Mgst1 microsomal glutathione S-transferase 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Mgst1provided by RGD
Official Full Name: microsomal glutathione S-transferase 1provided by RGD
Primary source: RGD:70927
See related: Ensembl:ENSRNOG00000007743 AllianceGenome:RGD:70927
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables glutathione binding activity; glutathione transferase activity; and identical protein binding activity. Involved in several processes, including Leydig cell differentiation; response to lipopolysaccharide; and response to xenobiotic stimulus. Located in several cellular components, including endoplasmic reticulum; mitochondrion; and peroxisomal membrane. Is integral component of membrane. Orthologous to human MGST1 (microsomal glutathione S-transferase 1). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Liver (RPKM 16474.0), Adrenal (RPKM 2830.6) and 2 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 4q44

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	4	NC_086022.1 (172760930..172776157)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	4	NC_051339.1 (171029666..171044893)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	4	NC_005103.4 (172119382..172134609)

Chromosome 4 - NC_086022.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The functional unit is a homotrimer centered on the crystallographic three-fold axes of the unit cell. The GSH substrate binds in an extended conformation at the interface between two subunits of the trimer supported by new in vitro mutagenesis data.
Title: Dead-end complex, lipid interactions and catalytic mechanism of microsomal glutathione transferase 1, an electron crystallography and mutagenesis investigation.
Since Mgst1expression was reported to decline with age, our results could represent a putative adaptive process during aging. It could also be an early mechanism protecting neuronal cells against some neurodegenerative insults
Title: Downregulation of microsomal glutathione-S-transferase 1 modulates protective mechanisms in differentiated PC12 cells.
Two doxorubicin derivatives/prodrugs (DNS-DOX; MNS-DOX) are substrates for MGST1; neoplasm drug resistance can be overcome in cell lines over-expressing recombinant MGST1.
Title: Characterization of new potential anticancer drugs designed to overcome glutathione transferase mediated resistance.
These results indicate that mitochondrial membrane glutathione transferase in the outer mitochondrial membrane is activated by gallic acid, which may contribute to mitochondrial permeability transition pore formation.
Title: Contribution of liver mitochondrial membrane-bound glutathione transferase to mitochondrial permeability transition pores.
Increased expression of miR-34a and miR-93 in rat liver during aging, and their impact on the expression of Mgst1 and Sirt1.
Title: Increased expression of miR-34a and miR-93 in rat liver during aging, and their impact on the expression of Mgst1 and Sirt1.
Results indicate that mtMGST1 is activated through mixed disulfide bond formation that contributes to cytochrome c release from mitochondria through the MPT pore.
Title: Novel function of glutathione transferase in rat liver mitochondrial membrane: role for cytochrome c release from mitochondria.
activation of microsomal glutathione S-transferase 1 by peroxynitrite is mediated by nitration of tyrosine residue 92
Title: Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione s-transferase by peroxynitrite.
measured mass of the homotrimer is 53 kDa, allowing for the mass of three MGST molecules in complex with one glutathione molecule.
Title: Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathione transferase-1 by electrospray mass spectrometry.
These results demonstrate that MGST1 is not a ready candidate for S-nitrosylation in the cellular content, despite its susceptibility to S-nitrosylation under broken cell conditions.
Title: Further evidence that rat liver microsomal glutathione transferase 1 is not a cellular protein target for S-nitrosylation.
Solvent kinetic isotope effect measurements demonstrated a 2-fold decrease in the rate constant (k(2)) for thiolate formation and k(cat) (in the reaction with 1-chloro-2,4-dinitrobenzene) for both unactivated and activated MGST1
Title: Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal glutathione transferase 1.

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General gene information

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Markers

RH142292 (e-PCR)
- UniSTS:231539

BI277057 (e-PCR)
- UniSTS:243579

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables glutathione binding	IDA Inferred from Direct Assay more info	PubMed
enables glutathione peroxidase activity	IEA Inferred from Electronic Annotation more info
enables glutathione peroxidase activity	ISO Inferred from Sequence Orthology more info
enables glutathione transferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables glutathione transferase activity	IDA Inferred from Direct Assay more info	PubMed
enables glutathione transferase activity	IEA Inferred from Electronic Annotation more info
enables glutathione transferase activity	ISO Inferred from Sequence Orthology more info
enables glutathione transferase activity	TAS Traceable Author Statement more info	PubMed
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in Leydig cell differentiation	IEP Inferred from Expression Pattern more info	PubMed
involved_in cellular oxidant detoxification	IEA Inferred from Electronic Annotation more info
involved_in cellular response to lipid hydroperoxide	IEA Inferred from Electronic Annotation more info
involved_in cellular response to lipid hydroperoxide	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within glutathione metabolic process	ISO Inferred from Sequence Orthology more info
involved_in glutathione transport	IEA Inferred from Electronic Annotation more info
involved_in glutathione transport	ISO Inferred from Sequence Orthology more info
involved_in response to lipopolysaccharide	IDA Inferred from Direct Assay more info	PubMed
involved_in response to xenobiotic stimulus	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in apical part of cell	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrial outer membrane	IEA Inferred from Electronic Annotation more info
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in peroxisomal membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: microsomal glutathione S-transferase 1

Names: microsomal GST-1; microsomal GST-I

NP_599176.1

EC 2.5.1.18

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.