ID   MOUB_ORNMO              Reviewed;         171 AA.
AC   Q04669;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Moubatin {ECO:0000303|PubMed:8449906, ECO:0000303|PubMed:8449907};
DE   AltName: Full=Lipocalin {ECO:0000303|PubMed:18694828};
DE   AltName: Full=Platelet aggregation inhibitor {ECO:0000303|PubMed:8449907};
DE            Short=PAI {ECO:0000305};
DE   Flags: Precursor;
OS   Ornithodoros moubata (Soft tick) (Argasid tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Argasidae; Ornithodoros.
OX   NCBI_TaxID=6938;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP   RECOMBINANT EXPRESSION.
RX   PubMed=8449907; DOI=10.1016/s0021-9258(18)53342-1;
RA   Keller P.M., Waxman L., Arnold B.A., Schultz L.D., Condra C.,
RA   Connolly T.M.;
RT   "Cloning of the cDNA and expression of moubatin, an inhibitor of platelet
RT   aggregation.";
RL   J. Biol. Chem. 268:5450-5456(1993).
RN   [2]
RP   FUNCTION.
RX   PubMed=8449906; DOI=10.1016/s0021-9258(18)53341-x;
RA   Waxman L., Connolly T.M.;
RT   "Isolation of an inhibitor selective for collagen-stimulated platelet
RT   aggregation from the soft tick Ornithodoros moubata.";
RL   J. Biol. Chem. 268:5445-5449(1993).
RN   [3]
RP   FUNCTION, AND RECOMBINANT EXPRESSION.
RX   PubMed=18694828; DOI=10.1016/j.ibmb.2008.06.007;
RA   Mans B.J., Ribeiro J.M.;
RT   "Function, mechanism and evolution of the moubatin-clade of soft tick
RT   lipocalins.";
RL   Insect Biochem. Mol. Biol. 38:841-852(2008).
CC   -!- FUNCTION: Tick salivary platelet aggregation inhibitor that plays an
CC       important part in the anti-hemostatic strategy of ticks. Acts by
CC       scavenging thromboxane A2 (TXA2), a potent inducer of platelet
CC       aggregation and blood vessel constriction (PubMed:8449906,
CC       PubMed:18694828). As a consequence, is a specific inhibitor of
CC       collagen-induced platelet aggregation (PubMed:8449907, PubMed:8449906).
CC       In addition, it also acts as a potent inhibitor of TXA2-mediated
CC       vasoconstriction (PubMed:18694828). Has also been found to bind
CC       leukotriene B4 (LTB4) (which also derives from arachidonic acid, as
CC       TXA2) with affinities in the nanomolar range (PubMed:18694828). It does
CC       not interact with complement protein C5 (PubMed:18694828).
CC       {ECO:0000269|PubMed:18694828, ECO:0000269|PubMed:8449906,
CC       ECO:0000269|PubMed:8449907}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18694828}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000305|PubMed:18694828}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000305|PubMed:8449906}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
CC   -!- CAUTION: There are 10 AA differences between the cDNA deduced sequence
CC       and the determined protein sequence. These differences are not
CC       indicated in the paper. {ECO:0000305|PubMed:8449907}.
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DR   EMBL; L04129; AAA29432.1; -; mRNA.
DR   PIR; A46618; A46618.
DR   AlphaFoldDB; Q04669; -.
DR   SMR; Q04669; -.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
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..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..171
FT                   /note="Moubatin"
FT                   /evidence="ECO:0000305|PubMed:8449907"
FT                   /id="PRO_0000021732"
FT   DISULFID        23..144
FT                   /evidence="ECO:0000250|UniProtKB:Q5YD59"
FT   DISULFID        55..166
FT                   /evidence="ECO:0000250|UniProtKB:Q5YD59"
FT   DISULFID        118..145
FT                   /evidence="ECO:0000250|UniProtKB:Q5YD59"
FT   CONFLICT        54
FT                   /note="D -> DE (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   171 AA;  18824 MW;  79EC7B7E460FA74B CRC64;
     MMLVLTTLIF SFSASIAYAQ SGCSVSDPLD ALKAFKDGAG TFLLQKSTDP QARDCLKGTP
     NGNRDGNTLP VTMTYKDDSK WVSLNWMFTL EGANIVATLE GKRKQRGELV YDVQSHDCHI
     TKLSSGVYQQ WQSNGSADDK DIKCCDEKFK ELTSGIDYTK PQEKGCETSA K