IBB_VICFA
ID IBB_VICFA Reviewed; 63 AA.
AC P24661;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Bowman-Birk type proteinase inhibitor;
DE AltName: Full=FBI;
OS Vicia faba (Broad bean) (Faba vulgaris).
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; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=1794984; DOI=10.1093/oxfordjournals.jbchem.a123695;
RA Asao T., Imai F., Tsuji I., Tashiro M., Iwami K., Ibuki F.;
RT "The amino acid sequence of a Bowman-Birk type proteinase inhibitor from
RT faba beans (Vicia faba L.).";
RL J. Biochem. 110:951-955(1991).
CC -!- FUNCTION: This inhibitor has two domains, each with separate
CC antiprotease activity. Inhibits bovine trypsin and chymotrypsin, in a
CC molar ratio of 1:1. The trypsin inhibition of FBI is independent of
CC chymotrypsin inhibition, but the chymotrypsin inhibition is not
CC completely independent of trypsin inhibition.
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR PIR; JX0198; TIVF.
DR AlphaFoldDB; P24661; -.
DR SMR; P24661; -.
DR MEROPS; I12.009; -.
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 Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Serine protease inhibitor.
FT CHAIN 1..63
FT /note="Bowman-Birk type proteinase inhibitor"
FT /id="PRO_0000105855"
FT SITE 16..17
FT /note="Reactive bond for trypsin"
FT SITE 42..43
FT /note="Reactive bond for chymotrypsin"
FT DISULFID 8..61
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 9..24
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 12..57
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 14..22
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 31..38
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 35..50
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 40..48
FT /evidence="ECO:0000250|UniProtKB:P80321"
SQ SEQUENCE 63 AA; 6989 MW; 9FDEB47973C14B34 CRC64;
GDDVKSACCD TCLCTKSEPP TCRCVDVGER CHSACNSCVC RYSNPPKCQC FDTHKFCYKS
CHN