ID   IBB2_PHAVU              Reviewed;         107 AA.
AC   P01060; Q05G19;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 3.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor 2;
DE   AltName: Full=Bowman-Birk type proteinase inhibitor II;
DE   Contains:
DE     RecName: Full=Bowman-Birk type proteinase inhibitor 2 long;
DE   Contains:
DE     RecName: Full=Bowman-Birk type proteinase inhibitor 2 short;
DE   Flags: Precursor;
GN   Name=BBI;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Cotyledon, and Leaf;
RX   DOI=10.1007/s11032-009-9260-4;
RA   Galasso I., Piergiovanni A.R., Lioi L., Campion B., Bollini R.,
RA   Sparvoli F.;
RT   "Genome organisation of serine proteinase inhibitors in common bean
RT   (Phaseolus vulgaris L.).";
RL   Mol. Breed. 23:617-624(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RA   Galasso I., Piergiovanni A.R., Daminati G.M., Lioi L.;
RT   "Inhibitory properties and binding loop polymorphism in Bowman-Birk
RT   inhibitors from Phaseolus species.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 37-59 AND 65-107.
RX   PubMed=1126951; DOI=10.1016/s0021-9258(19)41412-9;
RA   Wilson K.A., Laskowski M. Sr.;
RT   "The partial amino acid sequence of trypsin inhibitor II from garden bean,
RT   Phaseolus vulgaris, with location of the trypsin and elastase-reactive
RT   sites.";
RL   J. Biol. Chem. 250:4261-4267(1975).
RN   [4]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=4684708; DOI=10.1016/s0021-9258(19)44332-9;
RA   Wilson K.A., Laskowski M. Sr.;
RT   "Isolation of three isoinhibitors of trypsin from garden bean, Phaseolus
RT   vulgaris, having either lysine or arginine at the reactive site.";
RL   J. Biol. Chem. 248:756-762(1973).
CC   -!- FUNCTION: This protein inhibits elastase and trypsin simultaneously and
CC       independently. {ECO:0000269|PubMed:4684708}.
CC   -!- PTM: The N-terminus of Bowman-Birk type proteinase inhibitor 2 long is
CC       blocked.
CC   -!- MISCELLANEOUS: Two forms of the inhibitor were isolated. The shorter
CC       form is probably derived by proteolytic degradation.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; AM406801; CAL51260.1; -; mRNA.
DR   EMBL; AM492522; CAM34247.1; -; Genomic_DNA.
DR   EMBL; FM173201; CAQ64594.1; -; Genomic_DNA.
DR   PIR; A01299; TIFB2.
DR   RefSeq; XP_007152477.1; XM_007152415.1.
DR   AlphaFoldDB; P01060; -.
DR   SMR; P01060; -.
DR   MEROPS; I12.008; -.
DR   EnsemblPlants; ESW24471; ESW24471; PHAVU_004G133900g.
DR   GeneID; 18632939; -.
DR   Gramene; ESW24471; ESW24471; PHAVU_004G133900g.
DR   KEGG; pvu:PHAVU_004G133900g; -.
DR   OMA; CKRRCTR; -.
DR   OrthoDB; 1551107at2759; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
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; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..107
FT                   /note="Bowman-Birk type proteinase inhibitor 2 long"
FT                   /id="PRO_0000375993"
FT   CHAIN           37..107
FT                   /note="Bowman-Birk type proteinase inhibitor 2 short"
FT                   /id="PRO_0000375994"
FT   SITE            53..54
FT                   /note="Reactive bond for elastase"
FT   SITE            80..81
FT                   /note="Reactive bond for trypsin"
FT   DISULFID        45..99
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        46..61
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        49..95
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        51..59
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        69..76
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        73..88
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        78..86
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   CONFLICT        58
FT                   /note="I -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   107 AA;  11637 MW;  3D7557A0A20BDC46 CRC64;
     MMVLKVCLLL VFLAGVTTAR MDLNHLIGSN HHDSSDEPSE SSEPCCDICV CTASIPPICQ
     CTDVRLNSCH SACKSCMCTR SMPGKCRCLD TTDYCYKSCK SSGEDDD