IBB_HORVU
ID IBB_HORVU Reviewed; 124 AA.
AC P12940;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Bowman-Birk type trypsin inhibitor;
GN Name=BBBI;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=cv. Distichum;
RA Nagasue A., Fukamachi H., Ikenaga H., Funatsu G.;
RT "The amino acid sequence of barley rootlet trypsin inhibitor.";
RL Agric. Biol. Chem. 52:1505-1514(1988).
RN [2] {ECO:0007744|PDB:1C2A}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-122, AND DISULFIDE BONDS.
RX PubMed=10547291; DOI=10.1006/jmbi.1999.3239;
RA Song H.K., Kim Y.S., Yang J.K., Moon J., Lee J.Y., Suh S.W.;
RT "Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor
RT from barley seeds at 1.9 A resolution.";
RL J. Mol. Biol. 293:1133-1144(1999).
RN [3] {ECO:0007744|PDB:1TX6}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH PORCINE PANCREATIC
RP TRYPSIN, AND DISULFIDE BONDS.
RX PubMed=15381428; DOI=10.1016/j.jmb.2004.08.027;
RA Park E.Y., Kim J.-A., Kim H.-W., Kim Y.S., Song H.K.;
RT "Crystal structure of the Bowman-Birk inhibitor from barley seeds in
RT ternary complex with porcine trypsin.";
RL J. Mol. Biol. 343:173-186(2004).
CC -!- FUNCTION: This inhibitor interacts with two molecules of trypsin.
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR PIR; JT0235; TIBHB.
DR PDB; 1C2A; X-ray; 1.90 A; A=4-122.
DR PDB; 1TX6; X-ray; 2.20 A; I/J=1-124.
DR PDB; 2FJ8; X-ray; 1.19 A; A=1-124.
DR PDBsum; 1C2A; -.
DR PDBsum; 1TX6; -.
DR PDBsum; 2FJ8; -.
DR AlphaFoldDB; P12940; -.
DR SMR; P12940; -.
DR MEROPS; I12.009; -.
DR MEROPS; I12.010; -.
DR MEROPS; I12.950; -.
DR EvolutionaryTrace; P12940; -.
DR ExpressionAtlas; P12940; baseline and differential.
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; 2.
DR Gene3D; 2.10.69.10; -; 2.
DR InterPro; IPR035995; Bowman-Birk_prot_inh.
DR InterPro; IPR000877; Prot_inh_BBI.
DR Pfam; PF00228; Bowman-Birk_leg; 3.
DR SMART; SM00269; BowB; 2.
DR SUPFAM; SSF57247; SSF57247; 2.
DR PROSITE; PS00281; BOWMAN_BIRK; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Repeat; Serine protease inhibitor.
FT CHAIN 1..124
FT /note="Bowman-Birk type trypsin inhibitor"
FT /id="PRO_0000105857"
FT REPEAT 1..62
FT REPEAT 63..124
FT SITE 17..18
FT /note="Reactive bond"
FT SITE 75..76
FT /note="Reactive bond"
FT DISULFID 9..62
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 10..25
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 15..23
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 32..39
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 36..50
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 67..121
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 68..83
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 73..81
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 90..97
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT DISULFID 94..109
FT /evidence="ECO:0000269|PubMed:10547291,
FT ECO:0000269|PubMed:15381428"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2FJ8"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2FJ8"
SQ SEQUENCE 124 AA; 13823 MW; 04CCA1CC80D2FEAD CRC64;
AGKKRPWKCC DEAVCTRSIP PICTCMDEVF ECPKTCKSCG PMGDPSRRIC QDQYVGDPGP
ICRPWECCDK AICTRSNPPT CRCVDEVKKC APTCKTCLPS RSRPSRRVCI DSYFGPVPPR
CTPR
