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VKTB5_DABSI
ID   VKTB5_DABSI             Reviewed;          90 AA.
AC   A8Y7P5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Kunitz-type serine protease inhibitor B5;
DE   AltName: Full=BBPTI-5;
DE            Short=BPTI-5;
DE   AltName: Full=Trypsin inhibitor 5;
DE   AltName: Full=Trypsin inhibitor B5;
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=Myanmar; TISSUE=Venom gland;
RX   PubMed=23428970; DOI=10.1016/j.peptides.2013.02.009;
RA   Guo C.T., McClean S., Shaw C., Rao P.F., Ye M.Y., Bjourson A.J.;
RT   "Purification, characterization and molecular cloning of chymotrypsin
RT   inhibitor peptides from the venom of Burmese Daboia russelli siamensis.";
RL   Peptides 43:126-132(2013).
CC   -!- FUNCTION: Serine protease inhibitor. {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; AM411372; CAL69613.1; -; mRNA.
DR   AlphaFoldDB; A8Y7P5; -.
DR   SMR; A8Y7P5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor 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; Protease inhibitor; Secreted; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..84
FT                   /note="Kunitz-type serine protease inhibitor B5"
FT                   /id="PRO_5000284438"
FT   PROPEP          85..90
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000377469"
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 chymotrypsin"
FT                   /evidence="ECO:0000250"
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   90 AA;  9901 MW;  B49325386CB5554B CRC64;
     MSSGGLLLLL GLLTLWAELT PISGHDRPKF CYLPADPGEC LAHMRSFYYD SESKKCKEFI
     YGGCHGNANK FPSRDKCRQT CGASAKGRPT
 
 
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