PI21_PLARH
ID PI21_PLARH Reviewed; 139 AA.
AC A0A6B9KZ59;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=U-reduvitoxin-Pr21 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr21 {ECO:0000303|PubMed:31752210};
DE AltName: Full=Protease inhibitor {ECO:0000255|PIRNR:PIRNR001625};
DE Contains:
DE RecName: Full=U-reduvitoxin-Pr21a.1 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr21a.1 {ECO:0000303|PubMed:31752210};
DE Contains:
DE RecName: Full=U-reduvitoxin-Pr21a.2 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr21a.2 {ECO:0000303|PubMed:31752210};
DE Contains:
DE RecName: Full=U-reduvitoxin-Pr21a.3 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr21a.3 {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-Pr21a.2]: Mass=3699.72; 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; MN208337; QHB21526.1; -; 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 InterPro; IPR016307; Prtase-inh_pacifastin.
DR Pfam; PF05375; Pacifastin_I; 2.
DR PIRSF; PIRSF001625; Prot_inhib_pacifastin; 1.
DR SUPFAM; SSF57283; SSF57283; 2.
DR PROSITE; PS51446; PACIFASTIN; 3.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; Protease inhibitor;
KW Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..57
FT /note="U-reduvitoxin-Pr21a.1"
FT /evidence="ECO:0000305|PubMed:31752210"
FT /id="PRO_0000454317"
FT CHAIN 59..91
FT /note="U-reduvitoxin-Pr21a.2"
FT /evidence="ECO:0000269|PubMed:31752210"
FT /id="PRO_5025721048"
FT CHAIN 98..139
FT /note="U-reduvitoxin-Pr21a.3"
FT /evidence="ECO:0000305|PubMed:31752210"
FT /id="PRO_0000454318"
FT DOMAIN 19..55
FT /note="Pacifastin 1"
FT /evidence="ECO:0000305"
FT DOMAIN 58..93
FT /note="Pacifastin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DOMAIN 106..139
FT /note="Pacifastin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT SITE 87..88
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 21..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 33..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 36..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 61..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 71..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 74..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 109..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 121..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 124..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
SQ SEQUENCE 139 AA; 15580 MW; B0F3D15DE02240BD CRC64;
MKTALFLLFA LVFIAVEARF CTPGQRIRAP DGCNWCRCTK GGRIGGCTKM FCRKNLVKMD
CKPGKKFKID CNTCICSKEG KAAACTQKLC LKKRPKRSLI NIEKSERNCK PGQNYMSKDR
CKKCVCMKDG NSACTKVKC
