GSTUE_ARATH
ID GSTUE_ARATH Reviewed; 243 AA.
AC Q9FUT1; Q9LFX4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glutathione S-transferase U14;
DE Short=AtGSTU14;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 14;
DE AltName: Full=Glutathione S-transferase 13;
GN Name=GSTU14; Synonyms=GST13; OrderedLocusNames=At1g27140; ORFNames=T7N9.20;
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], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [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;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79859.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g27130 has been split into 2 genes: At1g27130 and At1g27140.; Evidence={ECO:0000305};
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DR EMBL; AF288178; AAG30127.1; -; mRNA.
DR EMBL; AC000348; AAF79859.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30786.1; -; Genomic_DNA.
DR EMBL; BT024850; ABD60733.1; -; mRNA.
DR RefSeq; NP_174034.1; NM_102476.4.
DR AlphaFoldDB; Q9FUT1; -.
DR SMR; Q9FUT1; -.
DR STRING; 3702.AT1G27140.1; -.
DR PaxDb; Q9FUT1; -.
DR PRIDE; Q9FUT1; -.
DR ProteomicsDB; 247339; -.
DR EnsemblPlants; AT1G27140.1; AT1G27140.1; AT1G27140.
DR GeneID; 839603; -.
DR Gramene; AT1G27140.1; AT1G27140.1; AT1G27140.
DR KEGG; ath:AT1G27140; -.
DR Araport; AT1G27140; -.
DR TAIR; locus:2205799; AT1G27140.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_0_1; -.
DR InParanoid; Q9FUT1; -.
DR OrthoDB; 236145at2759; -.
DR PhylomeDB; Q9FUT1; -.
DR BioCyc; ARA:AT1G27140-MON; -.
DR PRO; PR:Q9FUT1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FUT1; baseline and differential.
DR Genevisible; Q9FUT1; 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; 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 Cytoplasm; Detoxification; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..243
FT /note="Glutathione S-transferase U14"
FT /id="PRO_0000413560"
FT DOMAIN 5..87
FT /note="GST N-terminal"
FT DOMAIN 93..220
FT /note="GST C-terminal"
FT BINDING 15..16
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 44..45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 58..59
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 MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZW27"
SQ SEQUENCE 243 AA; 27229 MW; 28D2DA7E3F5EB79A CRC64;
MAQNDTVKLI GCSDDPFSIR PRVALHLKSI KYEYLEEPDD DLGEKSQLLL KSNPIHKKTP
VLIHGDLAIC ESLNIVQYLD EAWPSDPSIL PSNAYDRASA RFWAQYIDDK CFEAANALTG
ANNDEERIAA TGKLTECLAI LEETFQKSSK GLGFFGGETI GYLDIACAAL LGPISVIEMF
SADKFVREET TPGLIQWAVR FRAHEAVRPY MPTVEEVTEL VKQRIEEGFK RNFKSNVSTS
EYE
