GSTUC_ARATH
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 03-AUG-2022, entry version 123.
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.AT1G69920.1; -.
DR PaxDb; Q6NMS0; -.
DR PRIDE; Q6NMS0; -.
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; locus:2196744; AT1G69920.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_0_1; -.
DR InParanoid; Q6NMS0; -.
DR OMA; DDSICES; -.
DR OrthoDB; 1225872at2759; -.
DR BioCyc; ARA:AT1G69920-MON; -.
DR PRO; PR:Q6NMS0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NMS0; baseline and differential.
DR Genevisible; Q6NMS0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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; PTHR11260; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 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
