ID   KUNI_ARGMO              Reviewed;         144 AA.
AC   Q09JW6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Monobin {ECO:0000303|PubMed:18070663, ECO:0000303|PubMed:18070664};
DE   AltName: Full=Thrombin inhibitor {ECO:0000303|PubMed:18070663};
DE   Flags: Precursor;
GN   ORFNames=AM-28 {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:ABI52647.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, IDENTIFICATION BY
RP   MASS SPECTROMETRY, PROBABLE PYROGLUTAMATE FORMATION AT GLN-17,
RP   PURIFICATION, AND RECOMBINANT EXPRESSION.
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:ABI52647.1}
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 thrombin inhibitor that plays an important part
CC       in the anti-hemostatic strategy of ticks.
CC       {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=13663.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18070663};
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DR   EMBL; DQ886730; ABI52647.1; -; mRNA.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR   Gene3D; 4.10.410.10; -; 2.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade inhibiting toxin; Cytoplasmic vesicle;
KW   Disulfide bond; Hemostasis impairing toxin; Protease inhibitor;
KW   Pyrrolidone carboxylic acid; Repeat; Secreted; Serine protease inhibitor;
KW   Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..144
FT                   /note="Monobin"
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT                   /id="PRO_5004167789"
FT   DOMAIN          18..73
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000250|UniProtKB:P56409"
FT   DOMAIN          86..139
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   REGION          74..85
FT                   /note="Linker"
FT                   /evidence="ECO:0000250|UniProtKB:P56409, ECO:0000305"
FT   MOTIF           92..94
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         17
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT   DISULFID        22..70
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT   DISULFID        31..53
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT   DISULFID        47..66
FT                   /evidence="ECO:0000305|PubMed:18070663"
FT   DISULFID        86..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000305|PubMed:18070663"
FT   DISULFID        95..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000305|PubMed:18070663"
FT   DISULFID        112..135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000305|PubMed:18070663"
SQ   SEQUENCE   144 AA;  15352 MW;  79005B32C5BE2914 CRC64;
     MRLLALFAFA VAVVSAQRNQ MCQQPRTQGS CDASNQITKF FYTGSGCTSA PVCSDTDGGY
     GTEDECIQAC TVQGGHHNEG AGEEGCSGDP PRGDCGGQVE ERYYFDSTTR TCQTFEYRGC
     SSGNPDNSYE TEIECEIACP SASS