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Q00285 (GSTMU_CRILO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 74. 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 Y1

EC=2.5.1.18
Alternative name(s):
Chain 3
GST class-mu
OrganismCricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Taxonomic identifier10030 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

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 Y1
PRO_0000185835

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
Q00285 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0498A5629DA2DA70

FASTA21825,819
        10         20         30         40         50         60 
MPMILGYWNV RGLTNPIRLL LEYTDSSYEE KKYTMGDAPD SDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSHKI TQSNAILRYI ARKHNLCGET EEERIRVDIV ENQAMDTRMQ LIMLCYNPDF 

       130        140        150        160        170        180 
EKQKPEFLKT IPEKMKMYSE FLGKRPWFAG DKVTLCGFLA YDVLDQYQMF EPKCLDPFPN 

       190        200        210 
LKDFLARFEG LKKISAYMKT SRFLRRPIFS KMAQWSNK 

« Hide

References

[1]"Coamplification of mu class glutathione S-transferase genes and an adenylate deaminase gene in coformycin-resistant Chinese hamster fibroblasts."
de Saint Vincent B.R., Hyrien O., Debatisse M., Buttin G.
Eur. J. Biochem. 193:19-24(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57489 mRNA. Translation: CAA40726.1.

3D structure databases

ProteinModelPortalQ00285.
SMRQ00285. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ00285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_CRILO
AccessionPrimary (citable) accession number: Q00285
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 74 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