ID   PALL_MECPA              Reviewed;         188 AA.
AC   Q27042;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Pallidipin {ECO:0000303|PubMed:20889972};
DE   AltName: Full=Pallidipin 2 {ECO:0000303|PubMed:20889972, ECO:0000303|PubMed:8106481, ECO:0000312|EMBL:AAA30329.1};
DE   Flags: Precursor;
OS   Meccus pallidipennis (Triatomine bug) (Triatoma pallidipennis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Meccus.
OX   NCBI_TaxID=30077;
RN   [1] {ECO:0000312|EMBL:AAA30329.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38, FUNCTION, AND
RP   RECOMBINANT EXPRESSION.
RC   TISSUE=Saliva, and Salivary gland;
RX   PubMed=8106481; DOI=10.1016/s0021-9258(17)37652-4;
RA   Noeske-Jungblut C., Kratzschmar J., Haendler B., Alagon A., Possani L.,
RA   Verhallen P., Donner P., Schleuning W.D.;
RT   "An inhibitor of collagen-induced platelet aggregation from the saliva of
RT   Triatoma pallidipennis.";
RL   J. Biol. Chem. 269:5050-5053(1994).
RN   [2]
RP   3D-STRUCTURE MODELING, AND PROBABLE FUNCTION.
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).
CC   -!- FUNCTION: Has been described as a specific inhibitor of collagen-
CC       induced platelet aggregation (PubMed:8106481). However, as it does not
CC       affect platelet shape change or adhesion, it is plausible that it
CC       exerts its antiplatelet activity by a mechanism similar to that of
CC       triplatin, moubatin and dipetalodipin as scavenging eicosanoids
CC       involved in inflammation such as thromboxan A2 (TXA2) (PubMed:20889972)
CC       (By similarity). {ECO:0000250|UniProtKB:G3CJS0,
CC       ECO:0000250|UniProtKB:Q04669, ECO:0000250|UniProtKB:Q18NS7,
CC       ECO:0000269|PubMed:20889972, ECO:0000269|PubMed:8106481}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8106481}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000305|PubMed:8106481}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Triabin family.
CC       {ECO:0000305}.
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DR   EMBL; L11310; AAA30329.1; -; mRNA.
DR   PIR; A53329; A53329.
DR   PIR; B53329; B53329.
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.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..188
FT                   /note="Pallidipin"
FT                   /id="PRO_5004203121"
FT   DISULFID        21..137
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
FT   DISULFID        55..184
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
FT   DISULFID        89..105
FT                   /evidence="ECO:0000250|UniProtKB:Q27049"
FT   VARIANT         97
FT                   /note="V -> G (in pallidipin-1)"
FT                   /evidence="ECO:0000269|PubMed:8106481"
SQ   SEQUENCE   188 AA;  20761 MW;  1529BCD287D7DC87 CRC64;
     MKVIIAATLL GILMHAFAEE CELMPPGDNF DLEKYFSIPH VYVTHSRNGP KEQVCREYKT
     TKNSDGTTTT LVTSDYKTGG KPYHSELKCT NTPKSGVKGQ FSVECEVPNG NGGKKKIHVE
     TSVIATDYKN YALLQSCTKT ESGIADDVLL LQTKKEGVDP GVTSVLKSVN WSLDDWFSRS
     KVNCDNMK