ID   VKT_BOMTE               Reviewed;          82 AA.
AC   D8KY58;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Kunitz-type serine protease inhibitor Bt-KTI;
DE   Flags: Precursor;
OS   Bombus terrestris (Buff-tailed bumblebee) (Apis terrestris).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Bombus; Bombus.
OX   NCBI_TaxID=30195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX   PubMed=23164714; DOI=10.1016/j.toxicon.2012.11.004;
RA   Qiu Y., Lee K.S., Choo Y.M., Kong D., Yoon H.J., Jin B.R.;
RT   "Molecular cloning and antifibrinolytic activity of a serine protease
RT   inhibitor from bumblebee (Bombus terrestris) venom.";
RL   Toxicon 63:1-6(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kim S.R., Yoon H.J., Park K.-H., Yun E.-Y., Kim I., Jin B.-R., Hwang J.-S.;
RT   "Molecular cloning of cDNA for kazal-type proteinase inhibitior from the
RT   bumblebee Bombus terrestris.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine protease inhibitor that inhibits plasmin (Ki=2.01 nM)
CC       and trypsin. Acts as an antifibrinolytic agent.
CC       {ECO:0000269|PubMed:23164714}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not inhibit chymotrypsin, factor Xa, thrombin, and
CC       tissue plasminogen activator (t-PA). {ECO:0000305|PubMed:23164714}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; EU860215; ACJ54179.1; -; mRNA.
DR   EMBL; JX273645; AFR69309.1; -; Genomic_DNA.
DR   EMBL; JX273646; AFR69310.1; -; mRNA.
DR   RefSeq; XP_003396032.1; XM_003395984.2.
DR   AlphaFoldDB; D8KY58; -.
DR   SMR; D8KY58; -.
DR   EnsemblMetazoa; XM_003395984.3; XP_003396032.1; LOC100631053.
DR   GeneID; 100631053; -.
DR   KEGG; bter:100631053; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:CACAO.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:CACAO.
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 Bt-KTI"
FT                   /id="PRO_0000429467"
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;  9020 MW;  24C4DFCED040E8CF CRC64;
     MNHKFIALLL VVLCCALSVH QVSAEIPSHC TLPLATGTCR GYFPRFGYNV EMGKCVEFIY
     GGCDGNANNF RNLEECQQSC SV