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Q91VS7 (MGST1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Catalytic activity

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

Enzyme regulation

Can be activated by reagents that attack Cys-50 sulfhydryl, such as N-ethylmaleimide. Activation also occurs via nitration of Tyr-93 by peroxynitrite By similarity.

Subunit structure

Homotrimer; The trimer binds only one molecule of glutathione By similarity.

Subcellular location

Microsome By similarity. Mitochondrion outer membrane; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Post-translational modification

Acetylation of Lys-42 and Lys-55 is observed in liver mitochondria from fasted mice but not from fed mice.

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

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 termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular response to lipid hydroperoxide

Inferred from electronic annotation. Source: Ensembl

glutathione metabolic process

Inferred from direct assay PubMed 10767383. Source: MGI

protein homotrimerization

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

peroxisomal membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionglutathione binding

Inferred from electronic annotation. Source: Ensembl

glutathione peroxidase activity

Inferred from electronic annotation. Source: Ensembl

glutathione transferase activity

Inferred from direct assay PubMed 10767383. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 155154Microsomal glutathione S-transferase 1
PRO_0000217737

Regions

Topological domain3 – 97Lumenal By similarity
Transmembrane10 – 3324Helical; By similarity
Topological domain34 – 6229Cytoplasmic By similarity
Transmembrane63 – 9634Helical; By similarity
Topological domain97 – 993Lumenal By similarity
Transmembrane100 – 12324Helical; By similarity
Topological domain124 – 1285Cytoplasmic By similarity
Transmembrane129 – 14820Helical; By similarity
Topological domain149 – 1557Lumenal By similarity

Sites

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

Amino acid modifications

Modified residue421N6-acetyllysine Ref.4
Modified residue551N6-acetyllysine Ref.4
Modified residue601N6-acetyllysine Ref.4

Experimental info

Sequence conflict51R → K in AAD51096. Ref.1
Sequence conflict561G → V in AAH09155. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q91VS7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C1E202663496C762

FASTA15517,552
        10         20         30         40         50         60 
MADLRQLMDN EVLMAFTSYA TIILTKMMFM SSATAFQRIT NKVFANPEDC AGFGKGENAK 

        70         80         90        100        110        120 
KFVRTDEKVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STALMHFRIF VGARIYHTIA 

       130        140        150 
YLTPLPQPNR GLAFFVGYGV TLSMAYRLLR SRLYL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, characterization and bacterial expression of full length cDNA for the mouse liver microsomal glutathione S-transferase."
Raza H., Mullick J., Avadhani N.G.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum and Kidney.
[3]"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: Mammary tumor.
[4]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-55 AND LYS-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF159050 mRNA. Translation: AAD51096.1.
AK002800 mRNA. Translation: BAB22368.1.
AK005122 mRNA. Translation: BAB23827.1.
BC009155 mRNA. Translation: AAH09155.1.
CCDSCCDS20668.1.
RefSeqNP_064330.2. NM_019946.4.
UniGeneMm.14796.

3D structure databases

ProteinModelPortalQ91VS7.
SMRQ91VS7. Positions 10-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91VS7. 2 interactions.
MINTMINT-1840438.

PTM databases

PhosphoSiteQ91VS7.

Proteomic databases

MaxQBQ91VS7.
PaxDbQ91VS7.
PRIDEQ91VS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000008684; ENSMUSP00000008684; ENSMUSG00000008540.
ENSMUST00000120230; ENSMUSP00000113859; ENSMUSG00000008540.
ENSMUST00000120302; ENSMUSP00000113257; ENSMUSG00000008540.
GeneID56615.
KEGGmmu:56615.
UCSCuc009enk.1. mouse.

Organism-specific databases

CTD4257.
MGIMGI:1913850. Mgst1.

Phylogenomic databases

eggNOGNOG71159.
GeneTreeENSGT00390000011980.
HOGENOMHOG000231759.
HOVERGENHBG052470.
InParanoidQ91VS7.
KOK00799.
OrthoDBEOG7288T0.
PhylomeDBQ91VS7.
TreeFamTF105327.

Gene expression databases

ArrayExpressQ91VS7.
BgeeQ91VS7.
CleanExMM_MGST1.
GenevestigatorQ91VS7.

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

ChiTaRSMGST1. mouse.
NextBio313039.
PROQ91VS7.
SOURCESearch...

Entry information

Entry nameMGST1_MOUSE
AccessionPrimary (citable) accession number: Q91VS7
Secondary accession number(s): Q9CQ57, Q9R191
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot