Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Microsomal glutathione S-transferase 1

Gene

Mgst1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

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

Enzyme regulationi

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Glutathione1 Publication
Sitei50 – 501Activates the enzyme when modified
Binding sitei73 – 731Glutathione1 Publication
Binding sitei74 – 741Glutathione1 Publication
Binding sitei76 – 761Glutathione1 Publication
Binding sitei81 – 811Glutathione1 Publication
Binding sitei121 – 1211Glutathione1 Publication

GO - Molecular functioni

  1. glutathione binding Source: UniProtKB
  2. glutathione peroxidase activity Source: Ensembl
  3. glutathione transferase activity Source: UniProtKB
  4. identical protein binding Source: RGD
  5. protein homodimerization activity Source: RGD

GO - Biological processi

  1. cellular response to lipid hydroperoxide Source: Ensembl
  2. glutathione metabolic process Source: Ensembl
  3. Leydig cell differentiation Source: RGD
  4. protein homotrimerization Source: UniProtKB
  5. response to drug Source: RGD
  6. response to lipopolysaccharide Source: RGD
  7. response to organonitrogen compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 5301.
ReactomeiREACT_278052. Aflatoxin activation and detoxification.
REACT_316307. Glutathione conjugation.
SABIO-RKP08011.

Names & Taxonomyi

Protein namesi
Recommended name:
Microsomal glutathione S-transferase 1 (EC:2.5.1.18)
Short name:
Microsomal GST-1
Alternative name(s):
Microsomal GST-I
Gene namesi
Name:Mgst1
Synonyms:Gst12
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi70927. Mgst1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini3 – 97Lumenal
Transmembranei10 – 3324HelicalAdd
BLAST
Topological domaini34 – 6229CytoplasmicAdd
BLAST
Transmembranei63 – 9634HelicalAdd
BLAST
Topological domaini97 – 993Lumenal
Transmembranei100 – 12324HelicalAdd
BLAST
Topological domaini124 – 1285Cytoplasmic
Transmembranei129 – 14820HelicalAdd
BLAST
Topological domaini149 – 1557Lumenal

GO - Cellular componenti

  1. apical part of cell Source: RGD
  2. endoplasmic reticulum Source: HGNC
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB
  5. mitochondrial inner membrane Source: Ensembl
  6. mitochondrial outer membrane Source: UniProtKB-SubCell
  7. mitochondrion Source: RGD
  8. nucleus Source: RGD
  9. peroxisomal membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761H → Q: Decreased enzyme activity. 1 Publication
Mutagenesisi81 – 811E → Q: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 155154Microsomal glutathione S-transferase 1PRO_0000217739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei93 – 931Nitrated tyrosine1 Publication

Post-translational modificationi

Peroxynitrite induces nitration at Tyr-93 which activates the enzyme.1 Publication

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

PaxDbiP08011.
PRIDEiP08011.

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiP08011. baseline and differential.
GenevestigatoriP08011.

Interactioni

Subunit structurei

Homotrimer; The trimer binds only one molecule of glutathione.1 Publication

Protein-protein interaction databases

MINTiMINT-4575717.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H8Aelectron microscopy3.20A2-155[»]
ProteinModelPortaliP08011.
SMRiP08011. Positions 10-148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08011.

Family & Domainsi

Sequence similaritiesi

Belongs to the MAPEG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71159.
GeneTreeiENSGT00390000011980.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiP08011.
KOiK00799.
OMAiVIKMLAM.
OrthoDBiEOG7288T0.
PhylomeDBiP08011.
TreeFamiTF105327.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLKQLMDN EVLMAFTSYA TIILAKMMFL SSATAFQRLT NKVFANPEDC
60 70 80 90 100
AGFGKGENAK KFLRTDEKVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL
110 120 130 140 150
STALIHFRIF VGARIYHTIA YLTPLPQPNR GLAFFVGYGV TLSMAYRLLR

SRLYL
Length:155
Mass (Da):17,472
Last modified:January 23, 2007 - v3
Checksum:i8FB62EEDF5A74489
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271M → V AA sequence (PubMed:3932348).Curated
Sequence conflicti55 – 551K → G AA sequence (PubMed:3932348).Curated
Sequence conflicti68 – 681K → T AA sequence (PubMed:3932348).Curated
Sequence conflicti97 – 971G → A AA sequence (PubMed:3932348).Curated
Sequence conflicti101 – 1011S → P AA sequence (PubMed:3932348).Curated
Sequence conflicti134 – 1341F → K AA sequence (PubMed:3932348).Curated
Sequence conflicti141 – 1411T → D AA sequence (PubMed:3932348).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03752 mRNA. Translation: AAA41281.1.
BC063150 mRNA. Translation: AAH63150.1.
PIRiA28083.
RefSeqiNP_599176.1. NM_134349.3.
UniGeneiRn.2580.

Genome annotation databases

EnsembliENSRNOT00000010579; ENSRNOP00000010579; ENSRNOG00000007743.
GeneIDi171341.
KEGGirno:171341.
UCSCiRGD:70927. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03752 mRNA. Translation: AAA41281.1.
BC063150 mRNA. Translation: AAH63150.1.
PIRiA28083.
RefSeqiNP_599176.1. NM_134349.3.
UniGeneiRn.2580.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H8Aelectron microscopy3.20A2-155[»]
ProteinModelPortaliP08011.
SMRiP08011. Positions 10-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4575717.

Proteomic databases

PaxDbiP08011.
PRIDEiP08011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010579; ENSRNOP00000010579; ENSRNOG00000007743.
GeneIDi171341.
KEGGirno:171341.
UCSCiRGD:70927. rat.

Organism-specific databases

CTDi4257.
RGDi70927. Mgst1.

Phylogenomic databases

eggNOGiNOG71159.
GeneTreeiENSGT00390000011980.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiP08011.
KOiK00799.
OMAiVIKMLAM.
OrthoDBiEOG7288T0.
PhylomeDBiP08011.
TreeFamiTF105327.

Enzyme and pathway databases

BRENDAi2.5.1.18. 5301.
ReactomeiREACT_278052. Aflatoxin activation and detoxification.
REACT_316307. Glutathione conjugation.
SABIO-RKP08011.

Miscellaneous databases

EvolutionaryTraceiP08011.
NextBioi622110.
PROiP08011.

Gene expression databases

ExpressionAtlasiP08011. baseline and differential.
GenevestigatoriP08011.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1987) [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(2003) [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(1984) [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(1983) [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(1999) [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(2005) [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(2005) [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.

Entry informationi

Entry nameiMGST1_RAT
AccessioniPrimary (citable) accession number: P08011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.