Q9SHH7 (GSTUP_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase U25
Short name=AtGSTU25
EC=2.5.1.18

Alternative name(s):
GST class-tau member 25

Gene names

Name:	GSTU25
Ordered Locus Names:	At1g17180
ORF Names:	F20D23.12A

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	221 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides By similarity.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subcellular location	Cytoplasm › cytosol Probable.
Sequence similarities	Belongs to the GST superfamily. Tau family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Detoxification
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to toxic substance Inferred from electronic annotation. Source: UniProtKB-KW toxin catabolic process Traceable author statement Ref.5. Source: TAIR
Cellular_component	cytoplasm Non-traceable author statement Ref.5. Source: TAIR cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 221	221	Glutathione S-transferase U25		PRO_0000413570
Regions
	Domain	3 – 82	80	GST N-terminal
	Domain	88 – 208	121	GST C-terminal
	Region	13 – 14	2	Glutathione binding By similarity
	Region	39 – 40	2	Glutathione binding By similarity
	Region	53 – 54	2	Glutathione binding By similarity
	Region	66 – 67	2	Glutathione binding By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SHH7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: BCEB3254B39364A8	FASTA	221	25,591
	10 20 30 40 50 60 MADEVILLDF WPSMFGMRTR IALEEKNVKF DYREQDLWNK SPILLEMNPV HKKIPVLIHN 70 80 90 100 110 120 GNPVCESLIQ IEYIDEVWPS KTPLLPSDPY QRAQAKFWGD FIDKKVYASA RLIWGAKGEE 130 140 150 160 170 180 HEAGKKEFIE ILKTLESELG DKTYFGGETF GYVDIALIGF YSWFEAYEKF GSFSIEAECP 190 200 210 220 KLIAWGKRCV ERESVAKSLP DSEKIIKFVP ELRKKLGIEI E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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: GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC007651 Genomic DNA. Translation: AAD50015.1. CP002684 Genomic DNA. Translation: AEE29555.1. AK118907 mRNA. Translation: BAC43490.1. BT005643 mRNA. Translation: AAO64063.1.
IPI	IPI00519758.
PIR	H86307.
RefSeq	NP_173161.1. NM_101579.3.
UniGene	At.41849.
3D structure databases
ProteinModelPortal	Q9SHH7.
SMR	Q9SHH7. Positions 1-219.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SHH7. 2 interactions.
STRING	3702.AT1G17180.1-P.
Proteomic databases
PaxDb	Q9SHH7.
PRIDE	Q9SHH7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G17180.1; AT1G17180.1; AT1G17180.
GeneID	838289.
KEGG	ath:AT1G17180.
Organism-specific databases
TAIR	At1g17180.
Phylogenomic databases
eggNOG	COG0625.
HOGENOM	HOG000125749.
InParanoid	Q9SHH7.
KO	K00799.
OMA	ASARLIW.
PhylomeDB	Q9SHH7.
ProtClustDB	CLSN2681880.
Gene expression databases
Genevestigator	Q9SHH7.
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. IPR012336. Thioredoxin-like_fold. [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

GSTUP_ARATH

Accession

Primary (citable) accession number: Q9SHH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program