P10648 (GSTA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase A2
EC=2.5.1.18

Alternative name(s):
GST class-alpha member 2
Glutathione S-transferase GT41A

Gene names

Name:

Gsta2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	222 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.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the GST superfamily. Alpha family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB response to stilbenoid Inferred from expression pattern. Source: UniProtKB
Molecular function	glutathione transferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 222

221

Glutathione S-transferase A2

PRO_0000185789

Regions

Domain

3 – 83

81

GST N-terminal

Domain

85 – 208

124

GST C-terminal

Region

67 – 68

2

Glutathione binding

Sites

Binding site

9

1

Glutathione By similarity

Binding site

45

1

Glutathione

Binding site

55

1

Glutathione; via amide nitrogen and carbonyl oxygen

Secondary structure

1

.

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222

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Helix

14 – 16

3

Helix

17 – 26

10

Beta strand

31 – 35

5

Helix

38 – 46

9

Beta strand

57 – 60

4

Beta strand

63 – 67

5

Helix

68 – 78

11

Helix

86 – 108

23

Helix

109 – 111

3

Turn

114 – 116

3

Helix

117 – 130

14

Helix

132 – 143

12

Beta strand

146 – 149

4

Helix

155 – 171

17

Helix

172 – 175

4

Helix

179 – 190

12

Helix

192 – 198

7

Helix

210 – 219

10

Sequences

	Sequence		Length	Mass (Da)
	P10648 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 72F6FFC49C56F71D	FASTA	222	25,533
	10 20 30 40 50 60 MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI 70 80 90 100 110 120 DGMKLVQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIGQLV LCPPDQREAK 130 140 150 160 170 180 TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDVHL LELLLYVEEL DASLLTPFPL 190 200 210 220 LKAFKSRISS LPNVKKFLQP GSQRKPPLDA KQIEEARKVF KF

References

[1]	"Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole." Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N. J. Biol. Chem. 263:13324-13332(1988) [PubMed: 3417659] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide." Gu Y., Xiao B., Wargo H.L., Bucher M.H., Singh S.V., Ji X. Biochemistry 42:917-921(2003) [PubMed: 12549910] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND SUBSTRATE ANALOG, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03958 mRNA. Translation: AAA37749.1.

IPI

IPI00116055.

UniGene

Mm.422778.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ML6	X-ray	1.90	A/B	2-221	[»]

ProteinModelPortal

P10648.

SMR

P10648. Positions 3-222.

ModBase

Search...

Protein-protein interaction databases

STRING

P10648.

PTM databases

PhosphoSite

P10648.

Proteomic databases

PRIDE

P10648.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

MGI

MGI:95863. Gsta2.

Phylogenomic databases

eggNOG

roNOG10125.

HOGENOM

HBG443985.

HOVERGEN

HBG053749.

InParanoid

P10648.

OrthoDB

EOG479F80.

Gene expression databases

ArrayExpress

P10648.

Bgee

P10648.

CleanEx

MM_GSTA2.

Genevestigator

P10648.

GermOnline

ENSMUSG00000057933. Mus musculus.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR11571:SF4. GST_alpha. 1 hit.

Pfam

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

PRINTS

PR01266. GSTRNSFRASEA.

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

SOURCE

Search...

Entry information

Entry name

GSTA2_MOUSE

Accession

Primary (citable) accession number: P10648

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	September 21, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program