DPTL_DIPMA
ID DPTL_DIPMA Reviewed; 182 AA.
AC G3CJS0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Dipetalodipin {ECO:0000303|PubMed:20889972};
DE Short=DPTL {ECO:0000303|PubMed:20889972};
DE AltName: Full=Salivary lipocalin {ECO:0000312|EMBL:AEM97974.1};
DE Flags: Precursor;
OS Dipetalogaster maximus (Blood-sucking bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Dipetalogaster.
OX NCBI_TaxID=72496;
RN [1] {ECO:0000312|EMBL:AEM97974.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND 3D-STRUCTURE MODELING.
RC TISSUE=Salivary gland;
RX PubMed=20889972; DOI=10.1074/jbc.m110.152835;
RA Assumpcao T.C., Alvarenga P.H., Ribeiro J.M., Andersen J.F.,
RA Francischetti I.M.;
RT "Dipetalodipin, a novel multifunctional salivary lipocalin that inhibits
RT platelet aggregation, vasoconstriction, and angiogenesis through unique
RT binding specificity for TXA2, PGF2alpha, and 15(S)-HETE.";
RL J. Biol. Chem. 285:39001-39012(2010).
RN [2] {ECO:0000312|EMBL:AEM97974.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Salivary gland;
RX PubMed=21058630; DOI=10.1021/pr100866h;
RA Assumpcao T.C., Charneau S., Santiago P.B., Francischetti I.M., Meng Z.,
RA Araujo C.N., Pham V.M., Queiroz R.M., de Castro C.N., Ricart C.A.,
RA Santana J.M., Ribeiro J.M.;
RT "Insight into the salivary transcriptome and proteome of Dipetalogaster
RT maxima.";
RL J. Proteome Res. 10:669-679(2011).
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, vasoconstriction, and
CC angiogenesis through binding to distinct eicosanoids involved in
CC inflammation (acts as a scavenger), and has a role in inhibiting host
CC innate immunity by impairing platelet-assisted formation of neutrophil
CC extracellular traps (NETs) (PubMed:20889972, PubMed:26110417). Inhibits
CC platelet aggregation by collagen (IC(50)=30 nM), thromboxane A2 mimetic
CC (TXA2 mimetic), or arachidonic acid (AA) without affecting aggregation
CC induced by ADP, convulxin (GP6 agonist), PMA, and ristocetin (vWF-
CC dependent platelet agglutinator) (PubMed:20889972, PubMed:26110417).
CC Binds with high affinity to TXA2, TXB2, prostaglandine H2 mimetic (PGH2
CC mimetic), PGD2, PGJ2, and PGF2alpha (PubMed:20889972). Also interacts
CC with 15(S)-hydroxyeicosatetraenoic acid (HETE), being the first
CC calycin/lipocalin described to date to bind to a derivative of 15-
CC lipoxygenase (PubMed:20889972). Binding is not observed to other
CC prostaglandins, leukotrienes, HETEs, lipids, and biogenic amines
CC (PubMed:20889972). It prevents contraction of rat uterus stimulated by
CC PGF2alpha and induces relaxation of aorta previously contracted with
CC TXA2 mimetic (PubMed:20889972). In addition, it inhibits angiogenesis
CC mediated by 15(S)-HETE and does not enhance inhibition of collagen-
CC induced platelet aggregation by SQ29548 (TXA2 antagonist) and
CC indomethacin (PubMed:20889972). Also impairs platelet-assisted
CC formation of neutrophil extracellular traps (NETs) (PubMed:26110417).
CC NETs are web-like structures of DNA and proteins that play an important
CC role in killing of pathogens (PubMed:26110417). In addition, NETs are
CC implicated in thrombus formation (PubMed:26110417). In vivo, this
CC protein exhibits antithrombotic activity in two distinct mice models
CC that are highly dependent on platelets (PubMed:26110417). It is
CC noteworthy that it inhibits thrombosis without promoting excessive
CC bleeding (PubMed:26110417). {ECO:0000269|PubMed:20889972,
CC ECO:0000269|PubMed:26110417}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20889972}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC {ECO:0000305|PubMed:20889972}.
CC -!- MISCELLANEOUS: Very abundant protein in the salivary gland, accounting
CC for at least 30% of total salivary lipocalins.
CC {ECO:0000269|PubMed:20889972}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Triabin family.
CC {ECO:0000305}.
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DR EMBL; HP639837; AEM97974.1; -; 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin; Vasoactive;
KW Vasoconstrictor.
FT SIGNAL 1..18
FT /evidence="ECO:0000305|PubMed:20889972"
FT CHAIN 19..182
FT /note="Dipetalodipin"
FT /evidence="ECO:0000305|PubMed:20889972"
FT /id="PRO_5003443009"
FT DISULFID 21..134
FT /evidence="ECO:0000250|UniProtKB:Q27049"
FT DISULFID 55..181
FT /evidence="ECO:0000250|UniProtKB:Q27049"
FT DISULFID 87..103
FT /evidence="ECO:0000250|UniProtKB:Q27049"
SQ SEQUENCE 182 AA; 19763 MW; 433ADF67EC6C5167 CRC64;
MKTIIAAIFL GILMHAFAKE CTLMAAASNF NSDKYFDVPH VYVTHSKNGP KEKVCREYNT
TKNSDKTTST TVVTLKTGGT QSIVLSCNNS PKSGVKGQYF MDCQVPGGTG GINIQLESSI
IATDNKNYAL VHFCPITGRG VTEDIVVLQT NKDNVDPGVT SAIKNYGWSL ENWKSRKDAG
CQ
