Glutathione S-transferase Mu 1 - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

P04905 (GSTM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 134. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

Recommended name:
Glutathione S-transferase Mu 1
EC=2.5.1.18

Alternative name(s):
GST 3-3
GSTM1-1
Glutathione S-transferase Yb-1
Short name=GST Yb1

Gene names

Name:

Gstm1

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	218 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. The olfactory GST may be crucial for the acuity of the olfactory process.
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.15 Ref.16
Subunit structure	Homodimer or heterodimer. Ref.3
Subcellular location	Cytoplasm.
Miscellaneous	Yb subclass selectively binds steroid hormones.
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Olfaction Sensory transduction
Cellular component	Cytoplasm
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from direct assay PubMed 10229687. Source: UniProtKB response to amino acid stimulus Inferred from expression pattern PubMed 11040448. Source: RGD response to antibiotic Inferred from expression pattern PubMed 8773182. Source: RGD response to lithium ion Inferred from expression pattern PubMed 18082333. Source: RGD sensory perception of smell Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from direct assay PubMed 10229687. Source: RGD
Molecular_function	glutathione transferase activity Inferred from direct assay PubMed 10229687. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 11015213. Source: RGD steroid binding Inferred from physical interaction PubMed 10229687. 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 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Chain

2 – 218

217

Glutathione S-transferase Mu 1

PRO_0000185831

Regions

Domain

2 – 88

GST N-terminal

Domain

90 – 208

119

GST C-terminal

Region

7 – 8

Glutathione binding

Region

43 – 50

Glutathione binding

Region

59 – 60

Glutathione binding

Region

72 – 73

Glutathione binding

Sites

Binding site

116

Substrate By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphotyrosine By similarity

Experimental info

Mutagenesis

Y → F or L: Reduces catalytic activity about 100-fold. Ref.16

Mutagenesis

C → S: No change in activity. Ref.12

Mutagenesis

116

Y → F: Reduces enzyme activity about 100-fold. Ref.15

Sequence conflict

199 – 200

KS → NC in AAA41287. Ref.2

Secondary structure

218

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04905 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1A8E80D09A5CACA8
Show »

FASTA

218

25,914

        10         20         30         40         50         60 
MPMILGYWNV RGLTHPIRLL LEYTDSSYEE KRYAMGDAPD YDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSRKI TQSNAIMRYL ARKHHLCGET EEERIRADIV ENQVMDNRMQ LIMLCYNPDF 

       130        140        150        160        170        180 
EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYHIF EPKCLDAFPN 

