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VKT2_DABSI
ID   VKT2_DABSI              Reviewed;          60 AA.
AC   P00990;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Kunitz-type serine protease inhibitor 2;
DE   AltName: Full=RVV-II;
DE   AltName: Full=Venom basic protease inhibitor 2;
DE   AltName: Full=Venom basic protease inhibitor II;
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   PROTEIN SEQUENCE, FUNCTION, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=4436285;
RA   Takahashi H., Iwanaga S., Kitagawa T., Hokama Y., Suzuki T.;
RT   "Snake venom proteinase inhibitors. II. Chemical structure of inhibitor II
RT   isolated from the venom of Russell's viper (Vipera russelli).";
RL   J. Biochem. 76:721-733(1974).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000269|PubMed:4436285}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   AlphaFoldDB; P00990; -.
DR   SMR; P00990; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           1..60
FT                   /note="Kunitz-type serine protease inhibitor 2"
FT                   /id="PRO_0000155446"
FT   DOMAIN          7..57
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            17..18
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|PubMed:4436285"
FT   DISULFID        16..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|PubMed:4436285"
FT   DISULFID        32..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|PubMed:4436285"
SQ   SEQUENCE   60 AA;  6850 MW;  5A7DCE9554CE6EA2 CRC64;
     HDRPTFCNLA PESGRCRGHL RRIYYNLESN KCKVFFYGGC GGNANNFETR DECRETCGGK
 
 
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