IBB1_DIOGL
ID IBB1_DIOGL Reviewed; 67 AA.
AC P82469;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Bowman-Birk type proteinase inhibitor 1;
DE AltName: Full=Bowman-Birk type proteinase inhibitor I;
DE AltName: Full=DgTI;
OS Dioclea glabra.
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; Macropsychanthus.
OX NCBI_TaxID=124593;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=10441512; DOI=10.1006/bbrc.1999.1099;
RA Bueno N.R., Fritz H., Auerswald E.A., Mentele R., Sampaio M.U.,
RA Sampaio C.A.M., Oliva M.L.V.;
RT "Primary structure of Dioclea glabra trypsin inhibitor, DgTI, a Bowman-Birk
RT inhibitor.";
RL Biochem. Biophys. Res. Commun. 261:838-843(1999).
CC -!- FUNCTION: Inhibits trypsin but not chymotrypsin. The inhibitor consists
CC of 2 domains and has 2 sites of interaction with trypsin.
CC -!- SUBUNIT: Monomer. Although dimerization may occur in solution.
CC -!- TISSUE SPECIFICITY: Seed.
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P82469; -.
DR SMR; P82469; -.
DR MEROPS; I12.001; -.
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..67
FT /note="Bowman-Birk type proteinase inhibitor 1"
FT /id="PRO_0000105837"
FT SITE 13..14
FT /note="Reactive bond for trypsin"
FT SITE 40..41
FT /note="Reactive bond for trypsin"
FT DISULFID 5..59
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 6..21
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 9..55
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 11..19
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 29..36
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 33..48
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 38..46
FT /evidence="ECO:0000250|UniProtKB:P80321"
SQ SEQUENCE 67 AA; 7242 MW; ED7C4BCCBA9F57B1 CRC64;
SSGPCCDRCR CTKSEPPQCQ CQDVRLNSCH SACEACVCSH SMPGLCSCLD ITHFCHEPCK
SSGDDED