ID   IN21B_ORYSI             Reviewed;         244 AA.
AC   A1XBB7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein IN2-1 homolog B;
DE   AltName: Full=Glutathione S-transferase GSTZ5;
GN   Name=GSTZ5;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hu T., Cao K., Wang X.;
RT   "Genomic structure and over expression of two tandem-arranged GSTZ genes in
RT   rice.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=cv. CO43; TISSUE=Leaf;
RX   PubMed=20034395; DOI=10.1186/1477-5956-7-47;
RA   Kandasamy S., Loganathan K., Muthuraj R., Duraisamy S., Seetharaman S.,
RA   Thiruvengadam R., Ponnusamy B., Ramasamy S.;
RT   "Understanding the molecular basis of plant growth promotional effect of
RT   Pseudomonas fluorescens on rice through protein profiling.";
RL   Proteome Sci. 7:47-47(2009).
CC   -!- INDUCTION: Up-regulated in the leaf sheaths of rice plants grown from
CC       seeds that were inoculated with the nonpathogenic P.fluorescens strain
CC       KH-1. {ECO:0000269|PubMed:20034395}.
CC   -!- MASS SPECTROMETRY: Mass=27458; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20034395};
CC   -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ323738; ABC74869.1; -; mRNA.
DR   AlphaFoldDB; A1XBB7; -.
DR   SMR; A1XBB7; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR044629; GSTL1/2/3.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44328; PTHR44328; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
FT   CHAIN           1..244
FT                   /note="Protein IN2-1 homolog B"
FT                   /id="PRO_0000361766"
FT   DOMAIN          32..113
FT                   /note="GST N-terminal"
FT   DOMAIN          118..241
FT                   /note="GST C-terminal"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         97..98
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  27361 MW;  89A442C0B999A3E3 CRC64;
     MAAAAAAPAS SEKEVLPPSL TSSSEPPPLF DGTTRLYVAY HCPYAQRAWI ARNYKGLQDK
     IKIVAIDLAD RPAWYKEKVY PENKVPSLEH NNQVKGESLD LVKYIDTNFE GPALLPDDSE
     KQQFAEELLA YTDAFNKASY SSIVAKGDVC DEAVAALDKI EAALSKFNDG PFFLGQFSLV
     DIAYVPFIER FQIFFSGIKN YDITKGRPNL QKFIEEVNKI HAYTETKQDP QFLLEHTKKR
     LGIA