ID   TRIP1_TRIIF             Reviewed;         182 AA.
AC   Q18NS7;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Triplatin {ECO:0000303|PubMed:22159626, ECO:0000303|PubMed:26110417};
DE   AltName: Full=Platelet inhibitor triplatin-1 {ECO:0000303|PubMed:16759235};
DE            Short=Tripla-1 {ECO:0000312|EMBL:BAE96121.1};
DE   Flags: Precursor;
OS   Triatoma infestans (Assassin bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Triatoma.
OX   NCBI_TaxID=30076;
RN   [1] {ECO:0000312|EMBL:BAE96121.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   RECOMBINANT EXPRESSION.
RC   TISSUE=Salivary gland;
RX   PubMed=16759235; DOI=10.1111/j.1742-4658.2006.05306.x;
RA   Morita A., Isawa H., Orito Y., Iwanaga S., Chinzei Y., Yuda M.;
RT   "Identification and characterization of a collagen-induced platelet
RT   aggregation inhibitor, triplatin, from salivary glands of the assassin bug,
RT   Triatoma infestans.";
RL   FEBS J. 273:2955-2962(2006).
RN   [2]
RP   FUNCTION, AND RECOMBINANT EXPRESSION.
RX   PubMed=22159626; DOI=10.1160/th11-10-0685;
RA   Ma D., Assumpcao T.C., Li Y., Andersen J.F., Ribeiro J.,
RA   Francischetti I.M.;
RT   "Triplatin, a platelet aggregation inhibitor from the salivary gland of the
RT   triatomine vector of Chagas disease, binds to TXA(2) but does not interact
RT   with glycoprotein PVI.";
RL   Thromb. Haemost. 107:111-123(2012).
RN   [3]
RP   FUNCTION, AND RECOMBINANT EXPRESSION.
RX   PubMed=26110417; DOI=10.1371/journal.pntd.0003869;
RA   Mizurini D.M., Aslan J.S., Gomes T., Ma D., Francischetti I.M.,
RA   Monteiro R.Q.;
RT   "Salivary thromboxane A2-binding proteins from triatomine vectors of Chagas
RT   disease inhibit platelet-mediated neutrophil extracellular traps (NETs)
RT   formation and arterial thrombosis.";
RL   PLoS Negl. Trop. Dis. 9:e0003869-e0003869(2015).
CC   -!- FUNCTION: Inhibits platelet aggregation and vasoconstriction through
CC       binding to distinct eicosanoids involved in inflammation (acts as a
CC       scavenger), and has a role in inhibiting host innate immunity by
CC       impairing platelet-assisted formation of neutrophil extracellular traps
CC       (NETs) (PubMed:22159626, PubMed:26110417). Inhibits platelet
CC       aggregation by collagen, and low doses of thromboxane A2 mimetic (TXA2
CC       mimetic), and arachidonic acid (AA) without affecting aggregation
CC       induced by ADP, convulxin (GP6 agonist), and PMA (PubMed:16759235,
CC       PubMed:22159626, PubMed:26110417). Binds to TXA2, TXB2, prostaglandine
CC       H2 mimetic (PGH2 mimetic), PGJ2, and PGF2alpha (PubMed:22159626).
CC       Binding is not observed to leukotrienes, AA, and biogenic amines (PGE1,
CC       5(S)-HETE, 12(S)-HETE, 20-HETE, norepinephrine, epinephrine,
CC       serotonine, LTC4 and ADP) (PubMed:22159626). Induces relaxation of
CC       aorta rat previously contracted with TXA2 mimetic (PubMed:22159626).
CC       Moreover, it also impairs platelet-assisted formation of neutrophil
CC       extracellular traps (NETs) (PubMed:26110417). NETs are web-like
CC       structures of DNA and proteins that play an important role in killing
CC       of pathogens (PubMed:26110417). In addition, NETs are implicated in
CC       thrombus formation (PubMed:26110417). In vivo, this protein exhibits
CC       antithrombotic activity in two distinct mice models that are highly
CC       dependent on platelets (PubMed:26110417). It is noteworthy that it
CC       inhibits thrombosis without promoting excessive bleeding
CC       (PubMed:26110417). {ECO:0000269|PubMed:16759235,
CC       ECO:0000269|PubMed:22159626, ECO:0000269|PubMed:26110417}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16759235}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000269|PubMed:16759235}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Triabin family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Morita et al. (2006) suggested that this protein inhibits
CC       collagen-induce platelet aggregation by binding to platelet
CC       glycoprotein VI, but a surface plasmon resonance experiment failed to
CC       demonstrate an interaction between these two proteins.
CC       {ECO:0000269|PubMed:22159626}.
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DR   EMBL; AB250209; BAE96121.1; -; mRNA.
DR   GO; GO:0030682; P:mitigation of host defenses by symbiont; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR005657; Triabi/Procalin.
DR   Pfam; PF03973; Triabin; 1.
DR   SUPFAM; SSF50814; SSF50814; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..182
FT                   /note="Triplatin"
FT                   /id="PRO_5004187176"
FT   DISULFID        21..133
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
FT   DISULFID        55..177
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
FT   DISULFID        88..105
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
SQ   SEQUENCE   182 AA;  19771 MW;  D7ED0C81CCFAFFE6 CRC64;
     MKMIIAVTFL GIVTIAFAEE CRLMQPAANF DAATYFSIPH VYVTHSKNEP KTDVCREYDT
     SKTDGGSTTV ITSNYKIKGQ AVNNKVTCTS TGLKNGQTGQ FSVVCQPPTG AAVTLTTSVL
     ATDNQNYAIL QRCPTSGQGN ILVLQTAKEG VNPGVKDFFQ KKGWNIDSWF SRTNVNCENI
     QS