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 27-MAR-2024, entry version 150. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9SHH8; -. DR PaxDb; 3702-AT1G17190-1; -. 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; AT1G17190; GSTU26. DR eggNOG; KOG0406; Eukaryota. DR HOGENOM; CLU_011226_18_2_1; -. DR InParanoid; Q9SHH8; -. DR OMA; KYEYKET; -. DR OrthoDB; 767442at2759; -. 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 GO; GO:0005737; C:cytoplasm; NAS:TAIR. 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; IEA:InterPro. 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 CDD; cd03058; GST_N_Tau; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 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:SF810; GLUTATHIONE S-TRANSFERASE U26; 1. DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1. DR SFLD; SFLDG00358; Main_(cytGST); 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. DR Genevisible; Q9SHH8; AT. 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 //