ID   GSTUC_ARATH             Reviewed;         254 AA.
AC   Q6NMS0; F4I3V4; Q9CAS5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Glutathione S-transferase U12;
DE            Short=AtGSTU12;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 12;
GN   Name=GSTU12; OrderedLocusNames=At1g69920; ORFNames=T17F3.5;
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 [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   [2]
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   [3]
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   [4]
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).
RN   [5]
RP   INDUCTION.
RX   PubMed=16698904; DOI=10.1104/pp.106.076869;
RA   Bae H., Kim M.S., Sicher R.C., Bae H.J., Bailey B.A.;
RT   "Necrosis- and ethylene-inducing peptide from Fusarium oxysporum induces a
RT   complex cascade of transcripts associated with signal transduction and cell
RT   death in Arabidopsis.";
RL   Plant Physiol. 141:1056-1067(2006).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19174456; DOI=10.1093/jxb/ern365;
RA   Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT   "Enzyme activities and subcellular localization of members of the
RT   Arabidopsis glutathione transferase superfamily.";
RL   J. Exp. Bot. 60:1207-1218(2009).
CC   -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC       a wide number of exogenous and endogenous hydrophobic electrophiles and
CC       have a detoxification role against certain herbicides. {ECO:0000250}.
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: Nucleus {ECO:0000269|PubMed:19174456}.
CC   -!- INDUCTION: By fungal elicitor. {ECO:0000269|PubMed:16698904}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52553.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC010675; AAG52553.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE34998.1; -; Genomic_DNA.
DR   EMBL; BT010687; AAR20744.1; -; mRNA.
DR   EMBL; BT011586; AAS46639.1; -; mRNA.
DR   PIR; F96721; F96721.
DR   RefSeq; NP_177150.2; NM_105660.6.
DR   AlphaFoldDB; Q6NMS0; -.
DR   SMR; Q6NMS0; -.
DR   STRING; 3702.Q6NMS0; -.
DR   PaxDb; 3702-AT1G69920-1; -.
DR   ProteomicsDB; 247338; -.
DR   EnsemblPlants; AT1G69920.1; AT1G69920.1; AT1G69920.
DR   GeneID; 843328; -.
DR   Gramene; AT1G69920.1; AT1G69920.1; AT1G69920.
DR   KEGG; ath:AT1G69920; -.
DR   Araport; AT1G69920; -.
DR   TAIR; AT1G69920; GSTU12.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_0_1; -.
DR   InParanoid; Q6NMS0; -.
DR   OMA; DDSICES; -.
DR   OrthoDB; 679898at2759; -.
DR   BioCyc; ARA:AT1G69920-MONOMER; -.
DR   PRO; PR:Q6NMS0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q6NMS0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA: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; IPR040079; Glutathione_S-Trfase.
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:SF564; GLUTATHIONE S-TRANSFERASE U12; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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; Q6NMS0; AT.
PE   2: Evidence at transcript level;
KW   Detoxification; Nucleus; Reference proteome; Stress response; Transferase.
FT   CHAIN           1..254
FT                   /note="Glutathione S-transferase U12"
FT                   /id="PRO_0000413558"
FT   DOMAIN          33..114
FT                   /note="GST N-terminal"
FT   DOMAIN          120..252
FT                   /note="GST C-terminal"
FT   MOTIF           19..23
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         43..44
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..86
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         98..99
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        244
FT                   /note="F -> S (in Ref. 3; AAR20744/AAS46639)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   254 AA;  27923 MW;  2A152B61669ABA85 CRC64;
     MLKNKKSDNS LSRDTLQIKK RKKTTMAQNG SNTTVKLIGT WASPFAIRAQ VALHLKSVEH
     EYVEETDVLK GKSDLLIKSN PIHKKVPVLI HGDVSICESL NIVQYVDESW PSDLSILPTL
     PSERAFARFW AHFVDGKLFE SIDAVAGAKD DAARMTLAGN LMENLAALEE AFQKSSKGGD
     FFGGGNIGFV DITVGAIVGP ISVIEAFSGV KFLRPDTTPG LIQWAEKFRA HEAVKPYMPT
     VAEFIEFAKK KFSV
//