IBB1_SOYBN
ID IBB1_SOYBN Reviewed; 110 AA.
AC P01055;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Bowman-Birk type proteinase inhibitor;
DE Short=BBI;
DE Flags: Precursor;
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed;
RX PubMed=8108518; DOI=10.1104/pp.102.2.687;
RA Baek J.M., Kim S.I.;
RT "Nucleotide sequence of a cDNA encoding soybean Bowman-Birk proteinase
RT inhibitor.";
RL Plant Physiol. 102:687-687(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-110.
RX PubMed=6086657; DOI=10.1016/s0021-9258(17)42782-7;
RA Hammond R.W., Foard D.E., Larkins B.A.;
RT "Molecular cloning and analysis of a gene coding for the Bowman-Birk
RT protease inhibitor in soybean.";
RL J. Biol. Chem. 259:9883-9890(1984).
RN [3]
RP ERRATUM OF PUBMED:6086657.
RA Hammond R.W., Foard D.E., Larkins B.A.;
RL J. Biol. Chem. 260:7806-7806(1985).
RN [4]
RP PROTEIN SEQUENCE OF 40-110.
RX PubMed=4672481; DOI=10.1093/oxfordjournals.jbchem.a129833;
RA Odani S., Ikenaka T.;
RT "Studies on soybean trypsin inhibitors. IV. Complete amino acid sequence
RT and the anti-proteinase sites of Bowman-Birk soybean proteinase
RT inhibitor.";
RL J. Biochem. 71:839-848(1972).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=4797072; DOI=10.1093/oxfordjournals.jbchem.a130295;
RA Odani S., Ikenaka T.;
RT "Studies on soybean trypsin inhibitors. 8. Disulfide bridges in soybean
RT Bowman-Birk proteinase inhibitor.";
RL J. Biochem. 74:697-715(1973).
RN [6]
RP DOMAINS.
RX PubMed=4797073; DOI=10.1093/oxfordjournals.jbchem.a130313;
RA Odani S., Ikenaka T.;
RT "Scission of soybean Bowman-Birk proteinase inhibitor into two small
RT fragments having either trypsin or chymotrypsin inhibitory activity.";
RL J. Biochem. 74:857-860(1973).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8954162; DOI=10.1111/j.1432-1033.1996.0122r.x;
RA Voss R.-H., Ermler U., Essen L.-O., Wenzl G., Kim Y.M., Flecker P.;
RT "Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at
RT 0.28-nm resolution. Structural peculiarities in a folded protein
RT conformation.";
RL Eur. J. Biochem. 242:122-131(1996).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=2012801; DOI=10.1021/bi00228a002;
RA Werner M.H., Wemmer D.E.;
RT "1H assignments and secondary structure determination of the soybean
RT trypsin/chymotrypsin Bowman-Birk inhibitor.";
RL Biochemistry 30:3356-3364(1991).
CC -!- FUNCTION: Inhibitor of trypsin and of chymotrypsin.
CC -!- DEVELOPMENTAL STAGE: This protein is apparently expressed only in
CC developing seeds.
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR EMBL; X68704; CAA48655.1; -; mRNA.
DR EMBL; K01968; AAA19613.1; -; mRNA.
DR PIR; JC2226; TISYO.
DR RefSeq; NP_001238547.1; NM_001251618.1.
DR PDB; 1BBI; NMR; -; A=40-110.
DR PDB; 1D6R; X-ray; 2.30 A; I=45-102.
DR PDB; 1K9B; X-ray; 2.80 A; A=45-102.
DR PDB; 2BBI; NMR; -; A=40-110.
DR PDB; 5J4Q; X-ray; 2.30 A; B=40-110.
DR PDB; 5J4S; X-ray; 2.10 A; B=40-110.
DR PDBsum; 1BBI; -.
DR PDBsum; 1D6R; -.
DR PDBsum; 1K9B; -.
DR PDBsum; 2BBI; -.
DR PDBsum; 5J4Q; -.
DR PDBsum; 5J4S; -.
DR AlphaFoldDB; P01055; -.
DR BMRB; P01055; -.
DR PCDDB; P01055; -.
DR SMR; P01055; -.
DR BioGRID; 989806; 1.
DR MINT; P01055; -.
DR STRING; 3847.GLYMA09G28700.1; -.
DR MEROPS; I12.001; -.
DR PRIDE; P01055; -.
DR GeneID; 548083; -.
DR KEGG; gmx:548083; -.
DR OrthoDB; 1551107at2759; -.
DR EvolutionaryTrace; P01055; -.
DR Proteomes; UP000008827; Unplaced.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Reference proteome; Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..39
FT /evidence="ECO:0000269|PubMed:4672481"
FT /id="PRO_0000003280"
FT CHAIN 40..110
FT /note="Bowman-Birk type proteinase inhibitor"
FT /id="PRO_0000003281"
FT SITE 55..56
FT /note="Reactive bond for trypsin"
FT SITE 82..83
FT /note="Reactive bond for chymotrypsin"
FT DISULFID 47..101
FT /evidence="ECO:0000269|PubMed:4797072"
FT DISULFID 48..63
FT /evidence="ECO:0000269|PubMed:4797072"
FT DISULFID 51..97
FT /evidence="ECO:0000269|PubMed:4797072"
FT DISULFID 53..61
FT /evidence="ECO:0000269|PubMed:4797072"
FT DISULFID 71..78
FT /evidence="ECO:0000269|PubMed:4797072"
FT DISULFID 75..90
FT /evidence="ECO:0000269|PubMed:4797072"
FT DISULFID 80..88
FT /evidence="ECO:0000269|PubMed:4797072"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:1D6R"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1D6R"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:5J4S"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:5J4S"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5J4S"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5J4S"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1BBI"
SQ SEQUENCE 110 AA; 12092 MW; DDE68317CA6AF54F CRC64;
MVVLKVCLVL LFLVGGTTSA NLRLSKLGLL MKSDHQHSND DESSKPCCDQ CACTKSNPPQ
CRCSDMRLNS CHSACKSCIC ALSYPAQCFC VDITDFCYEP CKPSEDDKEN
