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Database: UniProt/SWISS-PROT
Entry: GSTUP_ARATH
LinkDB: GSTUP_ARATH
Original site: GSTUP_ARATH 
ID   GSTUP_ARATH             Reviewed;         221 AA.
AC   Q9SHH7;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 128.
DE   RecName: Full=Glutathione S-transferase U25;
DE            Short=AtGSTU25;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 25;
GN   Name=GSTU25; OrderedLocusNames=At1g17180; ORFNames=F20D23.12A;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
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
RT   gene family.";
RL   Plant Mol. Biol. 49:515-532(2002).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: May be involved in the conjugation of reduced
CC       glutathione to a wide number of exogenous and endogenous
CC       hydrophobic electrophiles and have a detoxification role against
CC       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.
CC       {ECO:0000305}.
DR   EMBL; AC007651; AAD50015.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29555.1; -; Genomic_DNA.
DR   EMBL; AK118907; BAC43490.1; -; mRNA.
DR   EMBL; BT005643; AAO64063.1; -; mRNA.
DR   PIR; H86307; H86307.
DR   RefSeq; NP_173161.1; NM_101579.4.
DR   UniGene; At.41849; -.
DR   PDB; 5G5A; X-ray; 1.95 A; A/B/C/D=1-221.
DR   PDBsum; 5G5A; -.
DR   ProteinModelPortal; Q9SHH7; -.
DR   SMR; Q9SHH7; -.
DR   BioGrid; 23529; 2.
DR   IntAct; Q9SHH7; 2.
DR   STRING; 3702.AT1G17180.1; -.
DR   iPTMnet; Q9SHH7; -.
DR   PaxDb; Q9SHH7; -.
DR   PRIDE; Q9SHH7; -.
DR   EnsemblPlants; AT1G17180.1; AT1G17180.1; AT1G17180.
DR   GeneID; 838289; -.
DR   Gramene; AT1G17180.1; AT1G17180.1; AT1G17180.
DR   KEGG; ath:AT1G17180; -.
DR   Araport; AT1G17180; -.
DR   TAIR; locus:2020312; AT1G17180.
DR   eggNOG; KOG0406; Eukaryota.
DR   eggNOG; ENOG410XSIX; LUCA.
DR   HOGENOM; HOG000125749; -.
DR   InParanoid; Q9SHH7; -.
DR   KO; K00799; -.
DR   OMA; SWFEAYE; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q9SHH7; -.
DR   BioCyc; ARA:AT1G17180-MONOMER; -.
DR   PRO; PR:Q9SHH7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SHH7; baseline and differential.
DR   Genevisible; Q9SHH7; 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:0046256; P:2,4,6-trinitrotoluene catabolic process; IDA:TAIR.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
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; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF02798; GST_N; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Detoxification; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895}.
FT   CHAIN         2    221       Glutathione S-transferase U25.
FT                                /FTId=PRO_0000413570.
FT   DOMAIN        3     82       GST N-terminal.
FT   DOMAIN       88    208       GST C-terminal.
FT   REGION       13     14       Glutathione binding. {ECO:0000250}.
FT   REGION       39     40       Glutathione binding. {ECO:0000250}.
FT   REGION       53     54       Glutathione binding. {ECO:0000250}.
FT   REGION       66     67       Glutathione binding. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   MOD_RES     149    149       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9ZW27}.
FT   STRAND        5      9       {ECO:0000244|PDB:5G5A}.
FT   HELIX        14     25       {ECO:0000244|PDB:5G5A}.
FT   STRAND       31     34       {ECO:0000244|PDB:5G5A}.
FT   HELIX        42     47       {ECO:0000244|PDB:5G5A}.
FT   TURN         49     51       {ECO:0000244|PDB:5G5A}.
FT   STRAND       56     59       {ECO:0000244|PDB:5G5A}.
FT   STRAND       62     66       {ECO:0000244|PDB:5G5A}.
FT   HELIX        67     77       {ECO:0000244|PDB:5G5A}.
FT   HELIX        89    115       {ECO:0000244|PDB:5G5A}.
FT   HELIX       118    139       {ECO:0000244|PDB:5G5A}.
FT   HELIX       152    161       {ECO:0000244|PDB:5G5A}.
FT   HELIX       164    171       {ECO:0000244|PDB:5G5A}.
FT   HELIX       175    178       {ECO:0000244|PDB:5G5A}.
FT   HELIX       180    190       {ECO:0000244|PDB:5G5A}.
FT   HELIX       193    198       {ECO:0000244|PDB:5G5A}.
FT   HELIX       202    215       {ECO:0000244|PDB:5G5A}.
SQ   SEQUENCE   221 AA;  25591 MW;  BCEB3254B39364A8 CRC64;
     MADEVILLDF WPSMFGMRTR IALEEKNVKF DYREQDLWNK SPILLEMNPV HKKIPVLIHN
     GNPVCESLIQ IEYIDEVWPS KTPLLPSDPY QRAQAKFWGD FIDKKVYASA RLIWGAKGEE
     HEAGKKEFIE ILKTLESELG DKTYFGGETF GYVDIALIGF YSWFEAYEKF GSFSIEAECP
     KLIAWGKRCV ERESVAKSLP DSEKIIKFVP ELRKKLGIEI E
//
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