ID   IBB_VIGRR               Reviewed;          72 AA.
AC   P01062;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Bowman-Birk type trypsin inhibitor;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6125033;
RA   Zhang Y., Luo S., Tan F., Qi Z., Xu L., Zhang A.;
RT   "Complete amino acid sequence of mung bean trypsin inhibitor.";
RL   Sci. Sin., Ser. B Chem. Biol. Agric. Med. Earth Sci. 25:268-277(1982).
RN   [2] {ECO:0007744|PDB:3MYW}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=8444191; DOI=10.1111/j.1432-1033.1993.tb17692.x;
RA   Lin G., Bode W., Huber R., Chi C., Engh R.A.;
RT   "The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung
RT   bean in ternary complex with porcine trypsin.";
RL   Eur. J. Biochem. 212:549-555(1993).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 10-31, SEQUENCE REVISION, AND
RP   DISULFIDE BONDS.
RX   PubMed=7798176; DOI=10.1093/oxfordjournals.jbchem.a124491;
RA   Li Y., Huang Q., Zhang S., Liu S., Qi C., Tang Y.;
RT   "Studies on an artificial trypsin inhibitor peptide derived from the mung
RT   bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic
RT   analysis of its complex with trypsin.";
RL   J. Biochem. 116:18-25(1994).
CC   -!- MISCELLANEOUS: Functionally this inhibitor is unusual in that it
CC       stoichiometrically inhibits trypsin in a molar ratio of 1:2.
CC   -!- MISCELLANEOUS: The specificities and functions of this superfamily of
CC       inhibitors depend not only on the active sites within the domains, but
CC       also upon the amino acid composition, and resulting molecular
CC       conformation, surrounding these regions.
CC   -!- MISCELLANEOUS: Three isoinhibitors are also found whose amino ends
CC       differ slightly from that shown.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A01301; TIMB.
DR   PDB; 1G9I; X-ray; 2.20 A; I=10-31.
DR   PDB; 1SBW; X-ray; 1.80 A; I=8-69.
DR   PDB; 1SMF; X-ray; 2.10 A; I=10-31.
DR   PDB; 3MYW; X-ray; 2.50 A; I=1-72.
DR   PDBsum; 1G9I; -.
DR   PDBsum; 1SBW; -.
DR   PDBsum; 1SMF; -.
DR   PDBsum; 3MYW; -.
DR   AlphaFoldDB; P01062; -.
DR   SMR; P01062; -.
DR   STRING; 3916.P01062; -.
DR   MEROPS; I12.001; -.
DR   MEROPS; I12.008; -.
DR   EvolutionaryTrace; P01062; -.
DR   Proteomes; UP000087766; Genome assembly.
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; Cysteine Protease (Bromelain) Inhibitor, subunit H; 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; Bowman-Birk inhibitor, BBI; 1.
DR   PROSITE; PS00281; BOWMAN_BIRK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..72
FT                   /note="Bowman-Birk type trypsin inhibitor"
FT                   /id="PRO_0000105849"
FT   SITE            20..21
FT                   /note="Reactive bond for trypsin"
FT   SITE            47..48
FT                   /note="Reactive bond for trypsin"
FT   DISULFID        12..66
FT                   /evidence="ECO:0000269|PubMed:8444191"
FT   DISULFID        13..28
FT                   /evidence="ECO:0000269|PubMed:8444191"
FT   DISULFID        16..62
FT                   /evidence="ECO:0000269|PubMed:8444191"
FT   DISULFID        18..26
FT                   /evidence="ECO:0000269|PubMed:7798176"
FT   DISULFID        36..43
FT                   /evidence="ECO:0000269|PubMed:8444191"
FT   DISULFID        40..55
FT                   /evidence="ECO:0000269|PubMed:8444191"
FT   DISULFID        45..53
FT                   /evidence="ECO:0000269|PubMed:8444191"
FT   VARIANT         1..2
FT                   /note="Missing (in 2nd and 3rd isoinhibitor)"
FT   VARIANT         2
FT                   /note="H -> D (in 1st isoinhibitor)"
FT   VARIANT         3
FT                   /note="D -> K (in 3rd isoinhibitor)"
FT   STRAND          17..23
FT                   /evidence="ECO:0007829|PDB:1SBW"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:3MYW"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:3MYW"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:3MYW"
FT   STRAND          52..55
FT                   /evidence="ECO:0007829|PDB:3MYW"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:3MYW"
SQ   SEQUENCE   72 AA;  7959 MW;  8359DE1A8E61E4F8 CRC64;
     SHDEPSESSE PCCDSCDCTK SIPPECHCAN IRLNSCHSAC KSCICTRSMP GKCRCLDTDD
     FCYKPCESMD KD
//