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P30116 (GSTMU_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. 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

EC=2.5.1.18
Alternative name(s):
GST class-mu
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Glutathione S-transferase
PRO_0000185836

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding By similarity
Region46 – 505Glutathione binding By similarity
Region59 – 602Glutathione binding By similarity
Region72 – 732Glutathione binding By similarity

Sites

Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P30116 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F5D81F3DE32F9EC5

FASTA21825,690
        10         20         30         40         50         60 
MPVTLGYWDI RGLAHAIRLL LEYTDTSYEE KKYTMGDAPN FDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSHKI TQSNAILRYI ARKHDLCGET EEERIQLDIL ENQAMDTRMQ LAMVCYSPDF 

       130        140        150        160        170        180 
EKRKPEYLEG LPEKMKLYSE FLGKRSWFAG DKITYVDFLI YDVLDQHRIF APKCLDAFPN 

       190        200        210 
LKDFLARFEG LKKISDYMKS SRFSCKQIFA KMAVWNSK 

« Hide

References

[1]"Cloning of a mu-class glutathione S-transferase gene and identification of the glucocorticoid regulatory domains in its 5' flanking sequence."
Fan W.M., Trifiletti R., Norris J.S., Cooper T.M.
Proc. Natl. Acad. Sci. U.S.A. 89:6104-6108(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Smooth muscle.
[2]"Cloning of a mu-class glutathione S-transferase complementary DNA and characterization of its glucocorticoid inducibility in a smooth muscle tumor cell line."
Norris J.S., Schwartz D.A., Macleod S.L., Fan W.M., O'Brien T.J., Harris S.E., Trifiletti R., Cornett L.E., Cooper T.M., Levi W.M., Smith R.G.
Mol. Endocrinol. 5:979-986(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Smooth muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59772 mRNA. Translation: AAA37075.1.
X61033 Genomic DNA. Translation: CAA43368.1.
PIRA23732.
RefSeqNP_001268559.1. NM_001281630.1.

3D structure databases

ProteinModelPortalP30116.
SMRP30116. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP30116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101829268.

Phylogenomic databases

HOVERGENHBG106842.

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.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTMU_MESAU
AccessionPrimary (citable) accession number: P30116
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 77 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