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GSTUQ_ARATH
ID   GSTUQ_ARATH             Reviewed;         220 AA.
AC   Q9SHH8;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Glutathione S-transferase U26;
DE            Short=AtGSTU26;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 26;
GN   Name=GSTU26; OrderedLocusNames=At1g17190; ORFNames=F20D23.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX   PubMed=16538523; DOI=10.1007/s00299-006-0146-1;
RA   Nutricati E., Miceli A., Blando F., De Bellis L.;
RT   "Characterization of two Arabidopsis thaliana glutathione S-transferases.";
RL   Plant Cell Rep. 25:997-1005(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12090627; DOI=10.1023/a:1015557300450;
RA   Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT   "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT   family.";
RL   Plant Mol. Biol. 49:515-532(2002).
CC   -!- FUNCTION: In vitro, possesses glutathione S-transferase activity toward
CC       1-chloro-2,4-dinitrobenzene (CDNB). May be involved in the conjugation
CC       of reduced glutathione to a wide number of exogenous and endogenous
CC       hydrophobic electrophiles and have a detoxification role against
CC       certain herbicides. {ECO:0000269|PubMed:16538523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC   -!- INDUCTION: By alachlor, metolachlor and benoxacor.
CC       {ECO:0000269|PubMed:16538523}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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DR   EMBL; AJ306688; CAC36895.1; -; mRNA.
DR   EMBL; AC007651; AAD50014.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29556.1; -; Genomic_DNA.
DR   EMBL; BT004605; AAO42851.1; -; mRNA.
DR   EMBL; AK227997; BAE99962.1; -; mRNA.
DR   PIR; A86308; A86308.
DR   RefSeq; NP_173162.1; NM_101580.4.
DR   AlphaFoldDB; Q9SHH8; -.
DR   SMR; Q9SHH8; -.
DR   BioGRID; 23530; 4.
DR   IntAct; Q9SHH8; 4.
DR   STRING; 3702.AT1G17190.1; -.
DR   PaxDb; Q9SHH8; -.
DR   PRIDE; Q9SHH8; -.
DR   ProteomicsDB; 247202; -.
DR   EnsemblPlants; AT1G17190.1; AT1G17190.1; AT1G17190.
DR   GeneID; 838290; -.
DR   Gramene; AT1G17190.1; AT1G17190.1; AT1G17190.
DR   KEGG; ath:AT1G17190; -.
DR   Araport; AT1G17190; -.
DR   TAIR; locus:2020302; AT1G17190.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_2_1; -.
DR   InParanoid; Q9SHH8; -.
DR   OMA; KYEYKET; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q9SHH8; -.
DR   BRENDA; 2.5.1.18; 399.
DR   PRO; PR:Q9SHH8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SHH8; baseline and differential.
DR   Genevisible; Q9SHH8; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009635; P:response to herbicide; IEP:TAIR.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03185; GST_C_Tau; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260; PTHR11260; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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   Cytoplasm; Detoxification; Reference proteome; Stress response;
KW   Transferase.
FT   CHAIN           1..220
FT                   /note="Glutathione S-transferase U26"
FT                   /id="PRO_0000413571"
FT   DOMAIN          4..83
FT                   /note="GST N-terminal"
FT   DOMAIN          89..210
FT                   /note="GST C-terminal"
FT   BINDING         14..15
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  25779 MW;  CE898118920E502A CRC64;
     MANDQVILLD YWPSMFGMRT KMALAEKGVK YEYKETDPWV KTPLLIEMNP IHKKIPVLIH
     NGKPICESLI QLEYIDEVWS DASPILPSDP YQKSRARFWA EFIDKKFYDP SWKVWATMGE
     EHAAVKKELL EHFKTLETEL GDKPYYGGEV FGYLDIALMG YYSWFKAMEK FGEFSIETEF
     PILTTWTKRC LERESVVKAL ADSDRIIEYV YVLRKKFGAA
 
 
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