ID   IBB3_PHAVU              Reviewed;          85 AA.
AC   P81484;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   02-JUN-2021, entry version 62.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor PVI-3(2);
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Borlotto;
RX   PubMed=8493818; DOI=10.1007/bf01197933;
RA   Funk A., Weder J.K., Belitz H.-D.;
RT   "Primary structures of proteinase inhibitors from Phaseolus vulgaris var.
RT   nanus (cv. Borlotto).";
RL   Z. Lebensm. Unters. Forsch. 196:343-350(1993).
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..85
FT                   /note="Bowman-Birk type proteinase inhibitor PVI-3(2)"
FT                   /id="PRO_0000105852"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            29..30
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            56..57
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..75
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        22..37
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        25..71
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        27..35
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        45..52
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        49..64
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        54..62
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
SQ   SEQUENCE   85 AA;  9221 MW;  32DFB3DF2C86300C CRC64;
     SGHRHESXBS TBXASXSSKP CCBHCACTKS IPPQCRCSBL RLNSCHSECK GCICTFSIPA
     QCICTDTNNF CYEPCKSSHG PBBNN