ID   RED2_PLARH              Reviewed;         242 AA.
AC   A0A6B9L900;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Venom redulysin 2 {ECO:0000303|PubMed:31752210};
DE            Short=Red2 {ECO:0000303|PubMed:31752210};
DE   Flags: Precursor;
OS   Platymeris rhadamanthus (Red spot assassin bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Platymeris.
OX   NCBI_TaxID=1134088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=31752210; DOI=10.3390/toxins11110673;
RA   Walker A.A., Robinson S.D., Undheim E.A.B., Jin J., Han X., Fry B.G.,
RA   Vetter I., King G.F.;
RT   "Missiles of mass disruption: composition and glandular origin of venom
RT   used as a projectile defensive weapon by the assassin bug Platymeris
RT   rhadamanthus.";
RL   Toxins 11:E673-E673(2019).
CC   -!- FUNCTION: Highly abundant protein that may be responsible for the
CC       observed disruption of sensory neuron membranes, since it is homologous
CC       to proteins such as trialysin, which forms pores in lipid bilayers
CC       (Probable). Probable insecticidal toxin (By similarity).
CC       {ECO:0000250|UniProtKB:P0DQR9, ECO:0000305|PubMed:31752210}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31752210}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland (posterior main gland)
CC       (at protein level). {ECO:0000269|PubMed:31752210}.
CC   -!- PTM: Contains 5 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the redulysin-like family. {ECO:0000305}.
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DR   EMBL; MN208354; QHB21543.1; -; mRNA.
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   Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..46
FT                   /evidence="ECO:0000250|UniProtKB:P0DQR9"
FT                   /id="PRO_0000454324"
FT   CHAIN           47..242
FT                   /note="Venom redulysin 2"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQR9"
FT                   /id="PRO_5025402274"
SQ   SEQUENCE   242 AA;  26859 MW;  A44F9AFDC338AB40 CRC64;
     MSKIWILLLL VGAVQFARGF PALEEEQEDD VIDWPSFEYD LSDEERGKGL DWLKKQWGKL
     KNSFKKVGAK VTATFNKGRD YLKKKGIKVD PLNCQGNKCR SCVIFTLKPK KFCIEYVFST
     SAITVSLIKE KDDEEKVLLG PFTIKTGNIP KCCKLGSFIG ELCLQGVEGR LKSSNGKPHV
     NLCVGLLLKK FGCGAKICVS YVDGKFSVSF KPKLFAGDEE NGTIMEAGEK EDEGKVIDAV
     PE