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Q01579 (GSTT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase theta-1

EC=2.5.1.18
Alternative name(s):
GST 5-5
GST class-theta-1
Glutathione S-transferase 5
Gene names
Name:Gstt1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Also binds steroids, bilirubin, carcinogens and numerous organic anions. Has dichloromethane dehalogenase activity. Ref.5

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.5

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

In liver, highest expression found in central vein limiting plate hepatocytes. In lung, expressed mainly in Clara cells of the bronchiolar epithelium and, at low levels, in type II alveolar cells. Ref.4

Sequence similarities

Belongs to the GST superfamily. Theta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 240239Glutathione S-transferase theta-1
PRO_0000185942

Regions

Domain2 – 8281GST N-terminal
Domain88 – 223136GST C-terminal
Region53 – 542Glutathione binding By similarity
Region66 – 672Glutathione binding By similarity

Sites

Binding site401Glutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01579 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 09583ACF9C85DF8F

FASTA24027,468
        10         20         30         40         50         60 
MVLELYLDLL SQPCRAIYIF AKKNNIPFQM HTVELRKGEH LSDAFAQVNP MKKVPAMKDG 

        70         80         90        100        110        120 
GFTLCESVAI LLYLAHKYKV PDHWYPQDLQ ARARVDEYLA WQHTTLRRSC LRTLWHKVMF 

       130        140        150        160        170        180 
PVFLGEQIRP EMLAATLADL DVNVQVLEDQ FLQDKDFLVG PHISLADVVA ITELMHPVGG 

       190        200        210        220        230        240 
GCPVFEGRPR LAAWYRRVEA AVGKDLFLEA HEVILKVRDC PPADPVIKQK LMPRVLTMIQ 

« Hide

References

« Hide 'large scale' references
[1]"An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences."
Pemble S.E., Taylor J.B.
Biochem. J. 287:957-963(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[3]"Theta, a new class of glutathione transferases purified from rat and man."
Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B.
Biochem. J. 274:409-414(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-47; 58-95; 120-131 AND 176-193.
Tissue: Liver.
[4]"The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human."
Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T.
Biochem. J. 318:297-303(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
Tissue: Liver and Lung.
[5]"Residue 234 is a master switch of the alternative-substrate activity profile of human and rodent theta class glutathione transferase T1-1."
Shokeer A., Mannervik B.
Biochim. Biophys. Acta 1800:466-473(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67654 mRNA. Translation: CAA47896.1.
BC086426 mRNA. Translation: AAH86426.1.
PIRS27161.
RefSeqNP_445745.1. NM_053293.2.
UniGeneRn.11122.

3D structure databases

ProteinModelPortalQ01579.
SMRQ01579. Positions 3-240.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ01579.
ChEMBLCHEMBL2423.

Proteomic databases

PaxDbQ01579.
PRIDEQ01579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001669; ENSRNOP00000001669; ENSRNOG00000049771.
GeneID25260.
KEGGrno:25260.
UCSCRGD:2765. rat.

Organism-specific databases

CTD2952.
RGD2765. Gstt1.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00540000069741.
HOGENOMHOG000125747.
HOVERGENHBG051854.
KOK00799.
OMATVKQKLM.
OrthoDBEOG7GTT59.
PhylomeDBQ01579.

Enzyme and pathway databases

SABIO-RKQ01579.

Gene expression databases

GenevestigatorQ01579.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605907.
PROQ01579.

Entry information

Entry nameGSTT1_RAT
AccessionPrimary (citable) accession number: Q01579
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families