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Protein

Glutathione S-transferase U18

Gene

GSTU18

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

RX + glutathione = HX + R-S-glutathione.

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. response to toxic substance Source: UniProtKB-KW
  2. toxin catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

BioCyciARA:AT1G10360-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase U18 (EC:2.5.1.18)
Short name:
AtGSTU18
Alternative name(s):
GST class-tau member 18
Glutathione S-transferase 29
Gene namesi
Name:GSTU18
Synonyms:GST29
Ordered Locus Names:At1g10360
ORF Names:F14N23.24
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G10360.

Subcellular locationi

Cytoplasmcytosol Curated

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Glutathione S-transferase U18PRO_0000413564Add
BLAST

Proteomic databases

PaxDbiQ9FUS9.
PRIDEiQ9FUS9.

Expressioni

Gene expression databases

GenevestigatoriQ9FUS9.

Interactioni

Protein-protein interaction databases

BioGridi22815. 1 interaction.
IntActiQ9FUS9. 1 interaction.
STRINGi3702.AT1G10360.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9FUS9.
SMRiQ9FUS9. Positions 4-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8380GST N-terminalAdd
BLAST
Domaini90 – 221132GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 152Glutathione bindingBy similarity
Regioni40 – 412Glutathione bindingBy similarity
Regioni54 – 552Glutathione bindingBy similarity
Regioni67 – 682Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Tau family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125749.
InParanoidiQ9FUS9.
KOiK00799.
OMAiHIGYLDI.
PhylomeDBiQ9FUS9.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FUS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEDVKLIG SWASVYVMRA RIALHLKSIS YEFLQETYGS KSELLLKSNP
60 70 80 90 100
VHKKMPVLIH ADKPVCESNI IVHYIDEAWN SSGPSILPSH PYDRAIARFW
110 120 130 140 150
AAYIDDQWFI SVRSILTAQG DEEKKAAIAQ VEERTKLLEK AFNDCSQGKP
160 170 180 190 200
FFNGDHIGYL DIALGSFLGW WRVVELDANH KFLDETKTPS LVKWAERFCD
210 220
DPAVKPIMPE ITKLAEFARK LFPKRQA
Length:227
Mass (Da):25,911
Last modified:February 28, 2001 - v1
Checksum:i2996DA12B9BF590B
GO

Sequence cautioni

The sequence AAD32886.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288190 mRNA. Translation: AAG30139.1.
AC005489 Genomic DNA. Translation: AAD32886.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28570.1.
BT000940 mRNA. Translation: AAN41340.1.
AK317183 mRNA. Translation: BAH19868.1.
RefSeqiNP_172507.1. NM_100910.4.
UniGeneiAt.11288.

Genome annotation databases

EnsemblPlantsiAT1G10360.1; AT1G10360.1; AT1G10360.
GeneIDi837575.
KEGGiath:AT1G10360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288190 mRNA. Translation: AAG30139.1.
AC005489 Genomic DNA. Translation: AAD32886.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28570.1.
BT000940 mRNA. Translation: AAN41340.1.
AK317183 mRNA. Translation: BAH19868.1.
RefSeqiNP_172507.1. NM_100910.4.
UniGeneiAt.11288.

3D structure databases

ProteinModelPortaliQ9FUS9.
SMRiQ9FUS9. Positions 4-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22815. 1 interaction.
IntActiQ9FUS9. 1 interaction.
STRINGi3702.AT1G10360.1-P.

Proteomic databases

PaxDbiQ9FUS9.
PRIDEiQ9FUS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G10360.1; AT1G10360.1; AT1G10360.
GeneIDi837575.
KEGGiath:AT1G10360.

Organism-specific databases

TAIRiAT1G10360.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125749.
InParanoidiQ9FUS9.
KOiK00799.
OMAiHIGYLDI.
PhylomeDBiQ9FUS9.

Enzyme and pathway databases

BioCyciARA:AT1G10360-MONOMER.

Gene expression databases

GenevestigatoriQ9FUS9.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  2. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
    Tissue: Rosette leaf.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiGSTUI_ARATH
AccessioniPrimary (citable) accession number: Q9FUS9
Secondary accession number(s): Q9SY78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2011
Last sequence update: February 28, 2001
Last modified: January 6, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.