IBB_VIGRR
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 03-AUG-2022, entry version 103.
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 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; -; 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.
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