ID   VKT3_BITGA              Reviewed;         151 AA.
AC   Q6T269;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Kunitz-type serine protease inhibitor bitisilin-3;
DE   AltName: Full=Two-Kunitz protease inhibitor;
DE   Flags: Fragment;
OS   Bitis gabonica (Gaboon adder) (Gaboon viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15276202; DOI=10.1016/j.gene.2004.03.024;
RA   Francischetti I.M.B., My-Pham V., Harrison J., Garfield M.K.,
RA   Ribeiro J.M.C.;
RT   "Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the
RT   full-length transcripts (cDNA) and proteins.";
RL   Gene 337:55-69(2004).
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; AY442289; AAR19275.1; -; mRNA.
DR   AlphaFoldDB; Q6T269; -.
DR   SMR; Q6T269; -.
DR   MEROPS; I02.062; -.
DR   MEROPS; I02.955; -.
DR   PRIDE; Q6T269; -.
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; 2.
DR   Gene3D; 4.10.410.10; -; 2.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 2.
DR   SUPFAM; SSF57362; SSF57362; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Repeat; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           <1..151
FT                   /note="Kunitz-type serine protease inhibitor bitisilin-3"
FT                   /id="PRO_0000376870"
FT   DOMAIN          18..68
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          72..122
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            28..29
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        18..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        27..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        43..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        72..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        81..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        97..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   NON_TER         1
SQ   SEQUENCE   151 AA;  16976 MW;  13E34ACE8DE581ED CRC64;
     PLRPGTEKHT FPFPAEFCNL PADLGPCKNY TGRFYYDSAS NKCEVFIYGG CPGNANNFKT
     REECRKTCVE ICILPAELGP CDEYTGRFYY DSASNKCEVF IYGGCQGNAN NFKTRDECRK
     TCVEICILPA ELGPCDEYTG RLLLRLGIKQ M