ID   RED1_PLARH              Reviewed;         628 AA.
AC   A0A6B9KZ90;
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 1 {ECO:0000303|PubMed:31752210};
DE            Short=Red1 {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; MN208352; QHB21541.1; -; 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..368
FT                   /evidence="ECO:0000250|UniProtKB:P0DQR9"
FT                   /id="PRO_0000454323"
FT   CHAIN           369..628
FT                   /note="Venom redulysin 1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQR9"
FT                   /id="PRO_5025381628"
FT   REGION          290..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   628 AA;  72028 MW;  FFFBA52FA428C23A CRC64;
     MSKLWLLLLL VAAFQAVHSY PAAESDYLEE PETTWDILKE TWGKMKDHYL NLGKETLAKL
     KELKENYKTW GKEKKQQFIA TLKDKLCTPQ DFEEDIDYAE SDEDKDLSFT MKVLLILKET
     LDKLKAAVGE EKEKLIQEVK GLRAKICDKL SDYEEEEEFE LEEDYEEDPE TTWGILKEAW
     GKMKEHYLNL GKATLAKLKE LKENYKTWGK EKLQIFVAKL KDKLCTQQDF EEDIDYTESD
     EEKDPALTAK ILLKLKEYLE KLKSAAGKEK EKLIQKIKDL RAKICDKLSD YEEEEEEEEE
     EEFELEEDYE EDPQQTTWGI LKETFGKIKD RWSQLTKIQL QKIIQVLKNR YCADQNDFED
     DVAESDEEQG GRQVIQKYLQ KLKEFYEKIK AAVGAKKEEL KKRLEETRQK FCAKLNAAAE
     QNDLEEDEDE ERGWLGKLGK GLKKVGKKFV KKMSSAMKAG CKKGMKMLKD NAVKVTPLVC
     EEKTCKTLVT ILTYSCGMQY TITRTNKATY LEVAFIVNGE VKAKKNVKLG DVPSCVNLGA
     LLGKICLKGI EGKGKSSSGQ ANVNFCLAIL ADKYNVGCKF CASYANKKFK VLPPKMFSGA
     QDDNGEILQA SDNGEDGILL DADEFEID