Q9FUS8 (GSTUH_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase U17
Short name=AtGSTU17
EC=2.5.1.18

Alternative name(s):
GST class-tau member 17
Glutathione S-transferase 30
Protein EARLY RESPONSIVE TO DEHYDRATION 9

Gene names

Name:	GSTU17
Synonyms:	ERD9, GST30, GST30B
Ordered Locus Names:	At1g10370
ORF Names:	F14N23.26

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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). Ref.7
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subcellular location	Cytoplasm › cytosol Probable.
Induction	By dehydration stress, auxin, abscisic acid (ABA), jasmonate, ozone and transition from dark to far-red and red light. Ref.1 Ref.6 Ref.7
Disruption phenotype	Delayed flowering, long-hypocotyl phenotype under low fluences of far-red light and insensitive to ABA-mediated inhibition of root elongation. Ref.7
Sequence similarities	Belongs to the GST superfamily. Tau family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.
Sequence caution	The sequence AAD32888.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Detoxification Growth regulation Stress response
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	de-etiolation Inferred from mutant phenotype Ref.7. Source: TAIR glutathione metabolic process Inferred from mutant phenotype Ref.7. Source: TAIR lateral root development Inferred from mutant phenotype Ref.7. Source: TAIR negative regulation of response to water deprivation Inferred from mutant phenotype PubMed 22095046. Source: TAIR regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW response to growth hormone stimulus Inferred from expression pattern Ref.7. Source: TAIR response to karrikin Inferred from expression pattern PubMed 20351290. Source: TAIR response to salt stress Inferred from mutant phenotype PubMed 22095046. Source: TAIR response to toxin Inferred from electronic annotation. Source: UniProtKB-KW toxin catabolic process Traceable author statement Ref.2. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay PubMed 18431481. Source: TAIR cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from direct assay Ref.7. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 227	227	Glutathione S-transferase U17		PRO_0000413563
Regions
	Domain	4 – 83	80	GST N-terminal
	Domain	90 – 222	133	GST C-terminal
	Region	14 – 15	2	Glutathione binding By similarity
	Region	40 – 41	2	Glutathione binding By similarity
	Region	54 – 55	2	Glutathione binding By similarity
	Region	67 – 68	2	Glutathione binding By similarity
Experimental info
	Sequence conflict	151	1	F → S in BAB63917. Ref.1
	Sequence conflict	161	1	D → N in BAB63917. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9FUS8 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 6A1743B849937442	FASTA	227	25,307
	10 20 30 40 50 60 MASSDVKLIG AWASPFVMRP RIALNLKSVP YEFLQETFGS KSELLLKSNP VHKKIPVLLH 70 80 90 100 110 120 ADKPVSESNI IVEYIDDTWS SSGPSILPSD PYDRAMARFW AAYIDEKWFV ALRGFLKAGG 130 140 150 160 170 180 EEEKKAVIAQ LEEGNAFLEK AFIDCSKGKP FFNGDNIGYL DIALGCFLAW LRVTELAVSY 190 200 210 220 KILDEAKTPS LSKWAENFCN DPAVKPVMPE TAKLAEFAKK IFPKPQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K. Plant Mol. Biol. 25:791-798(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: cv. Columbia.
[2]	"Probing the diversity of the Arabidopsis glutathione S-transferase gene family." Wagner U., Edwards R., Dixon D.P., Mauch F. Plant Mol. Biol. 49:515-532(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Ozone-induced expression of stress-related genes in Arabidopsis thaliana." Sharma Y.K., Davis K.R. Plant Physiol. 105:1089-1096(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[7]	"A glutathione S-transferase regulated by light and hormones participates in the modulation of Arabidopsis seedling development." Jiang H.W., Liu M.J., Chen I.C., Huang C.H., Chao L.Y., Hsieh H.L. Plant Physiol. 154:1646-1658(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB039930 mRNA. Translation: BAB63917.1. AF288191 mRNA. Translation: AAG30140.1. AC005489 Genomic DNA. Translation: AAD32888.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE28571.1. BT023743 mRNA. Translation: AAZ23935.1.
IPI	IPI00532578.
RefSeq	NP_172508.4. NM_100911.5.
UniGene	At.11290.
3D structure databases
HSSP	HSSP built from PDB template 1GWC based on UniProtKB O04941.
ProteinModelPortal	Q9FUS8.
SMR	Q9FUS8. Positions 5-219.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G10370.1-P.
Proteomic databases
PRIDE	Q9FUS8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G10370.1; AT1G10370.1; AT1G10370.
GeneID	837576.
KEGG	ath:AT1G10370.
Organism-specific databases
TAIR	At1g10370.
Phylogenomic databases
eggNOG	NOG288793.
HOGENOM	HOG000125749.
InParanoid	Q9FUS8.
KO	K00799.
OMA	QAMSQGL.
PhylomeDB	Q9FUS8.
ProtClustDB	CLSN2679578.
Gene expression databases
ArrayExpress	Q9FUS8.
Genevestigator	Q9FUS8.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF00043. GST_C. 1 hit. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSTUH_ARATH

Accession

Primary (citable) accession number: Q9FUS8
Secondary accession number(s): Q94II0, Q9SY80

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program