ID   VKT_VESBI               Reviewed;          77 AA.
AC   C0LNR2;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Kunitz-type serine protease inhibitor bicolin;
DE   Flags: Precursor;
OS   Vespa bicolor (Black shield wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=619325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=19258046; DOI=10.1016/j.cbpb.2009.02.010;
RA   Yang X., Wang Y., Lu Z., Zhai L., Jiang J., Liu J., Yu H.;
RT   "A novel serine protease inhibitor from the venom of Vespa bicolor
RT   Fabricius.";
RL   Comp. Biochem. Physiol. 153:116-120(2009).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits trypsin (Ki=550 nM)
CC       and thrombin (Ki=26000 nM). Exerts anticoagulant activity probably by
CC       the way of inhibiting thrombin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=5749.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19258046};
CC   -!- MISCELLANEOUS: Does not show inhibition on elastase and chymotrypsin.
CC       {ECO:0000305|PubMed:19258046}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; FJ749250; ACN58230.1; -; mRNA.
DR   AlphaFoldDB; C0LNR2; -.
DR   SMR; C0LNR2; -.
DR   MEROPS; I02.972; -.
DR   PRIDE; C0LNR2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Hemostasis impairing toxin; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal; Toxin.
FT   SIGNAL          1..24
FT   CHAIN           25..77
FT                   /note="Kunitz-type serine protease inhibitor bicolin"
FT                   /id="PRO_0000429465"
FT   DOMAIN          28..76
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            40..41
FT                   /note="Reactive bond homolog"
FT   DISULFID        28..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        37..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        51..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   77 AA;  8141 MW;  1534A6BE7C09837F CRC64;
     MNAKILALLI GVVFVGLFTV STPAHPLCLL DPPFGFCQSS ISRFAPVVGK CREYIYGGCS
     GKANNFQAQA KCQANCG