Q91VS7 (MGST1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 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 component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Acetylation Nitration
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from electronic annotation. Source: Compara cellular response to lipid hydroperoxide Inferred from electronic annotation. Source: Compara 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: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to organic nitrogen Inferred from electronic annotation. Source: Compara
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to 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 nucleus Inferred from electronic annotation. Source: Compara peroxisomal membrane Inferred from electronic annotation. Source: Compara
Molecular_function	glutathione binding Inferred from electronic annotation. Source: Compara glutathione peroxidase activity Inferred from electronic annotation. Source: Compara glutathione transferase activity Inferred from direct assay PubMed 10767383. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 155	154	Microsomal glutathione S-transferase 1		PRO_0000217737
Regions
	Topological domain	3 – 9	7	Lumenal By similarity
	Transmembrane	10 – 33	24	Helical; By similarity
	Topological domain	34 – 62	29	Cytoplasmic By similarity
	Transmembrane	63 – 96	34	Helical; By similarity
	Topological domain	97 – 99	3	Lumenal By similarity
	Transmembrane	100 – 123	24	Helical; By similarity
	Topological domain	124 – 128	5	Cytoplasmic By similarity
	Transmembrane	129 – 148	20	Helical; By similarity
	Topological domain	149 – 155	7	Lumenal By similarity
Sites
	Binding site	38	1	Glutathione By similarity
	Binding site	73	1	Glutathione By similarity
	Binding site	74	1	Glutathione By similarity
	Binding site	76	1	Glutathione By similarity
	Binding site	81	1	Glutathione By similarity
	Binding site	121	1	Glutathione By similarity
	Site	50	1	Activates the enzyme when modified By similarity
Amino acid modifications
	Modified residue	42	1	N6-acetyllysine Ref.4
	Modified residue	55	1	N6-acetyllysine Ref.4
	Modified residue	93	1	Nitrated tyrosine By similarity
Experimental info
	Sequence conflict	5	1	R → K in AAD51096. Ref.1
	Sequence conflict	56	1	G → V in AAH09155. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q91VS7 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C1E202663496C762	FASTA	155	17,552
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42 AND LYS-55, MASS SPECTROMETRY. 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.
IPI	IPI00331322.
RefSeq	NP_064330.2. NM_019946.4.
UniGene	Mm.14796.
3D structure databases
ProteinModelPortal	Q91VS7.
SMR	Q91VS7. Positions 10-148.
ModBase	Search...
PTM databases
PhosphoSite	Q91VS7.
Proteomic databases
PaxDb	Q91VS7.
PRIDE	Q91VS7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000008684; ENSMUSP00000008684; ENSMUSG00000008540. ENSMUST00000120230; ENSMUSP00000113859; ENSMUSG00000008540. ENSMUST00000120302; ENSMUSP00000113257; ENSMUSG00000008540.
GeneID	56615.
KEGG	mmu:56615.
Organism-specific databases
CTD	4257.
MGI	MGI:1913850. Mgst1.
Phylogenomic databases
eggNOG	NOG71159.
GeneTree	ENSGT00390000011980.
HOGENOM	HOG000231759.
HOVERGEN	HBG052470.
InParanoid	Q91VS7.
KO	K00799.
OrthoDB	EOG4DJJXQ.
Gene expression databases
ArrayExpress	Q91VS7.
Bgee	Q91VS7.
CleanEx	MM_MGST1.
Genevestigator	Q91VS7.
GermOnline	ENSMUSG00000008540. Mus musculus.
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
ChiTaRS	MGST1. mouse.
NextBio	313039.
SOURCE	Search...

Entry information

Entry name

MGST1_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program