ID   GSTUH_ARATH             Reviewed;         227 AA.
AC   Q9FUS8; Q94II0; Q9SY80;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=Glutathione S-transferase U17;
DE            Short=AtGSTU17;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 17;
DE   AltName: Full=Glutathione S-transferase 30;
DE   AltName: Full=Protein EARLY RESPONSIVE TO DEHYDRATION 9;
GN   Name=GSTU17; Synonyms=ERD9, GST30, GST30B;
GN   OrderedLocusNames=At1g10370; ORFNames=F14N23.26;
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], AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=8075396; DOI=10.1007/bf00028874;
RA   Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K.;
RT   "Cloning of cDNAs for genes that are early-responsive to dehydration stress
RT   (ERDs) in Arabidopsis thaliana L.: identification of three ERDs as HSP
RT   cognate genes.";
RL   Plant Mol. Biol. 25:791-798(1994).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INDUCTION.
RX   PubMed=12232267; DOI=10.1104/pp.105.4.1089;
RA   Sharma Y.K., Davis K.R.;
RT   "Ozone-induced expression of stress-related genes in Arabidopsis
RT   thaliana.";
RL   Plant Physiol. 105:1089-1096(1994).
RN   [7]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20935176; DOI=10.1104/pp.110.159152;
RA   Jiang H.W., Liu M.J., Chen I.C., Huang C.H., Chao L.Y., Hsieh H.L.;
RT   "A glutathione S-transferase regulated by light and hormones participates
RT   in the modulation of Arabidopsis seedling development.";
RL   Plant Physiol. 154:1646-1658(2010).
CC   -!- FUNCTION: Involved in light signaling, mainly phyA-mediated
CC       photomorphogenesis and in the integration of various phytohormone
CC       signals to modulate various aspects of plant development by affecting
CC       glutathione pools. In vitro, possesses glutathione S-transferase
CC       activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl
CC       isothiocyanate (BITC). {ECO:0000269|PubMed:20935176}.
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 dehydration stress, auxin, abscisic acid (ABA),
CC       jasmonate, ozone and transition from dark to far-red and red light.
CC       {ECO:0000269|PubMed:12232267, ECO:0000269|PubMed:20935176,
CC       ECO:0000269|PubMed:8075396}.
CC   -!- DISRUPTION PHENOTYPE: Delayed flowering, long-hypocotyl phenotype under
CC       low fluences of far-red light and insensitive to ABA-mediated
CC       inhibition of root elongation. {ECO:0000269|PubMed:20935176}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD32888.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB039930; BAB63917.1; -; mRNA.
DR   EMBL; AF288191; AAG30140.1; -; mRNA.
DR   EMBL; AC005489; AAD32888.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28571.1; -; Genomic_DNA.
DR   EMBL; BT023743; AAZ23935.1; -; mRNA.
DR   RefSeq; NP_172508.4; NM_100911.6.
DR   AlphaFoldDB; Q9FUS8; -.
DR   SMR; Q9FUS8; -.
DR   STRING; 3702.Q9FUS8; -.
DR   PaxDb; 3702-AT1G10370-1; -.
DR   ProteomicsDB; 247198; -.
DR   EnsemblPlants; AT1G10370.1; AT1G10370.1; AT1G10370.
DR   GeneID; 837576; -.
DR   Gramene; AT1G10370.1; AT1G10370.1; AT1G10370.
DR   KEGG; ath:AT1G10370; -.
DR   Araport; AT1G10370; -.
DR   TAIR; AT1G10370; ERD9.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_0_1; -.
DR   InParanoid; Q9FUS8; -.
DR   OMA; KWAENFC; -.
DR   OrthoDB; 767442at2759; -.
DR   PhylomeDB; Q9FUS8; -.
DR   BioCyc; ARA:AT1G10370-MONOMER; -.
DR   BRENDA; 2.5.1.18; 399.
DR   PRO; PR:Q9FUS8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FUS8; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0009704; P:de-etiolation; IMP:TAIR.
DR   GO; GO:0006749; P:glutathione metabolic process; IMP:TAIR.
DR   GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR   GO; GO:0080148; P:negative regulation of response to water deprivation; IMP:TAIR.
DR   GO; GO:0060416; P:response to growth hormone; IEP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP: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; IPR004046; GST_C.
DR   InterPro; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF615; GLUTATHIONE S-TRANSFERASE U17; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF00043; GST_C; 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; Q9FUS8; AT.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Detoxification; Growth regulation; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..227
FT                   /note="Glutathione S-transferase U17"
FT                   /id="PRO_0000413563"
FT   DOMAIN          4..83
FT                   /note="GST N-terminal"
FT   DOMAIN          90..222
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"
FT   CONFLICT        151
FT                   /note="F -> S (in Ref. 1; BAB63917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="D -> N (in Ref. 1; BAB63917)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   227 AA;  25307 MW;  6A1743B849937442 CRC64;
     MASSDVKLIG AWASPFVMRP RIALNLKSVP YEFLQETFGS KSELLLKSNP VHKKIPVLLH
     ADKPVSESNI IVEYIDDTWS SSGPSILPSD PYDRAMARFW AAYIDEKWFV ALRGFLKAGG
     EEEKKAVIAQ LEEGNAFLEK AFIDCSKGKP FFNGDNIGYL DIALGCFLAW LRVTELAVSY
     KILDEAKTPS LSKWAENFCN DPAVKPVMPE TAKLAEFAKK IFPKPQA
//