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P00502 (GSTA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 alpha-1

EC=2.5.1.18
Alternative name(s):
GST 1-1
GST 1a-1a
GST A1-1
GST B
Glutathione S-transferase Ya-1
Short name=GST Ya1
Ligandin
Gene names
Name:Gsta1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length222 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.

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.4

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm.

Miscellaneous

In addition to its enzymatic activity, the homodimer of Ya chains, called ligandin, binds various organic anions, xenobiotics, and azocarcinogen dyes.

Sequence similarities

Belongs to the GST superfamily. Alpha family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Glutathione S-transferase alpha-1
PRO_0000185792
Initiator methionine11Removed; alternate By similarity
Chain2 – 222221Glutathione S-transferase alpha-1, N-terminally processed
PRO_0000423205

Regions

Domain3 – 8381GST N-terminal
Domain85 – 208124GST C-terminal
Region67 – 682Glutathione binding

Sites

Binding site91Glutathione
Binding site451Glutathione
Binding site551Glutathione; via amide nitrogen and carbonyl oxygen

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict1521R → K Ref.1
Sequence conflict1521R → K Ref.3
Sequence conflict2081V → M in AAA41283. Ref.1

Secondary structure

................................ 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00502 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AE43A1BEBE8549CF

FASTA22225,607
        10         20         30         40         50         60 
MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL MFDQVPMVEI 

        70         80         90        100        110        120 
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIMQLV ICPPDQKEAK 

       130        140        150        160        170        180 
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LELLLYVEEF DASLLTSFPL 

       190        200        210        220 
LKAFKSRISS LPNVKKFLQP GSQRKLPVDA KQIEEARKIF KF 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone."
Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C., Tu C.-P.D.
J. Biol. Chem. 259:5536-5542(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
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: Kidney.
[3]"Rat glutathione S-transferase. Cloning of double-stranded cDNA and induction of its mRNA."
Kalinyak J.E., Taylor J.M.
J. Biol. Chem. 257:523-530(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-197.
[4]"Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y."
Adman E.T., Le Trong I., Stenkamp R.E., Nieslanik B.S., Dietze E.C., Tai G., Ibarra C., Atkins W.M.
Proteins 42:192-200(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01931 mRNA. Translation: AAA41283.1.
BC078706 mRNA. Translation: AAH78706.1.
PIRA24735.
XURTG. A92479.
RefSeqNP_058709.2. NM_017013.4.
UniGeneRn.144550.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EV4X-ray2.20A/C/D2-219[»]
1EV9X-ray2.20A/C/D2-221[»]
DisProtDP00731.
ProteinModelPortalP00502.
SMRP00502. Positions 2-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4564141.
STRING10116.ENSRNOP00000043510.

Chemistry

ChEMBLCHEMBL2390.

PTM databases

PhosphoSiteP00502.

Proteomic databases

PaxDbP00502.
PRIDEP00502.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24422.
KEGGrno:24422.

Organism-specific databases

CTD2939.
RGD2753. Gsta1.

Phylogenomic databases

eggNOGNOG266414.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidP00502.
KOK00799.
OrthoDBEOG79CZ0K.
PhylomeDBP00502.
TreeFamTF105321.

Gene expression databases

GenevestigatorP00502.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11571:SF4. PTHR11571:SF4. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00502.
NextBio603283.

Entry information

Entry nameGSTA1_RAT
AccessionPrimary (citable) accession number: P00502
Secondary accession number(s): Q6AZ72
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 129 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references