ID   PLK1A_PLARH             Reviewed;          54 AA.
AC   A0A6B9KZ83;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=U-reduvitoxin-Pr1a {ECO:0000303|PubMed:31752210};
DE            Short=U-RDTX-Pr1a {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], MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   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: Binds reversibly and blocks P/Q-type voltage-gated calcium
CC       channels (Cav). {ECO:0000250|UniProtKB:P58608}.
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   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=3835.62; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:31752210};
CC   -!- SIMILARITY: Belongs to the venom Ptu1-like knottin family.
CC       {ECO:0000305}.
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DR   EMBL; MN208345; QHB21534.1; -; mRNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012325; Assassin_bug_toxin-like.
DR   Pfam; PF08117; Toxin_30; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..54
FT                   /note="U-reduvitoxin-Pr1a"
FT                   /evidence="ECO:0000269|PubMed:31752210"
FT                   /id="PRO_5025350039"
FT   DISULFID        24..39
FT                   /evidence="ECO:0000250|UniProtKB:P58606"
FT   DISULFID        31..44
FT                   /evidence="ECO:0000250|UniProtKB:P58606"
FT   DISULFID        38..51
FT                   /evidence="ECO:0000250|UniProtKB:P58606"
SQ   SEQUENCE   54 AA;  5939 MW;  654AF86FA3C38FA7 CRC64;
     MKLLGLLLLV FTFMALAFAD EKDCIARGQK CVGENKPCCK GTTCMYYANR CVGV