       190        200        210 
LKDFLARFEG LKKISAYMKS SRYLSTPIFS KLAQWSNK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of a cDNA for a rat liver glutathione S-transferase Yb subunit." Lai H.-C.J., Grove G., Tu C.-P.D. Nucleic Acids Res. 14:6101-6114(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Rat liver glutathione S-transferases. Nucleotide sequence analysis of a Yb1 cDNA clone and prediction of the complete amino acid sequence of the Yb1 subunit." Ding G.J.-F., Lu A.Y.H., Pickett C.B. J. Biol. Chem. 260:13268-13271(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital." Ding G.J.-F., Ding V.D.-H., Rodkey J.A., Bennett C.D., Lu A.Y.H., Pickett C.B. J. Biol. Chem. 261:7952-7957(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-24, SUBUNIT.
[4]	"Identification of glutathione S-transferase Yb1 mRNA as the androgen-repressed mRNA by cDNA cloning and sequence analysis." Chang C., Saltzman A.G., Sorensen N.S., Hiipakka R.A., Liao S. J. Biol. Chem. 262:11901-11903(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"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.
[6]	"Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3." Katusz R.M., Bono B., Colman R.F. Arch. Biochem. Biophys. 298:667-677(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20; 83-96 AND 109-122.
[7]	"Expression of Yb1 glutathione S-transferase using a baculovirus expression system." Hsieh J.C., Liu L.F., Chen W.L., Tam M.F. Biochem. Biophys. Res. Commun. 162:1147-1154(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21 AND 212-218.
[8]	"Identification of rat liver glutathione S-transferase Yb subunits by partial N-terminal sequencing after electroblotting of proteins onto a polyvinylidene difluoride membrane from an analytical isoelectric focusing gel." Chang L.H., Hsieh J.C., Chen W.L., Tam M.F. Electrophoresis 11:589-593(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.
[9]	"Glutathione S-transferases in rat olfactory epithelium: purification, molecular properties and odorant biotransformation." Ben-Arie N., Khen M., Lancet D. Biochem. J. 292:379-384(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24. Strain: Wistar. Tissue: Olfactory epithelium.
[10]	"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties." Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H. Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20.
[11]	Lubec G., Chen W.-Q., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 19-32; 33-50; 53-68; 70-78; 97-108; 137-144; 174-187 AND 203-218, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain and Hippocampus.
[12]	"Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 3-3." Hsieh J.-C., Huang S.-C., Chen W.-L., Lai Y.-C., Tam M.F. Biochem. J. 278:293-297(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-87.
[13]	"The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution." Ji X., Zhang P., Armstrong R.N., Gilliland G.L. Biochemistry 31:10169-10184(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
[14]	"New crystal forms of a mu-class glutathione S-transferase from rat liver." Fu J.-H., Rose J., Tam M.F., Wang B.-C. Acta Crystallogr. D 50:219-224(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[15]	"Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene." Ji X., Johnson W.W., Sesay M.A., Dickert L., Prasad S.M., Ammon H.L., Armstrong R.N., Gilliland G.L. Biochemistry 33:1043-1052(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-116.
[16]	"First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase." Xiao G., Liu S., Ji X., Johnson W.W., Chen J., Parsons J.F., Stevens W.J., Gilliland G.L., Armstrong R.N. Biochemistry 35:4753-4765(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT PHE-7 IN COMPLEXES WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-7.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04229 mRNA. Translation: CAA27811.1.
M11719 mRNA. Translation: AAA41287.1.
J02810 mRNA. Translation: AAA41293.1.
BC063172 mRNA. Translation: AAH63172.1.

IPI

IPI00231639.

PIR

A29794.

RefSeq

NP_058710.1. NM_017014.1.

UniGene

Rn.202944.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GSB	X-ray	2.50	A/B/C/D	2-218	[»]
1GSC	X-ray	2.50	A/B/C/D	2-218	[»]
1MTC	X-ray	2.20	A/B	2-217	[»]
2GST	X-ray	1.80	A/B	2-218	[»]
3FYG	X-ray	2.20	A/B	2-217	[»]
3GST	X-ray	1.90	A/B	2-218	[»]
4GST	X-ray	1.90	A/B	2-217	[»]
5FWG	X-ray	2.00	A/B	2-218	[»]
5GST	X-ray	2.00	A/B	2-217	[»]
6GST	X-ray	2.20	A/B	2-218	[»]
6GSU	X-ray	1.85	A/B	2-217	[»]
6GSV	X-ray	1.75	A/B	2-217	[»]
6GSW	X-ray	1.85	A/B	2-217	[»]
6GSX	X-ray	1.91	A/B	2-217	[»]
6GSY	X-ray	2.20	A/B	2-218	[»]

ProteinModelPortal

P04905.

SMR

P04905. Positions 2-218.

ModBase

Search...

PTM databases

PhosphoSite

P04905.

Proteomic databases

PaxDb

P04905.

PRIDE

P04905.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

24423.

KEGG

rno:24423.

UCSC

RGD:2755. rat.

Organism-specific databases

CTD

2944.

RGD

2755. Gstm1.

Phylogenomic databases

eggNOG

KOG1695.

HOGENOM

HOG000115735.

HOVERGEN

HBG106842.

InParanoid

P04905.

K00799.

Gene expression databases

ArrayExpress

P04905.

Genevestigator

P04905.

GermOnline

ENSRNOG00000029726. Rattus norvegicus.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01267. GSTRNSFRASEM.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2209.

EvolutionaryTrace

P04905.

NextBio

603287.

Entry information

Entry name

GSTM1_RAT

Accession

Primary (citable) accession number: P04905

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 134 of the entry and version 2 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

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents