ID   IN21_MAIZE              Reviewed;         243 AA.
AC   P49248;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Protein IN2-1;
GN   Name=IN2-1; Synonyms=SAF1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Missouri 17;
RX   PubMed=1912492; DOI=10.1007/bf00037053;
RA   Hershey H.P., Stoner T.D.;
RT   "Isolation and characterization of cDNA clones for RNA species induced by
RT   substituted benzenesulfonamides in corn.";
RL   Plant Mol. Biol. 17:679-690(1991).
CC   -!- TISSUE SPECIFICITY: Leaves and roots. It is more strongly induced in
CC       the leaves relative to the roots.
CC   -!- DEVELOPMENTAL STAGE: It appears in the roots within 30 min of
CC       induction, maximum levels are reached by 6 hours, and remains constant
CC       for 2 days. In leaves it is seen 9 hours after induction, and reaches
CC       maximum levels after 24 hours.
CC   -!- INDUCTION: By N-(aminocarbonyl)-2-chlorobenzenesulfonamide (2-CBSU).
CC   -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC       {ECO:0000305}.
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DR   EMBL; X58573; CAA41447.1; -; mRNA.
DR   PIR; S17743; S17743.
DR   RefSeq; NP_001105433.1; NM_001111963.1.
DR   AlphaFoldDB; P49248; -.
DR   SMR; P49248; -.
DR   STRING; 4577.GRMZM2G084369_P01; -.
DR   PaxDb; P49248; -.
DR   PRIDE; P49248; -.
DR   GeneID; 542388; -.
DR   KEGG; zma:542388; -.
DR   MaizeGDB; 121983; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   OrthoDB; 1225872at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P49248; baseline and differential.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0010731; P:protein glutathionylation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..243
FT                   /note="Protein IN2-1"
FT                   /id="PRO_0000084192"
FT   DOMAIN          31..112
FT                   /note="GST N-terminal"
FT   DOMAIN          109..240
FT                   /note="GST C-terminal"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         70
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         96..97
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   243 AA;  26989 MW;  2A971ED2C0309E52 CRC64;
     MAAAAGPSSS VKESLPPALG STSQPPPVFD GTTRLYICYF CPFAQRAWVT RNLKGLQDKM
     ELVAIDLQDK PAWYKDKVYA QGTVPSLEHD SEVRGESLDL IRYIDSNFDG PALLPEDAAK
     RQFADELFAS ANAFTKALYS PLLSHAAVSD EVVAALDKLE ADLSKFDDGP FFLGQFSLAD
     VAYVTILERV QIYYSHLRNY DIAQGRPNLQ EFIDEMNKIE AYAQTKNDPL FLLDLAKSHL
     KIA