GSTUH_ARATH
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 03-AUG-2022, entry version 124.
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; OrderedLocusNames=At1g10370;
GN 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.AT1G10370.1; -.
DR PaxDb; Q9FUS8; -.
DR PRIDE; Q9FUS8; -.
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; locus:2012773; AT1G10370.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_0_1; -.
DR InParanoid; Q9FUS8; -.
DR OMA; KWAENFC; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9FUS8; -.
DR BioCyc; ARA:AT1G10370-MON; -.
DR BRENDA; 2.5.1.18; 399.
DR PRO; PR:Q9FUS8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FUS8; baseline and differential.
DR Genevisible; Q9FUS8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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: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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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 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; PTHR11260; 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; 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; 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
