Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04904 (GSTA3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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-3

EC=2.5.1.18
Alternative name(s):
GST 2-2
GST A3-3
GST AA
Glutathione S-transferase Yc-1
Short name=GST Yc1
Gene names
Name:Gsta3
Synonyms:Gstyc1
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.

Developmental stage

Liver from adult female rats contains about 2-fold greater levels of YC1 than is found in liver from adult male rats.

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 Ref.5 Ref.8
Chain2 – 221220Glutathione S-transferase alpha-3
PRO_0000185794

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

Experimental info

Sequence conflict1021L → I Ref.2
Sequence conflict1841L → K Ref.2

Sequences

Sequence LengthMass (Da)Tools
P04904 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C45C5AF03573707F

FASTA22125,319
        10         20         30         40         50         60 
MPGKPVLHYF DGRGRMEPIR WLLAAAGVEF EEQFLKTRDD LARLRNDGSL MFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIATKYN LYGKDMKERA LIDMYAEGVA DLDEIVLHYP YIPPGEKEAS 

       130        140        150        160        170        180 
LAKIKDKARN RYFPAFEKVL KSHGQDYLVG NRLSRADVYL VQVLYHVEEL DPSALANFPL 

       190        200        210        220 
LKALRTRVSN LPTVKKFLQP GSQRKPLEDE KCVESAVKIF S 

« Hide

References

« Hide 'large scale' 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]"Rat liver glutathione S-transferases. Construction of a cDNA clone complementary to a Yc mRNA and prediction of the complete amino acid sequence of a Yc subunit."
Telakowski-Hopkins C.A., Rodkey K.A., Bennett C.D., Lu A.Y.H., Pickett C.B.
J. Biol. Chem. 260:5820-5825(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genomic cloning and characterization of the rat glutathione S-transferase-A3-subunit gene."
Fotouhi-Ardakani N., Batist G.
Biochem. J. 339:685-693(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer.
Tissue: Liver.
[4]"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: Liver and Pituitary.
[5]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 21-36; 70-78; 142-152; 156-182; 188-195 AND 197-204, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[6]"The Yc and Ya subunits of rat liver glutathione S-transferases are the products of separate genes."
Tu C.-P.D., Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C.
J. Biol. Chem. 259:9434-9439(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-221.
[7]"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.
[8]"Expression in Escherichia coli of rat liver cytosolic glutathione S-transferase Yc cDNA."
Huskey S.E., Wang R.W., Linemeyer D.L., Pickett C.B., Lu A.Y.H.
Arch. Biochem. Biophys. 279:116-121(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78848 mRNA. Translation: CAA55405.1.
S72505 mRNA. Translation: AAP21064.1.
K01932 mRNA. Translation: AAA41294.1.
AF111160 mRNA. Translation: AAD28714.1.
BC059128 mRNA. Translation: AAH59128.1.
BC088127 mRNA. Translation: AAH88127.1.
PIRA26753.
RefSeqNP_113697.1. NM_031509.2.
XP_006226824.1. XM_006226762.1.
UniGeneRn.10460.

3D structure databases

ProteinModelPortalP04904.
SMRP04904. Positions 4-220.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4565454.

Chemistry

BindingDBP04904.
ChEMBLCHEMBL4436.

PTM databases

PhosphoSiteP04904.

2D gel databases

World-2DPAGE0004:P04904.

Proteomic databases

PaxDbP04904.
PRIDEP04904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018325; ENSRNOP00000018325; ENSRNOG00000013484.
GeneID102550391.
24421.
KEGGrno:24421.

Organism-specific databases

CTD2938.
RGD2753. Gsta3.

Phylogenomic databases

eggNOGNOG266414.
GeneTreeENSGT00670000097856.
HOVERGENHBG053749.
InParanoidP04904.
KOK00799.
OMAYNESFIS.
OrthoDBEOG79CZ0K.
PhylomeDBP04904.
TreeFamTF105321.

Gene expression databases

ArrayExpressP04904.
GenevestigatorP04904.

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

NextBio603279.

Entry information

Entry nameGSTA3_RAT
AccessionPrimary (citable) accession number: P04904
Secondary accession number(s): Q6LD92
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 125 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