PI12A_PLARH
ID PI12A_PLARH Reviewed; 96 AA.
AC A0A6B9L3M7;
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-Pr12a {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr12a {ECO:0000303|PubMed:31752210};
DE AltName: Full=Venom pacifastin domain peptide Pr12a {ECO:0000312|EMBL:QHB21532.1};
DE Contains:
DE RecName: Full=U-reduvitoxin-Pr12a.1 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr12a.1 {ECO:0000303|PubMed:31752210};
DE Contains:
DE RecName: Full=U-reduvitoxin-Pr12a.2 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr12a.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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP 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 -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC {ECO:0000305}.
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DR EMBL; MN208343; QHB21532.1; -; 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; 1.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..56
FT /note="U-reduvitoxin-Pr12a.1"
FT /evidence="ECO:0000269|PubMed:31752210"
FT /id="PRO_5025501165"
FT CHAIN 57..96
FT /note="U-reduvitoxin-Pr12a.2"
FT /evidence="ECO:0000305|PubMed:31752210"
FT /id="PRO_0000454316"
FT DOMAIN 21..55
FT /note="Pacifastin 1"
FT /evidence="ECO:0000305"
FT DOMAIN 59..94
FT /note="Pacifastin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT REGION 54..56
FT /note="Pro-Pro-Arg motif necessary for proteolytic
FT processing"
FT /evidence="ECO:0000305|PubMed:31752210"
FT SITE 88..89
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..53
FT /evidence="ECO:0000305|PubMed:31752210"
FT DISULFID 36..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 62..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 72..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 75..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
SQ SEQUENCE 96 AA; 10560 MW; 395E483C16AAD1C1 CRC64;
MKTALLLFFA LVFIAFETEA CRPGALTVAP DGCNMCTCLS NGKLGRCTHD LICPPRMFKL
ECEPGKPFKN DCNDCICSED GLTAKCTRKL CIHKKP
