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P13745 (GSTA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 A1

EC=2.5.1.18
Alternative name(s):
GST class-alpha member 1
Glutathione S-transferase Ya
Glutathione S-transferase Ya1
Gene names
Name:Gsta1
Synonyms:Gsta, Gstya
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length223 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.4

Induction

Induced in the liver by beta-naphthoflavone (BNF) and 23-t-butyl-4-hydroxyanisole (BHA). Ref.3

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 – 223223Glutathione S-transferase A1
PRO_0000185788
Initiator methionine11Removed; alternate By similarity
Chain2 – 223222Glutathione S-transferase A1, N-terminally processed
PRO_0000423204

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

Secondary structure

.................................. 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13745 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A348A07133FBEC1D

FASTA22325,608
        10         20         30         40         50         60 
MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI 

        70         80         90        100        110        120 
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYSEGIL DLTEMIGQLV LCPPDQREAK 

       130        140        150        160        170        180 
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LEVLLYVEEF DASLLTPFPL 

       190        200        210        220 
LKAFKSRISS LPNVKKFLQP GSQRKPPMDA KQIQEARKAF KIQ 

« Hide

References

« Hide 'large scale' references
[1]"Mouse glutathione S-transferase Ya subunit: gene structure and sequence."
Daniel V., Sharon R., Tichauer Y., Sarid S.
DNA 6:317-324(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: Brain.
[3]"Regulation of mouse glutathione S-transferases by chemoprotectors. Molecular evidence for the existence of three distinct alpha-class glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver."
McLellan L.I., Kerr L.A., Cronshaw A.D., Hayes J.D.
Biochem. J. 276:461-469(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-36; 51-59; 63-165 AND 208-223, INDUCTION.
Tissue: Liver.
[4]"Residue R216 and catalytic efficiency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide."
Gu Y., Singh S.V., Ji X.
Biochemistry 39:12552-12557(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND SUBSTRATE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19256 expand/collapse EMBL AC list , M19251, M19252, M19253, M19254, M19255 Genomic DNA. Translation: AAA37750.1. Sequence problems.
BC132572 mRNA. Translation: AAI32573.1.
BC132576 mRNA. Translation: AAI32577.1.
CCDSCCDS23358.1.
PIRA27848.
RefSeqNP_032207.3. NM_008181.3.
UniGeneMm.467426.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3AX-ray1.90A/B2-223[»]
1F3BX-ray2.00A/B2-223[»]
ProteinModelPortalP13745.
SMRP13745. Positions 2-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP13745. 3 interactions.
MINTMINT-4096961.

Chemistry

DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP13745.

Proteomic databases

MaxQBP13745.
PaxDbP13745.
PRIDEP13745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098537; ENSMUSP00000096139; ENSMUSG00000074183.
GeneID14857.
KEGGmmu:14857.
UCSCuc009qtz.1. mouse.

Organism-specific databases

CTD2938.
MGIMGI:1095417. Gsta1.

Phylogenomic databases

eggNOGNOG266414.
GeneTreeENSGT00670000097856.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidA2RTN4.
KOK00799.
OMAILHYSND.
OrthoDBEOG79CZ0K.
PhylomeDBP13745.
TreeFamTF105321.

Gene expression databases

BgeeP13745.
CleanExMM_GSTA1.
GenevestigatorP13745.

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]
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

EvolutionaryTraceP13745.
NextBio287087.
PROP13745.
SOURCESearch...

Entry information

Entry nameGSTA1_MOUSE
AccessionPrimary (citable) accession number: P13745
Secondary accession number(s): A2RTN4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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