PI11A_PLARH
ID PI11A_PLARH Reviewed; 97 AA.
AC A0A6B9KZ79;
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-Pr11a {ECO:0000305|PubMed:31752210};
DE Short=U-RDTX-Pr11a {ECO:0000305|PubMed:31752210};
DE AltName: Full=Venom pacifastin domain peptide Pr11a {ECO:0000312|EMBL:QHB21531.1};
DE Contains:
DE RecName: Full=U-reduvitoxin-Pr11a.1 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr11a.1 {ECO:0000303|PubMed:31752210};
DE Contains:
DE RecName: Full=U-reduvitoxin-Pr11a.2 {ECO:0000303|PubMed:31752210};
DE Short=U-RDTX-Pr11a.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-Pr11a.1]: Mass=4172.82; Method=MALDI;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:31752210};
CC -!- MASS SPECTROMETRY: [U-reduvitoxin-Pr11a.2]: Mass=4070.81; Method=MALDI;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:31752210};
CC -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MN208342; QHB21531.1; -; 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..20
FT /evidence="ECO:0000305|PubMed:31752210"
FT CHAIN 21..59
FT /note="U-reduvitoxin-Pr11a.1"
FT /evidence="ECO:0000269|PubMed:31752210"
FT /id="PRO_5025351512"
FT CHAIN 60..97
FT /note="U-reduvitoxin-Pr11a.2"
FT /evidence="ECO:0000269|PubMed:31752210"
FT /id="PRO_0000454315"
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 93..94
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; 10426 MW; 0DEF4FAB29197B57 CRC64;
MKTALFLVFA LAFIAVEGKM SRACSKPGQT VLAPDGCNHC RCSEKGILMA CTKMMCPPRT
IEKSCKPGTT FKHKDGCNTC KCSDDGKNAL CTSKLCL
