ID   VKTB3_DABSI             Reviewed;          84 AA.
AC   A8Y7P3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Kunitz-type serine protease inhibitor B3;
DE   AltName: Full=BPTI-3;
DE   AltName: Full=Trypsin inhibitor 3;
DE   AltName: Full=Trypsin inhibitor B3;
DE   Flags: Precursor;
OS   Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=343250;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Burma; TISSUE=Venom gland;
RA   Guo C., McClean S., Shaw C., Rao P., Ye M., Anthony John B.;
RT   "BPTI petides from Burmese Daboia russellii siamensis.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine protease inhibitor that inhibits plasmin and trypsin.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; AM411370; CAL69611.1; -; mRNA.
DR   AlphaFoldDB; A8Y7P3; -.
DR   SMR; A8Y7P3; -.
DR   MEROPS; I02.062; -.
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; Glycoprotein; Hemostasis impairing toxin;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..84
FT                   /note="Kunitz-type serine protease inhibitor B3"
FT                   /id="PRO_5000284436"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            41..42
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   84 AA;  9341 MW;  F0FF41D522EDF474 CRC64;
     MSSGGLLLLL GLLTLWAELT PISGHDRPTF CNLAPESGRC RGHLRRIYYN LESNKCEVFF
     YGGCGGNDNN FSTRDECRHT CVGK