ID   PLK1A_PLABI             Reviewed;          29 AA.
AC   P0DV13;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=U-reduvitoxin-Pbi1a {ECO:0000305};
DE            Short=U-RDTX-Pbi1a {ECO:0000305};
DE   AltName: Full=Pbi1a {ECO:0000303|PubMed:31752210, ECO:0000303|Ref.1};
OS   Platymeris biguttatus (Two-spotted assassin bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Platymeris.
OX   NCBI_TaxID=2588089;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Moore E.L.;
RT   "A biochemical and molecular analysis of venom with distinct physiological
RT   actions from two arthropod sources: the parasitoid jewel wasp, Ampulex
RT   compressa, of the insect order hymenoptera and the obligate entomophagous
RT   assassin bug, Platymeris biguttata, of the insect order hemiptera.";
RL   Thesis (2003), University of California, United States.
RN   [2]
RP   REVIEW.
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|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the venom Ptu1-like knottin family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   PEPTIDE         1..29
FT                   /note="U-reduvitoxin-Pbi1a"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000454321"
FT   DISULFID        1..15
FT                   /evidence="ECO:0000250|UniProtKB:P58606"
FT   DISULFID        8..20
FT                   /evidence="ECO:0000250|UniProtKB:P58606"
FT   DISULFID        14..25
FT                   /evidence="ECO:0000250|UniProtKB:P58606"
SQ   SEQUENCE   29 AA;  3098 MW;  439451619811882E CRC64;
     CIPAANPCRG NARCCGNYVC KNGRCLPRS