P08010 (GSTM2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase Mu 2
EC=2.5.1.18

Alternative name(s):
GST 4-4
GSTM2-2
Glutathione S-transferase Yb-2
Short name=GST Yb2

Gene names

Name:

Gstm2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › 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.
Subunit structure	Homodimer or heterodimer.
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
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from expression pattern PubMed 16029322. Source: RGD response to organic cyclic compound Inferred from expression pattern PubMed 14646352. Source: RGD sensory perception of smell Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Traceable author statement Ref.4. Source: RGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 11684093. Source: RGD
Molecular_function	glutathione transferase activity Inferred from mutant phenotype PubMed 12027896. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2 Ref.5 Ref.6 Ref.7

Chain

2 – 218

217

Glutathione S-transferase Mu 2

PRO_0000185832

Regions

Domain

2 – 88

87

GST N-terminal

Domain

90 – 214

125

GST C-terminal

Region

7 – 8

2

Glutathione binding

Region

43 – 50

8

Glutathione binding

Region

59 – 60

2

Glutathione binding

Region

72 – 73

2

Glutathione binding

Sites

Binding site

116

1

Substrate By similarity

Experimental info

Sequence conflict

147

1

W → S AA sequence Ref.2

Secondary structure

1

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218

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Turn

12 – 14

3

Helix

15 – 23

9

Beta strand

28 – 33

6

Turn

38 – 40

3

Helix

44 – 50

7

Beta strand

60 – 65

6

Beta strand

68 – 72

5

Helix

73 – 83

11

Helix

91 – 116

26

Helix

120 – 142

23

Beta strand

150 – 152

3

Helix

155 – 170

16

Turn

172 – 177

6

Helix

179 – 189

11

Helix

192 – 198

7

Beta strand

214 – 216

3

Sequences

	Sequence		Length	Mass (Da)
	P08010 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: C23B30C171DB852F	FASTA	218	25,703
	10 20 30 40 50 60 MPMTLGYWDI RGLAHAIRLF LEYTDTSYED KKYSMGDAPD YDRSQWLSEK FKLGLDFPNL 70 80 90 100 110 120 PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDVL ENQAMDTRLQ LAMVCYSPDF 130 140 150 160 170 180 ERKKPEYLEG LPEKMKLYSE FLGKQPWFAG NKITYVDFLV YDVLDQHRIF EPKCLDAFPN 190 200 210 LKDFVARFEG LKKISDYMKS GRFLSKPIFA KMAFWNPK

References

[1]	"Gene expression of rat glutathione S-transferases. Evidence for gene conversion in the evolution of the Yb multigene family." Lai H.-C.J., Qian B., Grove G., Tu C.-P.D. J. Biol. Chem. 263:11389-11395(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cytosolic rat liver glutathione transferase 4-4. Primary structure of the protein reveals extensive differences between homologous glutathione transferases of classes alpha and mu." Alin P., Mannervik B., Joernvall H. Eur. J. Biochem. 156:343-350(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-218. Strain: Sprague-Dawley.
[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] OF 25-218.
[4]	"Rat glutathione S-transferases supergene family. Characterization of an anionic Yb subunit cDNA clone." Lai H.-C.J., Tu C.-P.D. J. Biol. Chem. 261:13793-13799(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-218.
[5]	"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 2-26.
[6]	"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 2-28.
[7]	"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 2-22. Strain: Wistar. Tissue: Olfactory epithelium.
[8]	Lubec G., Afjehi-Sadat L., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-43; 137-144; 153-168 AND 174-182, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain and Spinal cord.
[9]	"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 (1.7 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02592 mRNA. Translation: AAA41285.1.
M13590 mRNA. Translation: AAA42351.1.
J03914 Genomic DNA. Translation: AAA41296.1.

IPI

IPI00411230.

PIR

XURTG4. A29231.

RefSeq

NP_803175.1. NM_177426.1.

UniGene

Rn.625.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B4P	X-ray	1.70	A	2-218	[»]

ProteinModelPortal

P08010.

SMR

P08010. Positions 2-218.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08010. 1 interaction.

Proteomic databases

PaxDb

P08010.

PRIDE

P08010.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000019094.

GeneID

24424.

KEGG

rno:24424.

UCSC

RGD:2756. rat.

Organism-specific databases

CTD

2946.

RGD

2756. Gstm2.

Phylogenomic databases

eggNOG

NOG300089.

GeneTree

ENSGT00550000074559.

HOGENOM

HOG000115735.

HOVERGEN

HBG106842.

InParanoid

P08010.

KO

K00799.

OMA

DTSYEDK.

OrthoDB

EOG47D9H2.

Gene expression databases

ArrayExpress

P08010.

Genevestigator

P08010.

GermOnline

ENSRNOG00000019094. 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

CHEMBL2504.

EvolutionaryTrace

P08010.

NextBio

603291.

Entry information

Entry name

GSTM2_RAT

Accession

Primary (citable) accession number: P08010

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program