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P30713 (GSTT2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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-2

EC=2.5.1.18
Alternative name(s):
GST 12-12
GST class-theta-2
Glutathione S-transferase 12
Glutathione S-transferase Yrs-Yrs
Gene names
Name:Gstt2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the inactivation of reactive sulfate esters in carcinogenic arylmethanols. Highest activity towards ethacrynic acid and cumene hydroperoxide.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm. Nucleus Ref.6.

Tissue specificity

Highest values found in liver followed by testis, adrenal gland, kidney, lung, brain and skeletal muscle. 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.6

Sequence similarities

Belongs to the GST superfamily. Theta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Molecular functionTransferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from direct assay PubMed 12038961. Source: MGI

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from direct assay PubMed 12038961. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 244243Glutathione S-transferase theta-2
PRO_0000185943

Regions

Domain2 – 8281GST N-terminal
Domain88 – 230143GST C-terminal
Region53 – 542Glutathione binding By similarity
Region66 – 672Glutathione binding By similarity

Sites

Binding site401Glutathione By similarity

Experimental info

Sequence conflict141S → C AA sequence Ref.5
Sequence conflict36 – 372LK → RC AA sequence Ref.5
Sequence conflict421S → C AA sequence Ref.5
Sequence conflict441Missing AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P30713 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B8FCC8B15F003679

FASTA24427,439
        10         20         30         40         50         60 
MGLELYLDLL SQPSRAVYIF AKKNGIPFQL RTVDLLKGQH LSEQFSQVNC LKKVPVLKDG 

        70         80         90        100        110        120 
SFVLTESTAI LIYLSSKYQV ADHWYPADLQ ARAQVHEYLG WHADNIRGTF GVLLWTKVLG 

       130        140        150        160        170        180 
PLIGVQVPEE KVERNRNSMV LALQRLEDKF LRDRAFIAGQ QVTLADLMSL EELIQPVALG 

       190        200        210        220        230        240 
CNLFEGRPQL TAWRERVEAF LGAELCQEAH NPIMSVLGQA AKKTLPVPPP EAHASMMLRI 


ARIP 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and amino acid sequencing of rat liver class theta glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters of carcinogenic arylmethanols."
Ogura K., Nishiyama T., Okada T., Kajita J., Narihata H., Watabe T., Hiratsuka A., Watabe T.
Biochem. Biophys. Res. Commun. 181:1294-1300(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Isolation and characterization of the gene encoding rat class theta glutathione S-transferase subunit yrs."
Ogura K., Nishiyama T., Hiratsuka A., Watabe T., Watabe T.
Biochem. Biophys. Res. Commun. 205:1250-1256(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"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: Prostate.
[4]"A new class of rat glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters as metabolites of carcinogenic arylmethanols."
Hiratsuka A., Sebata N., Kawashima K., Okuda H., Ogura K., Watabe T., Satoh K., Hatayama I., Tsuchida S., Ishikawa T., Sato K.
J. Biol. Chem. 265:11973-11981(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26, CHARACTERIZATION.
Strain: Sprague-Dawley.
Tissue: Liver.
[5]"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: PROTEIN SEQUENCE OF 2-47; 140-162; 222-234 AND 238-244.
Tissue: Liver.
[6]"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, SUBCELLULAR LOCATION.
Tissue: Liver and Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10026 mRNA. Translation: BAA00916.1.
D38556 Genomic DNA. Translation: BAA07559.1.
BC061856 mRNA. Translation: AAH61856.1.
PIRJC2425.
S14346.
RefSeqNP_036928.1. NM_012796.2.
UniGeneRn.87212.

3D structure databases

ProteinModelPortalP30713.
SMRP30713. Positions 1-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4565859.

PTM databases

PhosphoSiteP30713.

Proteomic databases

PaxDbP30713.
PRIDEP30713.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000037656; ENSRNOP00000033158; ENSRNOG00000028188.
GeneID29487.
KEGGrno:29487.
UCSCRGD:69362. rat.

Organism-specific databases

CTD2953.
RGD69362. Gstt2.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00540000069741.
HOGENOMHOG000125747.
HOVERGENHBG051854.
InParanoidP30713.
KOK00799.
OMAGVPLWVQ.
OrthoDBEOG7V1FRJ.
PhylomeDBP30713.
TreeFamTF325759.

Gene expression databases

GenevestigatorP30713.

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.
PF13417. GST_N_3. 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

NextBio609358.
PROP30713.

Entry information

Entry nameGSTT2_RAT
AccessionPrimary (citable) accession number: P30713
Secondary accession number(s): P36971
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 112 of the entry and version 3 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