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P04905 (GSTM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. 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 1

EC=2.5.1.18
Alternative name(s):
GST 3-3
GSTM1-1
Glutathione S-transferase Yb-1
Short name=GST Yb1
Gene names
Name:Gstm1
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. Ref.15 Ref.16

Subunit structure

Homodimer or heterodimer. Ref.3

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.

Ontologies

Keywords
   Biological processOlfaction
Sensory transduction
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from direct assay PubMed 10229687. Source: UniProtKB

response to amino acid

Inferred from expression pattern PubMed 11040448. Source: RGD

response to antibiotic

Inferred from expression pattern PubMed 8773182. Source: RGD

response to axon injury

Inferred from expression pattern PubMed 20298122. Source: RGD

response to drug

Inferred from expression pattern PubMed 18754104. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 22545783. Source: RGD

response to lead ion

Inferred from expression pattern PubMed 9750042. Source: RGD

response to lithium ion

Inferred from expression pattern PubMed 18082333. Source: RGD

response to metal ion

Inferred from expression pattern PubMed 23470461. Source: RGD

sensory perception of smell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from direct assay PubMed 10229687. Source: RGD

protein complex

Inferred from direct assay PubMed 11015213. Source: RGD

   Molecular_functionglutathione transferase activity

Inferred from direct assay PubMed 10229687. Source: RGD

nickel cation binding

Inferred from direct assay PubMed 7831282. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 11015213. Source: RGD

steroid binding

Inferred from physical interaction PubMed 10229687. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Chain2 – 218217Glutathione S-transferase Mu 1
PRO_0000185831

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding
Region43 – 508Glutathione binding
Region59 – 602Glutathione binding
Region72 – 732Glutathione binding

Sites

Binding site1161Substrate By similarity

Experimental info

Mutagenesis71Y → F or L: Reduces catalytic activity about 100-fold. Ref.16
Mutagenesis871C → S: No change in activity. Ref.12
Mutagenesis1161Y → F: Reduces enzyme activity about 100-fold. Ref.15
Sequence conflict199 – 2002KS → NC in AAA41287. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P04905 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1A8E80D09A5CACA8

FASTA21825,914
        10         20         30         40         50         60 
MPMILGYWNV RGLTHPIRLL LEYTDSSYEE KRYAMGDAPD YDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSRKI TQSNAIMRYL ARKHHLCGET EEERIRADIV ENQVMDNRMQ LIMLCYNPDF 

       130        140        150        160        170        180 
EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYHIF EPKCLDAFPN 

       190        200        210 
LKDFLARFEG LKKISAYMKS SRYLSTPIFS KLAQWSNK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of a cDNA for a rat liver glutathione S-transferase Yb subunit."
Lai H.-C.J., Grove G., Tu C.-P.D.
Nucleic Acids Res. 14:6101-6114(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rat liver glutathione S-transferases. Nucleotide sequence analysis of a Yb1 cDNA clone and prediction of the complete amino acid sequence of the Yb1 subunit."
Ding G.J.-F., Lu A.Y.H., Pickett C.B.
J. Biol. Chem. 260:13268-13271(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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], PROTEIN SEQUENCE OF 2-24, SUBUNIT.
[4]"Identification of glutathione S-transferase Yb1 mRNA as the androgen-repressed mRNA by cDNA cloning and sequence analysis."
Chang C., Saltzman A.G., Sorensen N.S., Hiipakka R.A., Liao S.
J. Biol. Chem. 262:11901-11903(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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: Pituitary.
[6]"Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3."
Katusz R.M., Bono B., Colman R.F.
Arch. Biochem. Biophys. 298:667-677(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20; 83-96 AND 109-122.
[7]"Expression of Yb1 glutathione S-transferase using a baculovirus expression system."
Hsieh J.C., Liu L.F., Chen W.L., Tam M.F.
Biochem. Biophys. Res. Commun. 162:1147-1154(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21 AND 212-218.
[8]"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 2-26.
[9]"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 2-24.
Strain: Wistar.
Tissue: Olfactory epithelium.
[10]"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 2-20.
[11]Lubec G., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 19-32; 33-50; 53-68; 70-78; 97-108; 137-144; 174-187 AND 203-218, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
[12]"Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 3-3."
Hsieh J.-C., Huang S.-C., Chen W.-L., Lai Y.-C., Tam M.F.
Biochem. J. 278:293-297(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-87.
[13]"The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution."
Ji X., Zhang P., Armstrong R.N., Gilliland G.L.
Biochemistry 31:10169-10184(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
[14]"New crystal forms of a mu-class glutathione S-transferase from rat liver."
Fu J.-H., Rose J., Tam M.F., Wang B.-C.
Acta Crystallogr. D 50:219-224(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[15]"Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene."
Ji X., Johnson W.W., Sesay M.A., Dickert L., Prasad S.M., Ammon H.L., Armstrong R.N., Gilliland G.L.
Biochemistry 33:1043-1052(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-116.
[16]"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 (1.75 ANGSTROMS) OF MUTANT PHE-7 IN COMPLEXES WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04229 mRNA. Translation: CAA27811.1.
M11719 mRNA. Translation: AAA41287.1.
J02810 mRNA. Translation: AAA41293.1.
BC063172 mRNA. Translation: AAH63172.1.
PIRA29794.
RefSeqNP_058710.1. NM_017014.1.
UniGeneRn.202944.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GSBX-ray2.50A/B/C/D2-218[»]
1GSCX-ray2.50A/B/C/D2-218[»]
1MTCX-ray2.20A/B2-218[»]
2GSTX-ray1.80A/B2-218[»]
3FYGX-ray2.20A/B2-218[»]
3GSTX-ray1.90A/B2-218[»]
4GSTX-ray1.90A/B2-218[»]
5FWGX-ray2.00A/B2-218[»]
5GSTX-ray2.00A/B2-218[»]
6GSTX-ray2.20A/B2-218[»]
6GSUX-ray1.85A/B2-218[»]
6GSVX-ray1.75A/B2-218[»]
6GSWX-ray1.85A/B2-218[»]
6GSXX-ray1.91A/B2-218[»]
6GSYX-ray2.20A/B2-218[»]
ProteinModelPortalP04905.
SMRP04905. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4564586.

Chemistry

ChEMBLCHEMBL2209.

PTM databases

PhosphoSiteP04905.

Proteomic databases

PaxDbP04905.
PRIDEP04905.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24423.
KEGGrno:24423.
UCSCRGD:2755. rat.

Organism-specific databases

CTD2944.
RGD2755. Gstm1.

Phylogenomic databases

eggNOGKOG1695.
HOGENOMHOG000115735.
HOVERGENHBG106842.
InParanoidP04905.
KOK00799.
PhylomeDBP04905.

Gene expression databases

GenevestigatorP04905.

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

EvolutionaryTraceP04905.
NextBio603287.

Entry information

Entry nameGSTM1_RAT
AccessionPrimary (citable) accession number: P04905
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 146 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