IBRO_ANACO
ID IBRO_ANACO Reviewed; 246 AA.
AC P01068; P27478; Q7Y0Z3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Bromelain inhibitor;
DE Short=BI;
DE Short=Bromein;
DE Contains:
DE RecName: Full=Bromelain inhibitor 1 chain B;
DE Short=BI-I B;
DE AltName: Full=Bromelain inhibitor VII light chain;
DE Short=BI-VII L;
DE Contains:
DE RecName: Full=Bromelain inhibitor 1 chain A;
DE Short=BI-I A;
DE AltName: Full=Bromelain inhibitor VII heavy chain;
DE Short=BI-VII H;
DE Contains:
DE RecName: Full=Bromelain inhibitor 3 chain B;
DE Short=BI-III B;
DE Contains:
DE RecName: Full=Bromelain inhibitor 3 chain A;
DE Short=BI-III A;
DE Contains:
DE RecName: Full=Bromelain inhibitor 2 chain B;
DE Short=BI-II B;
DE AltName: Full=Bromelain inhibitor VI light chain;
DE Short=BI-VI L;
DE Contains:
DE RecName: Full=Bromelain inhibitor 2 chain A;
DE Short=BI-II A;
DE AltName: Full=Bromelain inhibitor VI heavy chain;
DE Short=BI-VI H;
DE Flags: Precursor;
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12016215; DOI=10.1074/jbc.m202600200;
RA Sawano Y., Muramatsu T., Hatano K., Nagata K., Tanokura M.;
RT "Characterization of genomic sequence coding for bromelain inhibitors in
RT pineapple and expression of its recombinant isoform.";
RL J. Biol. Chem. 277:28222-28227(2002).
RN [2]
RP PROTEIN SEQUENCE OF 20-30; 36-76; 172-182 AND 188-228.
RX PubMed=1112827; DOI=10.1016/s0021-9258(19)41756-0;
RA Reddy M.N., Keim P.S., Heinrikson R.L., Kezdy F.J.;
RT "Primary structural analysis of sulfhydryl protease inhibitors from
RT pineapple stem.";
RL J. Biol. Chem. 250:1741-1750(1975).
RN [3]
RP PROTEIN SEQUENCE OF 172-182 AND 188-228.
RX PubMed=1515075; DOI=10.1515/bchm3.1992.373.2.459;
RA Lenarcic B., Ritonja A., Turk B., Dolenc I., Turk V.;
RT "Characterization and structure of pineapple stem inhibitor of cysteine
RT proteinases.";
RL Biol. Chem. Hoppe-Seyler 373:459-464(1992).
RN [4]
RP PROTEIN SEQUENCE OF 172-182 AND 188-228, AND STRUCTURE BY NMR.
RX PubMed=7556179; DOI=10.1111/j.1432-1033.1995.335zz.x;
RA Hatano K., Kojima M., Tanokura M., Takahashi K.;
RT "Primary structure, sequence-specific 1H-NMR assignments and secondary
RT structure in solution of bromelain inhibitor VI from pineapple stem.";
RL Eur. J. Biochem. 232:335-343(1995).
RN [5]
RP PROTEOLYTIC PROCESSING.
RX PubMed=15927893; DOI=10.1515/bc.2005.058;
RA Sawano Y., Hatano K., Tanokura M.;
RT "Susceptibility of the interchain peptide of a bromelain inhibitor
RT precursor to the target proteases bromelain, chymotrypsin, and trypsin.";
RL Biol. Chem. 386:491-498(2005).
RN [6]
RP STRUCTURE BY NMR OF 172-182 AND 188-228.
RX PubMed=8611527; DOI=10.1021/bi952754+;
RA Hatano K., Kojima M., Tanokura M., Takahashi K.;
RT "Solution structure of bromelain inhibitor IV from pineapple stem:
RT structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from
RT soybean.";
RL Biochemistry 35:5379-5384(1996).
CC -!- FUNCTION: Weak inhibitor of cysteine proteinases.
CC -!- SUBUNIT: Each inhibitor is composed of two chains, designated A and B
CC linked by three disulfide bonds.
CC -!- SIMILARITY: Belongs to the protease inhibitor I67 family.
