ID   VKT_BOMIG               Reviewed;          82 AA.
AC   G3LH89;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Kunitz-type serine protease inhibitor Bi-KTI;
DE   Flags: Precursor;
OS   Bombus ignitus (Bumblebee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Bombus; Bombus.
OX   NCBI_TaxID=130704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=22359676; DOI=10.1371/journal.pone.0032269;
RA   Choo Y.M., Lee K.S., Yoon H.J., Qiu Y., Wan H., Sohn M.R., Sohn H.D.,
RA   Jin B.R.;
RT   "Antifibrinolytic role of a bee venom serine protease inhibitor that acts
RT   as a plasmin inhibitor.";
RL   PLoS ONE 7:E32269-E32269(2012).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits plasmin (IC(50)=43.53
CC       nM, Ki=3.6 nM). Acts as an antifibrinolytic agent. May act in a
CC       cooperative manner with the serine protease Bi-VSP (AC B5U2W0) to
CC       promote the spread of bee venom under anti-bleeding conditions.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not inhibit factor Xa, thrombin, and tissue
CC       plasminogen activator (t-PA). {ECO:0000305|PubMed:22359676}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; JN381496; AEM68408.1; -; mRNA.
DR   AlphaFoldDB; G3LH89; -.
DR   SMR; G3LH89; -.
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   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..82
FT                   /note="Kunitz-type serine protease inhibitor Bi-KTI"
FT                   /id="PRO_0000429466"
FT   DOMAIN          30..80
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            40..41
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        39..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        55..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   82 AA;  8966 MW;  3019D1FB3F5DE8CF CRC64;
     MNHKFIALLL VVLCCALAVH QVSAEVPSHC TLSLATGTCK GYFPRFGYNI EMGKCVEFIY
     GGCDGNANNF RNLEECQQSC SV