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Glutathione S-transferase U17 (AtGSTU17) (EC 2.5.1.18) (GST class-tau member 17) (Glutathione S-transferase 30) (Protein EARLY RESPONSIVE TO DEHYDRATION 9)

 GSTUH_ARATH             Reviewed;         227 AA.
Q9FUS8; Q94II0; Q9SY80;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
16-JAN-2019, entry version 110.
RecName: Full=Glutathione S-transferase U17;
Short=AtGSTU17;
EC=2.5.1.18;
AltName: Full=GST class-tau member 17;
AltName: Full=Glutathione S-transferase 30;
AltName: Full=Protein EARLY RESPONSIVE TO DEHYDRATION 9;
Name=GSTU17; Synonyms=ERD9, GST30, GST30B;
OrderedLocusNames=At1g10370; ORFNames=F14N23.26;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=8075396; DOI=10.1007/BF00028874;
Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K.;
"Cloning of cDNAs for genes that are early-responsive to dehydration
stress (ERDs) in Arabidopsis thaliana L.: identification of three ERDs
as HSP cognate genes.";
Plant Mol. Biol. 25:791-798(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=12090627; DOI=10.1023/A:1015557300450;
Wagner U., Edwards R., Dixon D.P., Mauch F.;
"Probing the diversity of the Arabidopsis glutathione S-transferase
gene family.";
Plant Mol. Biol. 49:515-532(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION.
PubMed=12232267; DOI=10.1104/pp.105.4.1089;
Sharma Y.K., Davis K.R.;
"Ozone-induced expression of stress-related genes in Arabidopsis
thaliana.";
Plant Physiol. 105:1089-1096(1994).
[7]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=20935176; DOI=10.1104/pp.110.159152;
Jiang H.W., Liu M.J., Chen I.C., Huang C.H., Chao L.Y., Hsieh H.L.;
"A glutathione S-transferase regulated by light and hormones
participates in the modulation of Arabidopsis seedling development.";
Plant Physiol. 154:1646-1658(2010).
-!- FUNCTION: Involved in light signaling, mainly phyA-mediated
photomorphogenesis and in the integration of various phytohormone
signals to modulate various aspects of plant development by
affecting glutathione pools. In vitro, possesses glutathione S-
transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and
benzyl isothiocyanate (BITC). {ECO:0000269|PubMed:20935176}.
-!- CATALYTIC ACTIVITY:
Reaction=glutathione + RX = a halide anion + an S-substituted
glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
ChEBI:CHEBI:90779; EC=2.5.1.18;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
-!- INDUCTION: By dehydration stress, auxin, abscisic acid (ABA),
jasmonate, ozone and transition from dark to far-red and red
light. {ECO:0000269|PubMed:12232267, ECO:0000269|PubMed:20935176,
ECO:0000269|PubMed:8075396}.
-!- DISRUPTION PHENOTYPE: Delayed flowering, long-hypocotyl phenotype
under low fluences of far-red light and insensitive to ABA-
mediated inhibition of root elongation.
{ECO:0000269|PubMed:20935176}.
-!- SIMILARITY: Belongs to the GST superfamily. Tau family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD32888.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB039930; BAB63917.1; -; mRNA.
EMBL; AF288191; AAG30140.1; -; mRNA.
EMBL; AC005489; AAD32888.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28571.1; -; Genomic_DNA.
EMBL; BT023743; AAZ23935.1; -; mRNA.
RefSeq; NP_172508.4; NM_100911.6.
UniGene; At.11290; -.
ProteinModelPortal; Q9FUS8; -.
SMR; Q9FUS8; -.
STRING; 3702.AT1G10370.1; -.
PaxDb; Q9FUS8; -.
PRIDE; Q9FUS8; -.
EnsemblPlants; AT1G10370.1; AT1G10370.1; AT1G10370.
GeneID; 837576; -.
Gramene; AT1G10370.1; AT1G10370.1; AT1G10370.
KEGG; ath:AT1G10370; -.
Araport; AT1G10370; -.
TAIR; locus:2012773; AT1G10370.
eggNOG; KOG0406; Eukaryota.
eggNOG; ENOG410XSIX; LUCA.
HOGENOM; HOG000125749; -.
InParanoid; Q9FUS8; -.
KO; K00799; -.
OMA; KHAASMK; -.
OrthoDB; 1225872at2759; -.
PhylomeDB; Q9FUS8; -.
BioCyc; ARA:AT1G10370-MONOMER; -.
BRENDA; 2.5.1.18; 399.
PRO; PR:Q9FUS8; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9FUS8; baseline and differential.
Genevisible; Q9FUS8; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
GO; GO:0009704; P:de-etiolation; IMP:TAIR.
GO; GO:0006749; P:glutathione metabolic process; IMP:TAIR.
GO; GO:0048527; P:lateral root development; IMP:TAIR.
GO; GO:0080148; P:negative regulation of response to water deprivation; IMP:TAIR.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0060416; P:response to growth hormone; IEP:TAIR.
GO; GO:0080167; P:response to karrikin; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR040079; Glutathione_S-Trfase.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Detoxification; Growth regulation;
Reference proteome; Stress response; Transferase.
CHAIN 1 227 Glutathione S-transferase U17.
/FTId=PRO_0000413563.
DOMAIN 4 83 GST N-terminal.
DOMAIN 90 222 GST C-terminal.
REGION 14 15 Glutathione binding. {ECO:0000250}.
REGION 40 41 Glutathione binding. {ECO:0000250}.
REGION 54 55 Glutathione binding. {ECO:0000250}.
REGION 67 68 Glutathione binding. {ECO:0000250}.
CONFLICT 151 151 F -> S (in Ref. 1; BAB63917).
{ECO:0000305}.
CONFLICT 161 161 D -> N (in Ref. 1; BAB63917).
{ECO:0000305}.
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


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