CC {ECO:0000305}.
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DR EMBL; AF509782; AAP47112.1; -; Genomic_DNA.
DR PIR; A01307; XBPI.
DR PIR; S66609; S66609.
DR PDB; 1BI6; NMR; -; H=188-228, L=172-182.
DR PDB; 2BI6; NMR; -; H=188-228, L=172-182.
DR PDBsum; 1BI6; -.
DR PDBsum; 2BI6; -.
DR AlphaFoldDB; P01068; -.
DR SMR; P01068; -.
DR MEROPS; I67.001; -.
DR PRIDE; P01068; -.
DR EvolutionaryTrace; P01068; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00023; BBI; 2.
DR Gene3D; 2.10.69.10; -; 3.
DR InterPro; IPR035995; Bowman-Birk_prot_inh.
DR InterPro; IPR036212; Bromein_sf.
DR InterPro; IPR000877; Prot_inh_BBI.
DR InterPro; IPR022713; Prot_inhib_I67_bromein.
DR Pfam; PF11405; Inhibitor_I67; 3.
DR SMART; SM00269; BowB; 3.
DR SUPFAM; SSF57243; SSF57243; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1112827"
FT PEPTIDE 20..30
FT /note="Bromelain inhibitor 1 chain B"
FT /id="PRO_0000021480"
FT PROPEP 31..35
FT /evidence="ECO:0000269|PubMed:1112827"
FT /id="PRO_0000246127"
FT PEPTIDE 36..76
FT /note="Bromelain inhibitor 1 chain A"
FT /id="PRO_0000021481"
FT PROPEP 77..95
FT /id="PRO_0000246128"
FT PEPTIDE 96..106
FT /note="Bromelain inhibitor 3 chain B"
FT /id="PRO_0000246129"
FT PROPEP 107..111
FT /id="PRO_0000246130"
FT PEPTIDE 112..152
FT /note="Bromelain inhibitor 3 chain A"
FT /id="PRO_0000246131"
FT PROPEP 153..171
FT /id="PRO_0000246132"
FT PEPTIDE 172..182
FT /note="Bromelain inhibitor 2 chain B"
FT /id="PRO_0000021482"
FT PROPEP 183..187
FT /id="PRO_0000246133"
FT PEPTIDE 188..228
FT /note="Bromelain inhibitor 2 chain A"
FT /id="PRO_0000021483"
FT PROPEP 229..246
FT /id="PRO_0000246134"
FT DISULFID 22..42
FT /evidence="ECO:0000250"
FT DISULFID 25..74
FT /evidence="ECO:0000250"
FT DISULFID 27..40
FT /evidence="ECO:0000250"
FT DISULFID 49..56
FT /evidence="ECO:0000250"
FT DISULFID 53..65
FT /evidence="ECO:0000250"
FT DISULFID 98..118
FT /evidence="ECO:0000250"
FT DISULFID 101..150
FT /evidence="ECO:0000250"
FT DISULFID 103..116
FT /evidence="ECO:0000250"
FT DISULFID 125..132
FT /evidence="ECO:0000250"
FT DISULFID 129..141
FT /evidence="ECO:0000250"
FT DISULFID 174..194
FT DISULFID 177..226
FT DISULFID 179..192
FT DISULFID 201..208
FT DISULFID 205..217
FT VARIANT 188
FT /note="E -> Q"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1BI6"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1BI6"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1BI6"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1BI6"
SQ SEQUENCE 246 AA; 27521 MW; 5193808D36BE3C64 CRC64;
MNMLLLFLHE VINGERVTLT ACSECVCPLQ TSSSDDEYKC YCADTYSDCP GFCKKCKAEF
GKYICLDLIS PNDCVKPVSS SEAKQKMIKG ERVTLTACSE CVCPLRTSSS DEEYKCYCTD
TYSDCPGFCK KCKAEFGKYI CLDLISPNDC VKPVSSLEAK QNMIKEERVT LTACSECVCP
LRTSSSDEEY KCYCTDTYSD CPGFCKTCKA EFGKYICLDL ISPNDCVKPV SSWEARQKIK
LLQGRE
