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P08010 (GSTM2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 Mu 2

EC=2.5.1.18
Alternative name(s):
GST 4-4
GSTM2-2
Glutathione S-transferase Yb-2
Short name=GST Yb2
Gene names
Name:Gstm2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length218 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. The olfactory GST may be crucial for the acuity of the olfactory process.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subunit structure

Homodimer or heterodimer.

Subcellular location

Cytoplasm.

Miscellaneous

Yb subclass selectively binds steroid hormones.

Sequence similarities

Belongs to the GST superfamily. Mu 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.2 Ref.5 Ref.6 Ref.7
Chain2 – 218217Glutathione S-transferase Mu 2
PRO_0000185832

Regions

Domain2 – 8887GST N-terminal
Domain90 – 214125GST C-terminal
Region7 – 82Glutathione binding
Region43 – 508Glutathione binding
Region59 – 602Glutathione binding
Region72 – 732Glutathione binding

Sites

Binding site1161Substrate By similarity

Experimental info

Sequence conflict1471W → S AA sequence Ref.2

Secondary structure

................................. 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08010 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C23B30C171DB852F

FASTA21825,703
        10         20         30         40         50         60 
MPMTLGYWDI RGLAHAIRLF LEYTDTSYED KKYSMGDAPD YDRSQWLSEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDVL ENQAMDTRLQ LAMVCYSPDF 

       130        140        150        160        170        180 
ERKKPEYLEG LPEKMKLYSE FLGKQPWFAG NKITYVDFLV YDVLDQHRIF EPKCLDAFPN 

       190        200        210 
LKDFVARFEG LKKISDYMKS GRFLSKPIFA KMAFWNPK 

« Hide

References

[1]"Gene expression of rat glutathione S-transferases. Evidence for gene conversion in the evolution of the Yb multigene family."
Lai H.-C.J., Qian B., Grove G., Tu C.-P.D.
J. Biol. Chem. 263:11389-11395(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cytosolic rat liver glutathione transferase 4-4. Primary structure of the protein reveals extensive differences between homologous glutathione transferases of classes alpha and mu."
Alin P., Mannervik B., Joernvall H.
Eur. J. Biochem. 156:343-350(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-218.
Strain: Sprague-Dawley.
[3]"Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital."
Ding G.J.-F., Ding V.D.-H., Rodkey J.A., Bennett C.D., Lu A.Y.H., Pickett C.B.
J. Biol. Chem. 261:7952-7957(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-218.
[4]"Rat glutathione S-transferases supergene family. Characterization of an anionic Yb subunit cDNA clone."
Lai H.-C.J., Tu C.-P.D.
J. Biol. Chem. 261:13793-13799(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-218.
[5]"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.
[6]"Identification of rat liver glutathione S-transferase Yb subunits by partial N-terminal sequencing after electroblotting of proteins onto a polyvinylidene difluoride membrane from an analytical isoelectric focusing gel."
Chang L.H., Hsieh J.C., Chen W.L., Tam M.F.
Electrophoresis 11:589-593(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-28.
[7]"Glutathione S-transferases in rat olfactory epithelium: purification, molecular properties and odorant biotransformation."
Ben-Arie N., Khen M., Lancet D.
Biochem. J. 292:379-384(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22.
Strain: Wistar.
Tissue: Olfactory epithelium.
[8]Lubec G., Afjehi-Sadat L., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 33-43; 137-144; 153-168 AND 174-182, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[9]"First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase."
Xiao G., Liu S., Ji X., Johnson W.W., Chen J., Parsons J.F., Stevens W.J., Gilliland G.L., Armstrong R.N.
Biochemistry 35:4753-4765(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02592 mRNA. Translation: AAA41285.1.
M13590 mRNA. Translation: AAA42351.1.
J03914 Genomic DNA. Translation: AAA41296.1.
PIRXURTG4. A29231.
RefSeqNP_803175.1. NM_177426.1.
UniGeneRn.625.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4PX-ray1.70A2-218[»]
ProteinModelPortalP08010.
SMRP08010. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08010. 1 interaction.

Chemistry

ChEMBLCHEMBL2504.

Proteomic databases

PaxDbP08010.
PRIDEP08010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000019094.
GeneID24424.
KEGGrno:24424.
UCSCRGD:2756. rat.

Organism-specific databases

CTD2946.
RGD2756. Gstm2.

Phylogenomic databases

eggNOGNOG300089.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115735.
HOVERGENHBG106842.
InParanoidP08010.
KOK00799.
OMARITESWA.
OrthoDBEOG7KH9M3.
PhylomeDBP08010.
TreeFamTF353040.

Gene expression databases

ArrayExpressP08010.
GenevestigatorP08010.

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...

Other

EvolutionaryTraceP08010.
NextBio603291.
PROP08010.

Entry information

Entry nameGSTM2_RAT
AccessionPrimary (citable) accession number: P08010
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 139 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