ID   IBBWT_MEDSA             Reviewed;          58 AA.
AC   P16346;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Bowman-Birk type wound-induced trypsin inhibitor;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=3888266; DOI=10.1021/bi00330a002;
RA   Brown W.E., Takio K., Titani K., Ryan C.A.;
RT   "Wound-induced trypsin inhibitor in alfalfa leaves: identity as a member of
RT   the Bowman-Birk inhibitor family.";
RL   Biochemistry 24:2105-2108(1985).
CC   -!- INDUCTION: By wounding.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   AlphaFoldDB; P16346; -.
DR   SMR; P16346; -.
DR   MEROPS; I12.001; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00023; BBI; 1.
DR   Gene3D; 2.10.69.10; -; 1.
DR   InterPro; IPR035995; Bowman-Birk_prot_inh.
DR   InterPro; IPR000877; Prot_inh_BBI.
DR   Pfam; PF00228; Bowman-Birk_leg; 2.
DR   SMART; SM00269; BowB; 1.
DR   SUPFAM; SSF57247; SSF57247; 1.
DR   PROSITE; PS00281; BOWMAN_BIRK; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..58
FT                   /note="Bowman-Birk type wound-induced trypsin inhibitor"
FT                   /id="PRO_0000105844"
FT   SITE            12..13
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            38..39
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..57
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        5..20
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        8..53
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        10..18
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        27..34
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        31..46
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        36..44
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   VARIANT         45
FT                   /note="H -> R"
FT   VARIANT         47
FT                   /note="A -> T"
SQ   SEQUENCE   58 AA;  6337 MW;  5C3C942E4717F1CC CRC64;
     TTACCNFCPC TRSIPPQCRC TDIGETCHSA CKTCLCTKSI PPQCHCADIT NFCYPKCN