ID   TRIP2_TRIIF             Reviewed;         178 AA.
AC   Q18NS6;
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=Platelet inhibitor triplatin-2 {ECO:0000303|PubMed:16759235};
DE            Short=Tripla-2 {ECO:0000312|EMBL:BAE96122.1};
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:BAE96122.1}
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).
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). Inhibits platelet aggregation by collagen, and low doses of
CC       thromboxane A2 mimetic (TXA2 mimetic), and arachidonic acid (AA)
CC       without affecting aggregation induced by ADP, convulxin (GP6 agonist),
CC       and PMA. Binds to TXA2, TXB2, prostaglandine H2 mimetic (PGH2 mimetic),
CC       PGJ2, and PGF2alpha. Binding is not observed to leukotrienes, AA, and
CC       biogenic amines (PGE1, 5(S)-HETE, 12(S)-HETE, 20-HETE, norepinephrine,
CC       epinephrine, serotonine, LTC4 and ADP). Induces relaxation of aorta rat
CC       previously contracted with TXA2 mimetic. Moreover, it also impairs
CC       platelet-assisted formation of neutrophil extracellular traps (NETs).
CC       NETs are web-like structures of DNA and proteins that play an important
CC       role in killing of pathogens. In addition, NETs are implicated in
CC       thrombus formation. In vivo, this protein exhibits antithrombotic
CC       activity in two distinct mice models that are highly dependent on
CC       platelets. It is noteworthy that it inhibits thrombosis without
CC       promoting excessive bleeding. {ECO:0000250|UniProtKB:Q18NS7}.
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:0000250|UniProtKB:Q18NS7}.
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DR   EMBL; AB250210; BAE96122.1; -; 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..178
FT                   /note="Platelet inhibitor triplatin-2"
FT                   /id="PRO_5004187270"
FT   DISULFID        25..134
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
FT   DISULFID        60..178
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
FT   DISULFID        90..106
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
SQ   SEQUENCE   178 AA;  19538 MW;  4C76B08CC6CE9210 CRC64;
     MKMIISLTFL GILMLAFAEV NSETCTLMEA AKNFDENKYF NIPLAYATHS KNREPETNVC
     REYSTARGPD GKTVTTFTIK DKTLTSAVKC TNTPIPGSNG QFSSDCELSA GNRITVTTSI
     LATDNEKYAI LQRCPTSGPG NILVLQTNKN GVEQGVQNYF NQKGWDISTW LSRTTVGC