ID   IBB2_PHAAN              Reviewed;          78 AA.
AC   P01061;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Bowman-Birk type proteinase inhibitors I-A, I-B, and I-A';
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=7309695; DOI=10.1093/oxfordjournals.jbchem.a133526;
RA   Kiyohara T., Yokota K., Masaki Y., Matsui O., Iwasaki T., Yoshikawa M.;
RT   "The amino acid sequences of proteinase inhibitors I-A and I-A' from adzuki
RT   beans.";
RL   J. Biochem. 90:721-728(1981).
CC   -!- FUNCTION: These inhibitors strongly inhibit trypsin.
CC   -!- MISCELLANEOUS: The I-A sequence is shown.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A01300; TIZB1A.
DR   PIR; B01300; TIZB1B.
DR   PIR; C01300; TIZB1P.
DR   AlphaFoldDB; P01061; -.
DR   SMR; P01061; -.
DR   MEROPS; I12.001; -.
DR   MEROPS; I12.008; -.
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..78
FT                   /note="Bowman-Birk type proteinase inhibitors I-A, I-B, and
FT                   I-A'"
FT                   /id="PRO_0000105847"
FT   SITE            26..27
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            53..54
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..72
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        19..34
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        22..68
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        24..32
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
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..6
FT                   /note="Missing (in the I-A' sequence)"
FT   VARIANT         40
FT                   /note="D -> N (in the I-A' sequence)"
FT   VARIANT         60
FT                   /note="R -> H (in the I-B sequence)"
SQ   SEQUENCE   78 AA;  8675 MW;  75D65A56EA832E5B CRC64;
     SVHHQDSSDE PSESSHPCCD LCLCTKSIPP QCQCADIRLD SCHSACKSCM CTRSMPGQCR
     CLDTHDFCHK PCKSRDKD