQDPHGPG RKRRDAYEME
     RQKRGVDFGL QRGFSGSELA KLKLALARAQ DPHGPGRK