ID   IBB_VICSN               Reviewed;          72 AA.
AC   P01065;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor;
DE   AltName: Full=VAI;
OS   Vicia sativa subsp. nigra (Common vetch) (Vicia angustifolia).
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; Fabeae; Vicia.
OX   NCBI_TaxID=3909;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Segetalis;
RA   Shimokawa Y., Kuromizu K., Araki T., Ohata J., Abe O.;
RT   "The complete amino acid sequence of Vicia angustifolia proteinase
RT   inhibitor.";
RL   Nat. Cult. 10:69-73(1983).
CC   -!- FUNCTION: This inhibitor has two domains, each with separate
CC       antiprotease activity. 1 mole of inhibitor inhibits either 1 mole of
CC       trypsin or 2 moles of chymotrypsin, stoichiometrically.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A01304; TIVTOA.
DR   AlphaFoldDB; P01065; -.
DR   SMR; P01065; -.
DR   MEROPS; I12.002; -.
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; 1.
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..72
FT                   /note="Bowman-Birk type proteinase inhibitor"
FT                   /id="PRO_0000105854"
FT   SITE            16..17
FT                   /note="Reactive bond for trypsin"
FT   SITE            42..43
FT                   /note="Reactive bond for chymotrypsin"
FT   DISULFID        8..61
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        9..24
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        12..57
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        14..22
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        31..38
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        35..50
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        40..48
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
SQ   SEQUENCE   72 AA;  8038 MW;  21AADB275DE33D83 CRC64;
     GDDVKSACCD TCLCTRSQPP TCRCVDVGER CHSACNHCVC NYSNPPQCQC FDTHKFCYKA
     CHSSEKEEVI KN