ID   IBB1_PHAAN              Reviewed;          82 AA.
AC   P01058;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor;
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
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; Vigna.
OX   NCBI_TaxID=3914;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=437138; DOI=10.1016/0014-5793(79)80257-4;
RA   Ishikawa C., Nakamura S., Watanabe K., Takahashi K.;
RT   "The amino acid sequence of adzuki bean proteinase inhibitor I.";
RL   FEBS Lett. 99:97-100(1979).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   AGRICOLA=IND79038424;
RA   Yoshikawa M., Kiyohara T., Iwasaki T., Ishii Y., Kimura N.;
RT   "Amino acid sequences of proteinase inhibitors II and II' from adzuki
RT   beans.";
RL   Agric. Biol. Chem. 43:787-796(1979).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=3032921; DOI=10.1093/oxfordjournals.jbchem.a121872;
RA   Tsunogae Y., Tanaka I., Yamane T., Kikkawa J., Ashida T., Ishikawa C.,
RA   Watanabe K., Nakamura S., Takahashi K.;
RT   "Structure of the trypsin-binding domain of Bowman-Birk type protease
RT   inhibitor and its interaction with trypsin.";
RL   J. Biochem. 100:1637-1646(1986).
CC   -!- FUNCTION: Trypsin and chymotrypsin are inhibited simultaneously. There
CC       are two separate reactive sites for trypsin and chymotrypsin but they
CC       do not inhibit simultaneously.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A90019; TIZB2.
DR   PIR; A91453; TIZB1.
DR   PDB; 1TAB; X-ray; 2.30 A; I=1-82.
DR   PDBsum; 1TAB; -.
DR   AlphaFoldDB; P01058; -.
DR   SMR; P01058; -.
DR   MEROPS; I12.001; -.
DR   EvolutionaryTrace; P01058; -.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..82
FT                   /note="Bowman-Birk type proteinase inhibitor"
FT                   /id="PRO_0000105846"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            26..27
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            53..54
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..72
FT                   /evidence="ECO:0000269|PubMed:3032921"
FT   DISULFID        19..34
FT                   /evidence="ECO:0000269|PubMed:3032921"
FT   DISULFID        22..68
FT                   /evidence="ECO:0000269|PubMed:3032921"
FT   DISULFID        24..32
FT                   /evidence="ECO:0000269|PubMed:3032921"
FT   DISULFID        42..49
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        46..61
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        51..59
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   VARIANT         1..9
FT                   /note="Missing (in a shorter form)"
FT   CONFLICT        5..6
FT                   /note="DE -> ED (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:1TAB"
FT   STRAND          22..29
FT                   /evidence="ECO:0007829|PDB:1TAB"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:1TAB"
SQ   SEQUENCE   82 AA;  9130 MW;  C5518784F31CBF33 CRC64;
     SGHHDETTDE PSESSKPCCD QCSCTKSMPP KCRCSDIRLN SCHSACKSCA CTYSIPAKCF
     CTDINDFCYE PCKSSRDDDW DN