ID   KUNP1_ARGMO             Reviewed;          87 AA.
AC   Q09JW4;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Monogrin 1 {ECO:0000303|PubMed:18070663};
DE            Short=MG1 {ECO:0000303|PubMed:18070663};
DE   AltName: Full=Monogrin 1A {ECO:0000312|EMBL:ABI52649.1};
DE   AltName: Full=Platelet aggregation inhibitor {ECO:0000303|PubMed:18070663};
DE            Short=PAI {ECO:0000305};
GN   ORFNames=AM-30A {ECO:0000303|PubMed:18070663, ECO:0000303|PubMed:18070664};
OS   Argas monolakensis (Mono lake bird tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Argasidae; Argas.
OX   NCBI_TaxID=34602;
RN   [1] {ECO:0000312|EMBL:ABI52649.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Salivary gland;
RX   PubMed=18070663; DOI=10.1016/j.ibmb.2007.09.002;
RA   Mans B.J., Andersen J.F., Schwan T.G., Ribeiro J.M.;
RT   "Characterization of anti-hemostatic factors in the argasid, Argas
RT   monolakensis: implications for the evolution of blood-feeding in the soft
RT   tick family.";
RL   Insect Biochem. Mol. Biol. 38:22-41(2008).
RN   [2] {ECO:0000312|EMBL:ABI52649.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=18070664; DOI=10.1016/j.ibmb.2007.09.003;
RA   Mans B.J., Andersen J.F., Francischetti I.M., Valenzuela J.G., Schwan T.G.,
RA   Pham V.M., Garfield M.K., Hammer C.H., Ribeiro J.M.C.;
RT   "Comparative sialomics between hard and soft ticks: implications for the
RT   evolution of blood-feeding behavior.";
RL   Insect Biochem. Mol. Biol. 38:42-58(2008).
CC   -!- FUNCTION: Tick salivary platelet aggregation inhibitor that plays an
CC       important part in the anti-hemostatic strategy of ticks. Inhibits
CC       platelet aggregation induced by ADP (IC(50)~150 nM), collagen, and
CC       platelet activating factor (PAF) (PubMed:18070663). Acts by binding to
CC       platelet membrane glycoprotein IIb-IIIa (ITGA2B/ITGB3) in a metal ion
CC       dependent manner (PubMed:18070663). Does not inhibit aggregation
CC       induced by ristocecin, an agonist that aggregates platelets
CC       independently from the glycoprotein IIb-IIIa (ITGA2B/ITGB3). In
CC       contrast to other tick platelet aggregation inhibitors, this protein
CC       does not protect ITGA2B/ITGB3 from dissociation under SDS condition,
CC       suggesting it may dissocate much faster than its orthologs
CC       (PubMed:18070663). {ECO:0000269|PubMed:18070663}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250|UniProtKB:Q8MVZ2}. Secreted {ECO:0000305|PubMed:18070663}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000305|PubMed:18070663, ECO:0000305|PubMed:18070664}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:18070663}.
CC   -!- MASS SPECTROMETRY: Mass=9827.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18070663};
CC   -!- MISCELLANEOUS: The monogrins comprise about 4% of the total salivary
CC       gland protein. {ECO:0000269|PubMed:18070663}.
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DR   EMBL; DQ886732; ABI52649.1; -; mRNA.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   SUPFAM; SSF57362; SSF57362; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Toxin.
FT   CHAIN           1..87
FT                   /note="Monogrin 1"
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT                   /id="PRO_0000456092"
FT   DOMAIN          8..62
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   MOTIF           17..19
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT   DISULFID        8..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        16..42
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT   DISULFID        35..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   87 AA;  9709 MW;  50015BFB0C4C491F CRC64;
     AKGDTRRCGY LMMRGCRGDT TATRAWGFNY EEKKCQQETV ICGTGGAPRN AFETKQDCDA
     LCEGYSGPQY SMQEMLQHLK ENAKKTG