IBBD2_SOYBN
ID IBBD2_SOYBN Reviewed; 83 AA.
AC P01064;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Bowman-Birk type proteinase inhibitor D-II;
DE AltName: Full=IV;
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].
RX AGRICOLA=IND92000914; DOI=10.1007/BF00014184;
RA Joudrier P.E., Foard D.E., Floener L.A., Larkins B.A.;
RT "Isolation and sequence of cDNA encoding the soybean protease inhibitors PI
RT IV and C-II.";
RL Plant Mol. Biol. 10:35-42(1987).
RN [2]
RP PROTEIN SEQUENCE OF 9-83.
RX PubMed=641033; DOI=10.1093/oxfordjournals.jbchem.a131967;
RA Odani S., Ikenaka T.;
RT "Studies on soybean trypsin inhibitors, XII. Linear sequences of two
RT soybean double-headed trypsin inhibitors, D-II and E-I.";
RL J. Biochem. 83:737-745(1978).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 18-81, AND DISULFIDE BONDS.
RX PubMed=1730730; DOI=10.2210/pdb1pi2/pdb;
RA Chen P., Rose J., Love R., Wei C.H., Wang B.C.;
RT "Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are
RT similar to other trypsin inhibitors.";
RL J. Biol. Chem. 267:1990-1994(1992).
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR EMBL; M20733; AAA33954.1; -; mRNA.
DR PIR; S07941; S07941.
DR RefSeq; NP_001235006.1; NM_001248077.1.
DR PDB; 1PI2; X-ray; 2.50 A; A=18-81.
DR PDBsum; 1PI2; -.
DR AlphaFoldDB; P01064; -.
DR SMR; P01064; -.
DR STRING; 3847.GLYMA16G33400.1; -.
DR MEROPS; I12.001; -.
DR MEROPS; I12.008; -.
DR PRIDE; P01064; -.
DR EvolutionaryTrace; P01064; -.
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.
FT PROPEP 1..8
FT /evidence="ECO:0000269|PubMed:641033"
FT /id="PRO_0000003284"
FT CHAIN 9..83
FT /note="Bowman-Birk type proteinase inhibitor D-II"
FT /id="PRO_0000003285"
FT SITE 32..33
FT /note="Reactive bond for trypsin"
FT SITE 59..60
FT /note="Reactive bond for trypsin"
FT DISULFID 24..78
FT /evidence="ECO:0000269|PubMed:1730730,
FT ECO:0007744|PDB:1PI2"
FT DISULFID 25..40
FT /evidence="ECO:0000269|PubMed:1730730,
FT ECO:0007744|PDB:1PI2"
FT DISULFID 28..74
FT /evidence="ECO:0000269|PubMed:1730730,
FT ECO:0007744|PDB:1PI2"
FT DISULFID 30..38
FT /evidence="ECO:0000269|PubMed:1730730,
FT ECO:0007744|PDB:1PI2"
FT DISULFID 48..55
FT /evidence="ECO:0000269|PubMed:1730730,
FT ECO:0007744|PDB:1PI2"
FT DISULFID 52..67
FT /evidence="ECO:0000269|PubMed:1730730,
FT ECO:0007744|PDB:1PI2"
FT DISULFID 57..65
FT /evidence="ECO:0000269|PubMed:1730730,
FT ECO:0007744|PDB:1PI2"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1PI2"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1PI2"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1PI2"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1PI2"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1PI2"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1PI2"
SQ SEQUENCE 83 AA; 9468 MW; 55A5F9524373C20B CRC64;
MCILSFLKSD QSSSYDDDEY SKPCCDLCMC TRSMPPQCSC EDIRLNSCHS DCKSCMCTRS
QPGQCRCLDT NDFCYKPCKS RDD