[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; TISSUE=Liver; PubMed=1637297 [NCBI, ExPASy, EBI, Israel, Japan] Hayes J.D., Judah D.J., Neal G.E., Nguyen T.; "Molecular cloning and heterologous expression of a cDNA encoding a mouse glutathione S-transferase Yc subunit possessing high catalytic activity for aflatoxin B1-8,9-epoxide."; Biochem. J. 285:173-180(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; TISSUE=Liver; PubMed=1728405 [NCBI, ExPASy, EBI, Israel, Japan] Buetler T.M., Eaton D.L.; "Complementary DNA cloning, messenger RNA expression, and induction of alpha-class glutathione S-transferases in mouse tissues."; Cancer Res. 52:314-318(1992).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PROTEIN SEQUENCE OF 16-56; 63-73; 94-110 AND 112-142. TISSUE=Liver; PubMed=2049074 [NCBI, ExPASy, EBI, Israel, Japan] McLellan L.I., Kerr L.A., Cronshaw A.D., Hayes J.D.; "Regulation of mouse glutathione S-transferases by chemoprotectors. Molecular evidence for the existence of three distinct alpha-class glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver."; Biochem. J. 276:461-469(1991).
[5]	CHARACTERIZATION, MASS SPECTROMETRY, AND ACETYLATION AT ALA-2. STRAIN=CD-1; TISSUE=Liver; DOI=10.1021/tx00050a009; PubMed=8605288 [NCBI, ExPASy, EBI, Israel, Japan] Mitchell A.E., Morin D., Lame M.W., Jones A.D.; "Purification, mass spectrometric characterization, and covalent modification of murine glutathione S-transferases."; Chem. Res. Toxicol. 8:1054-1062(1995).

Comments

FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This GST has a high catalytic activity for aflatoxin B1-8,9 epoxide.
CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MASS SPECTROMETRY: Mass=25271.4; Mass_error=2; Method=Electrospray; Range=2-221; Source=PubMed:8605288;.
SIMILARITY: Belongs to the GST superfamily. Alpha family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X65021; CAA46155.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M73483; AAA37751.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009805; AAH09805.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S24322; S24322.

RefSeq

NP_001070821.1; -.
NP_034486.2; -.

UniGene

Mm.394593

3D structure databases

HSSP

P08263; 1K3O. [HSSP ENTRY / PDB]

SMR

P30115; 4-220.

ModBase

P30115.

Protein-protein interaction databases

IntAct

P30115; -.

PTM databases

PhosphoSite

P30115; -.

2D gel databases

SWISS-2DPAGE

P30115; -.

Organism-specific databases

MGI

MGI:95856; Gsta3.

Gene expression databases

ArrayExpress

P30115; -.

CleanEx

MM_GSTA3; -.

GermOnline

ENSMUSG00000025934; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from InterPro).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR010987; Glutathione-S-Trfase_C-like.
IPR003080; GST_alpha.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR11571:SF4; GST_alpha; 1.

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR01266; GSTRNSFRASEA.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P30115.

Genome annotation databases

Ensembl

ENSMUSG00000025934; Mus musculus. [Contig view]

GeneID

14859; -.

KEGG

mmu:14859; -.

Phylogenomic databases

HOGENOM

P30115; -.

HOVERGEN

P30115; -.

Other

NextBio

287095; -.

SOURCE

Gsta3; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 221`	`220`	`Glutathione S-transferase A3.`	`PRO_0000185790`
`DOMAIN`	`3 83`	`81`	`GST N-terminal.`
`DOMAIN`	`85 207`	`123`	`GST C-terminal.`
`MOD_RES`	`2 2`		`N-acetylalanine.`

Sequence information

Length: 221 AA [This is the length of the unprocessed precursor]

Molecular weight: 25361 Da [This is the MW of the unprocessed precursor]

CRC64: 6F7332488794081F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGKPVLHYF DGRGRMEPIR WLLAAAGVEF EEKFLKTRDD LARLRSDGSL MFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTKA ILNYIASKYN LYGKDMKERA IIDMYTEGVA DLEIMILYYP HMPPEEKEAS 

       130        140        150        160        170        180 
LAKIKEQTRN RYFPAFEKVL KSHGQDYLVG NRLSRADIAL VELLYHVEEL DPGVVDNFPL 

       190        200        210        220 
LKALRSRVSN LPTVKKFLQP GSQRKPFDDA KCVESAKKIF S

P30115 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools