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P46418 (GSTA5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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 alpha-5

EC=2.5.1.18
Alternative name(s):
GST A5-5
Glutathione S-transferase Yc-2
Short name=GST Yc2
Gene names
Name:Gsta5
Synonyms:Gstyc2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length221 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. Has substantial activity toward aflatoxin B1-8,9-epoxide.

Catalytic activity

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

Subunit structure

Heterodimer of YC1 and YC2.

Subcellular location

Cytoplasm.

Tissue specificity

Liver, nasal mucosa and epididymis.

Developmental stage

Liver from adult female rats contains about 10-fold greater levels of YC2 than is found in liver from adult male rats.

Induction

By ethoxyquin, oltipraz, butylated hydroxyanisole, and phenobarbitol.

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

Initiator methionine11Removed By similarity
Chain2 – 221220Glutathione S-transferase alpha-5
PRO_0000185796

Regions

Domain3 – 8381GST N-terminal
Domain85 – 207123GST C-terminal
Region54 – 552Glutathione binding By similarity
Region67 – 682Glutathione binding By similarity

Sites

Binding site91Glutathione By similarity
Binding site451Glutathione By similarity

Amino acid modifications

Modified residue41N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P46418 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EEDE9873765BFDB5

FASTA22125,347
        10         20         30         40         50         60 
MPGKPVLHYF DGRGRMEPIR WLLAAAGVEF EENFLKTRDD LARLRSDGSL MFEQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTKA ILNYIATKYN LYGKDMKERA LIDMYAEGVA DLELMVLYYP YMPPGEKEAS 

       130        140        150        160        170        180 
LAKIKDKARN RYFPAYEKVL KSHGQDYLVG NKLSRADVSL VELLYHVEEM DPGIVDNFPL 

       190        200        210        220 
LKALRTRVSN LPTVKKFLQP GSQRKPFDDE KCVESAKKIF S 

« Hide

References

[1]"Cloning of cDNAs from fetal rat liver encoding glutathione S-transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat liver resistant to the hepatocarcinogen aflatoxin B1."
Hayes J.D., Nguyen T., Judah D.J., Petersson D.G., Neal G.E.
J. Biol. Chem. 269:20707-20717(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer 344.
Tissue: Liver.
[2]"Characterization of the rat glutathione S-transferase Yc2 subunit gene, GSTA5: identification of a putative antioxidant-responsive element in the 5'-flanking region of rat GSTA5 that may mediate chemoprotection against aflatoxin B1."
Pulford D.J., Hayes J.D.
Biochem. J. 318:75-84(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Ethoxyquin-induced resistance to aflatoxin B1 in the rat is associated with the expression of a novel alpha-class glutathione S-transferase subunit, Yc2, which possesses high catalytic activity for aflatoxin B1-8,9-epoxide."
Hayes J.D., Judah D.J., McLellan L.I., Kerr L.A., Peacock S.D., Neal G.E.
Biochem. J. 279:385-398(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Strain: Fischer 344.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78847 mRNA. Translation: CAA55404.1.
S72506 mRNA. Translation: AAP21065.1.
S82820 mRNA. Translation: AAB46796.1.
PIRA54858.
RefSeqNP_001009920.1. NM_001009920.2.
NP_001153211.1. NM_001159739.2.
UniGeneRn.120929.

3D structure databases

ProteinModelPortalP46418.
SMRP46418. Positions 4-220.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP46418.
PRIDEP46418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000040950; ENSRNOP00000042770; ENSRNOG00000029711.
GeneID494500.
KEGGrno:494500.
UCSCRGD:2753. rat.

Organism-specific databases

CTD2940.
RGD2753. Gsta5.

Phylogenomic databases

eggNOGNOG266414.
GeneTreeENSGT00670000097856.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidP46418.
KOK00799.
OMALEIMILY.
OrthoDBEOG79CZ0K.
PhylomeDBP46418.
TreeFamTF105321.

Gene expression databases

GenevestigatorP46418.

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

NextBio697639.
PROP46418.

Entry information

Entry nameGSTA5_RAT
AccessionPrimary (citable) accession number: P46418
Secondary accession number(s): Q6LD91
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 107 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