Microsomal glutathione S-transferase 1 - Rattus norvegicus (Rat)

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P08011 (MGST1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Acetylation Nitration
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from expression pattern PubMed 15149725. Source: RGD cellular response to lipid hydroperoxide Inferred from electronic annotation. Source: Compara glutathione metabolic process Inferred from electronic annotation. Source: Compara 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 organic nitrogen Inferred from direct assay PubMed 18634816. Source: RGD
Cellular_component	apical 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 to membrane Inferred from direct assay Ref.7. Source: UniProtKB mitochondrial inner membrane Inferred from electronic annotation. Source: Compara 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_function	glutathione binding Inferred from direct assay Ref.7. Source: UniProtKB glutathione peroxidase activity Inferred from electronic annotation. Source: Compara glutathione transferase activity Traceable author statement Ref.7. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 18634816. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 155

154

Microsomal glutathione S-transferase 1

PRO_0000217739

Regions

Topological domain

3 – 9

Lumenal Ref.7

Transmembrane

10 – 33

Helical

Topological domain

34 – 62

Cytoplasmic Ref.7

Transmembrane

63 – 96

Helical

Topological domain

97 – 99

Lumenal Ref.7

Transmembrane

100 – 123

Helical

Topological domain

124 – 128

Cytoplasmic Ref.7

Transmembrane

129 – 148

Helical

Topological domain

149 – 155

Lumenal Ref.7

Sites

Binding site

Glutathione

Binding site

Glutathione

Binding site

Glutathione

Binding site

Glutathione

Binding site

Glutathione

Binding site

121

Glutathione

Site

Activates the enzyme when modified

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Nitrated tyrosine Ref.6

Experimental info

Mutagenesis

H → Q: Decreased enzyme activity. Ref.7

Mutagenesis

E → Q: Loss of enzyme activity. Ref.7

Sequence conflict

M → V AA sequence Ref.3

Sequence conflict

K → G AA sequence Ref.3

Sequence conflict

K → T AA sequence Ref.3

Sequence conflict

G → A AA sequence Ref.3

Sequence conflict

101

S → P AA sequence Ref.3

Sequence conflict

134

F → K AA sequence Ref.3

Sequence conflict

141

T → D AA sequence Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P08011 [UniParc].

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

155

17,472

        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' referencesShow '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.

IPI

IPI00230889.

PIR

A28083.

RefSeq

NP_599176.1. NM_134349.3.

UniGene

Rn.2580.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H8A	X-ray	3.20	A	2-154	[»]

ProteinModelPortal

P08011.

SMR

P08011. Positions 10-148.

ModBase

Search...

Proteomic databases

PaxDb

P08011.

PRIDE

P08011.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000010579; ENSRNOP00000010579; ENSRNOG00000007743.

GeneID

171341.

KEGG

rno:171341.

UCSC

RGD:70927. rat.

Organism-specific databases

CTD

4257.

RGD

70927. Mgst1.

Phylogenomic databases

eggNOG

NOG71159.

GeneTree

ENSGT00390000011980.

HOGENOM

HOG000231759.

HOVERGEN

HBG052470.

InParanoid

P08011.

K00799.

OMA

ALIHFRI.

OrthoDB

EOG4DJJXQ.

Enzyme and pathway databases

SABIO-RK

P08011.

Gene expression databases

ArrayExpress

P08011.

Genevestigator

P08011.

GermOnline

ENSRNOG00000007743. Rattus norvegicus.

Family and domain databases

Gene3D

1.20.120.550. 1 hit.

InterPro

IPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]

Pfam

PF01124. MAPEG. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08011.

NextBio

622110.

Entry information

Entry name

MGST1_RAT

Accession

Primary (citable) accession number: P08011

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents