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P08011 (MGST1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. 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:
Microsomal glutathione S-transferase 1

Short name=Microsomal GST-1
EC=2.5.1.18
Alternative name(s):
Microsomal GST-I
Gene names
Name:Mgst1
Synonyms:Gst12
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length155 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.

Enzyme regulation

Can be activated by reagents that attack Cys-50 sulfhydryl, such as N-ethylmaleimide, except in the testis. Activation also occurs via nitration of Tyr-93 by peroxynitrite. Ref.5 Ref.6

Subunit structure

Homotrimer; The trimer binds only one molecule of glutathione. Ref.7

Subcellular location

Microsome. Mitochondrion outer membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.4 Ref.7.

Tissue specificity

Highest in the liver, followed by kidney and testis and much lower in seminal vesicles, spleen, lung and brain.

Post-translational modification

Peroxynitrite induces nitration at Tyr-93 which activates the enzyme.

Sequence similarities

Belongs to the MAPEG family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
Mitochondrion
Mitochondrion outer membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMAcetylation
Nitration
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from expression pattern PubMed 15149725. Source: RGD

cellular response to lipid hydroperoxide

Inferred from electronic annotation. Source: Ensembl

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from direct assay Ref.7. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 17571305. Source: RGD

response to lipopolysaccharide

Inferred from direct assay PubMed 18634816. Source: RGD

response to organonitrogen compound

Inferred from direct assay PubMed 18634816. Source: RGD

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 9010624. Source: RGD

endoplasmic reticulum

Inferred from direct assay PubMed 14561759. Source: HGNC

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from direct assay Ref.7. Source: UniProtKB

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 18634816. Source: RGD

nucleus

Inferred from direct assay PubMed 9010624. Source: RGD

peroxisomal membrane

Inferred from direct assay PubMed 16385473. Source: RGD

   Molecular_functionglutathione binding

Inferred from direct assay Ref.7. Source: UniProtKB

glutathione peroxidase activity

Inferred from electronic annotation. Source: Ensembl

glutathione transferase activity

Traceable author statement Ref.7. Source: UniProtKB

identical protein binding

Inferred from direct assay PubMed 14726533. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 18634816. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 155154Microsomal glutathione S-transferase 1
PRO_0000217739

Regions

Topological domain3 – 97Lumenal Ref.7
Transmembrane10 – 3324Helical
Topological domain34 – 6229Cytoplasmic Ref.7
Transmembrane63 – 9634Helical
Topological domain97 – 993Lumenal Ref.7
Transmembrane100 – 12324Helical
Topological domain124 – 1285Cytoplasmic Ref.7
Transmembrane129 – 14820Helical
Topological domain149 – 1557Lumenal Ref.7

Sites

Binding site381Glutathione
Binding site731Glutathione
Binding site741Glutathione
Binding site761Glutathione
Binding site811Glutathione
Binding site1211Glutathione
Site501Activates the enzyme when modified

Amino acid modifications

Modified residue421N6-acetyllysine By similarity
Modified residue551N6-acetyllysine By similarity
Modified residue601N6-acetyllysine By similarity
Modified residue931Nitrated tyrosine Ref.6

Experimental info

Mutagenesis761H → Q: Decreased enzyme activity. Ref.7
Mutagenesis811E → Q: Loss of enzyme activity. Ref.7
Sequence conflict271M → V AA sequence Ref.3
Sequence conflict551K → G AA sequence Ref.3
Sequence conflict681K → T AA sequence Ref.3
Sequence conflict971G → A AA sequence Ref.3
Sequence conflict1011S → P AA sequence Ref.3
Sequence conflict1341F → K AA sequence Ref.3
Sequence conflict1411T → D AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P08011 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8FB62EEDF5A74489

FASTA15517,472
        10         20         30         40         50         60 
MADLKQLMDN EVLMAFTSYA TIILAKMMFL SSATAFQRLT NKVFANPEDC AGFGKGENAK 

        70         80         90        100        110        120 
KFLRTDEKVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STALIHFRIF VGARIYHTIA 

       130        140        150 
YLTPLPQPNR GLAFFVGYGV TLSMAYRLLR SRLYL 

« Hide

References

« Hide 'large scale' references
[1]"Gene expression of rat and human microsomal glutathione S-transferases."
Dejong J.L., Morgenstern R., Joernvall H., Depierre J.W., Tu C.-P.D.
J. Biol. Chem. 263:8430-8436(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[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: Pituitary.
[3]"Microsomal glutathione transferase. Primary structure."
Morgenstern R., Depierre J.W., Joernvall H.
J. Biol. Chem. 260:13976-13983(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-155.
[4]"The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms."
Morgenstern R., Lundqvist G., Andersson G., Balk L., Depierre J.W.
Biochem. Pharmacol. 33:3609-3614(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: Sprague-Dawley.
Tissue: Liver.
[5]"Reactivity of cysteine-49 and its influence on the activation of microsomal glutathione transferase 1: evidence for subunit interaction."
Svensson R., Rinaldi R., Swedmark S., Morgenstern R.
Biochemistry 39:15144-15149(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE OF CYS-50 IN ENZYME REGULATION.
[6]"Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione s-transferase by peroxynitrite."
Ji Y., Neverova I., Van Eyk J.E., Bennett B.M.
J. Biol. Chem. 281:1986-1991(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION AT TYR-93, ENZYME REGULATION.
[7]"Structural basis for detoxification and oxidative stress protection in membranes."
Holm P.J., Bhakat P., Jegerschold C., Gyobu N., Mitsuoka K., Fujiyoshi Y., Morgenstern R., Hebert H.
J. Mol. Biol. 360:934-945(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-154 IN COMPLEX WITH GLUTATHIONE, SUBUNIT, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, MUTAGENESIS OF HIS-76 AND GLU-81, GLUTATHIONE BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03752 mRNA. Translation: AAA41281.1.
BC063150 mRNA. Translation: AAH63150.1.
PIRA28083.
RefSeqNP_599176.1. NM_134349.3.
UniGeneRn.2580.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H8AX-ray3.20A2-154[»]
ProteinModelPortalP08011.
SMRP08011. Positions 10-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4575717.

Proteomic databases

PaxDbP08011.
PRIDEP08011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010579; ENSRNOP00000010579; ENSRNOG00000007743.
GeneID171341.
KEGGrno:171341.
UCSCRGD:70927. rat.

Organism-specific databases

CTD4257.
RGD70927. Mgst1.

Phylogenomic databases

eggNOGNOG71159.
GeneTreeENSGT00390000011980.
HOGENOMHOG000231759.
HOVERGENHBG052470.
InParanoidP08011.
KOK00799.
OMALIHFRIF.
OrthoDBEOG7288T0.
PhylomeDBP08011.
TreeFamTF105327.

Enzyme and pathway databases

SABIO-RKP08011.

Gene expression databases

ArrayExpressP08011.
GenevestigatorP08011.

Family and domain databases

Gene3D1.20.120.550. 1 hit.
InterProIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamPF01124. MAPEG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08011.
NextBio622110.
PROP08011.

Entry information

Entry nameMGST1_RAT
AccessionPrimary (citable) accession number: P08011
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 109 of the entry and version 3 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