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P10648 (GSTA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutathione S-transferase A2
EC=2.5.1.18
Alternative name(s):
GST class-alpha member 2
Glutathione S-transferase GT41A
Gene names
Name:Gsta2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

Subunit structure

Homodimer. Ref.5

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
Chain2 – 222221Glutathione S-transferase A2
PRO_0000185789

Regions

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

Sites

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

Experimental info

Sequence conflict1991H → Q in AAA37749. Ref.1

Secondary structure

1 .................................. 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10648 [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: 837FFFC49C56F70F

FASTA22225,542
        10         20         30         40         50         60 
MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIGQLV LCPPDQREAK 

       130        140        150        160        170        180 
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDVHL LELLLYVEEL DASLLTPFPL 

       190        200        210        220 
LKAFKSRISS LPNVKKFLHP GSQRKPPLDA KQIEEARKVF KF

« Hide

References

« Hide 'large scale' references
[1]"Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole."
Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N.
J. Biol. Chem. 263:13324-13332(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Kidney.
[5]"Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide."
Gu Y., Xiao B., Wargo H.L., Bucher M.H., Singh S.V., Ji X.
Biochemistry 42:917-921(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND SUBSTRATE ANALOG, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03958 mRNA. Translation: AAA37749.1.
AC138587 Genomic DNA. No translation available.
CH466522 Genomic DNA. Translation: EDL26384.1.
CH466522 Genomic DNA. Translation: EDL26385.1.
CH466522 Genomic DNA. Translation: EDL26386.1.
CH466522 Genomic DNA. Translation: EDL26387.1.
BC061133 mRNA. Translation: AAH61133.1.
IPIIPI00116055.
IPI00480411.
RefSeqNP_032208.2. NM_008182.3.
UniGeneMm.422778.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML6X-ray1.90A/B2-221[»]
ProteinModelPortalP10648.
SMRP10648. Positions 3-222.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4080211.
STRING10090.ENSMUSP00000034902.

PTM databases

PhosphoSiteP10648.

Proteomic databases

PaxDbP10648.
PRIDEP10648.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034902; ENSMUSP00000034902; ENSMUSG00000057933.
GeneID14858.
KEGGmmu:14858.
UCSCuc009quf.1. mouse.

Organism-specific databases

CTD2939.
MGIMGI:95863. Gsta2.

Phylogenomic databases

eggNOGNOG266414.
GeneTreeENSGT00670000097856.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidP10648.
KOK00799.
OMAKSRYFPA.
OrthoDBEOG479F80.

Gene expression databases

CleanExMM_GSTA2.
GenevestigatorP10648.
GermOnlineENSMUSG00000057933. Mus musculus.

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

EvolutionaryTraceP10648.
NextBio287091.
SOURCESearch...

Entry information

Entry nameGSTA2_MOUSE
AccessionPrimary (citable) accession number: P10648
Secondary accession number(s): Q6P8Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: May 29, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents