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P00502 (GSTA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 222221Glutathione S-transferase alpha-1
PRO_0000185792

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 residue21N-acetylserine By similarity

Experimental info

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

Secondary structure

1 ................................ 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.
IPIIPI00231638.
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[»]
ProteinModelPortalP00502.
SMRP00502. Positions 2-221.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000043510.

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.
OMANIRGRME.
OrthoDBEOG479F80.

Gene expression databases

ArrayExpressP00502.
GenevestigatorP00502.
GermOnlineENSRNOG00000000201. Rattus norvegicus.

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.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
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. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL2390.
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 3, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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