ID   PI10A_PLARH             Reviewed;          97 AA.
AC   A0A6B9KZ89;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=U-reduvitoxin-Pr10a {ECO:0000303|PubMed:31752210};
DE            Short=U-RDTX-Pr10a {ECO:0000303|PubMed:31752210};
DE   AltName: Full=Venom pacifastin domain peptide Pr10a {ECO:0000312|EMBL:QHB21530.1};
DE   Contains:
DE     RecName: Full=U-reduvitoxin-Pr10a.1 {ECO:0000303|PubMed:31752210};
DE              Short=U-RDTX-Pr10a.1 {ECO:0000303|PubMed:31752210};
DE   Contains:
DE     RecName: Full=U-reduvitoxin-Pr10a.2 {ECO:0000303|PubMed:31752210};
DE              Short=U-RDTX-Pr10a.2 {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, AND SUBCELLULAR LOCATION.
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: Inhibits trypsin activity and prophenoloxidase (PPO)
CC       activation, an enzyme essential for both clotting and insect innate
CC       immune responses. It does not inhibit activity of chymotrypsin and
CC       protease K, and has no effect on phenoloxidase (PO) activity.
CC       {ECO:0000250|UniProtKB:A0A7M6UNN1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31752210}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31752210}.
CC   -!- MASS SPECTROMETRY: [U-reduvitoxin-Pr10a.2]: Mass=4158.78; Method=MALDI;
CC       Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:31752210};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC       {ECO:0000305}.
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DR   EMBL; MN208341; QHB21530.1; -; mRNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008037; Pacifastin_dom.
DR   InterPro; IPR036201; Pacifastin_dom_sf.
DR   Pfam; PF05375; Pacifastin_I; 2.
DR   SUPFAM; SSF57283; SSF57283; 2.
DR   PROSITE; PS51446; PACIFASTIN; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond; Protease inhibitor; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..59
FT                   /note="U-reduvitoxin-Pr10a.1"
FT                   /evidence="ECO:0000305|PubMed:31752210"
FT                   /id="PRO_0000454314"
FT   CHAIN           60..97
FT                   /note="U-reduvitoxin-Pr10a.2"
FT                   /evidence="ECO:0000269|PubMed:31752210"
FT                   /id="PRO_5025442757"
FT   DOMAIN          22..59
FT                   /note="Pacifastin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DOMAIN          62..97
FT                   /note="Pacifastin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   REGION          57..59
FT                   /note="Pro-Pro-Arg motif necessary for proteolytic
FT                   processing"
FT                   /evidence="ECO:0000305|PubMed:31752210"
FT   SITE            53..54
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        24..42
FT                   /evidence="ECO:0000305|PubMed:31752210"
FT   DISULFID        37..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        40..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        65..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        77..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        80..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
SQ   SEQUENCE   97 AA;  10470 MW;  793C6095E423ED9B CRC64;
     MKTALFLVFA LAFIAVEGKF SKACSKPGQT VLAPDGCNHC RCSKNGIIMG CTKKMCPPRT
     MKQSCKPGAT FKHKDGCNTC KCSDDGKSAR CTARLCW