[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; PubMed=6201485 [NCBI, ExPASy, EBI, Israel, Japan] Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C., Tu C.-P.D.; "The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone."; J. Biol. Chem. 259:5536-5542(1984).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; 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).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 46-197. PubMed=6273441 [NCBI, ExPASy, EBI, Israel, Japan] Kalinyak J.E., Taylor J.M.; "Rat glutathione S-transferase. Cloning of double-stranded cDNA and induction of its mRNA."; J. Biol. Chem. 257:523-530(1982).

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: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: In addition to its enzymatic activity, the homodimer of Ya chains, called ligandin, binds various organic anions, xenobiotics, and azocarcinogen dyes.
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

K01931; AAA41283.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078706; AAH78706.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24735; A24735.
A92479; XURTG.

RefSeq

NP_058709.2; -.

UniGene

Rn.144550

3D structure databases

PDB

1EV4; X-ray; 2.20 A; A/C/D=1-222.	[ExPASy / RCSB / EBI]
1EV9; X-ray; 2.20 A; A/C/D=1-222.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1EV4; -.
1EV9; -.

ModBase

P00502.

Organism-specific databases

RGD

2753; Gsta1.

Gene expression databases

ArrayExpress

P00502; -.

GermOnline

ENSRNOG00000000201; Rattus norvegicus.

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

P00502.

Genome annotation databases

Ensembl

ENSRNOG00000000201; Rattus norvegicus. [Contig view]

GeneID

24422; -.

KEGG

rno:24422; -.

Phylogenomic databases

HOVERGEN

P00502; -.

Other

LinkHub

P00502; -.

NextBio

603283; -.

UniRef

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

Keywords

3D-structure; Cytoplasm; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 222`	`221`	`Glutathione S-transferase alpha-1.`	`PRO_0000185792`
`DOMAIN`	`3 83`	`81`	`GST N-terminal.`
`DOMAIN`	`85 208`	`124`	`GST C-terminal.`
`CONFLICT`	`152 152`		`R -> K (in Ref. 1 and 3).`
`CONFLICT`	`208 208`		`V -> M (in Ref. 1; AAA41283).`
`STRAND`	`6 12`	`7`
`HELIX`	`16 25`	`10`
`STRAND`	`31 35`	`5`
`HELIX`	`38 46`	`9`
`STRAND`	`57 60`	`4`
`STRAND`	`63 67`	`5`
`HELIX`	`68 79`	`12`
`HELIX`	`86 109`	`24`
`HELIX`	`114 116`	`3`
`HELIX`	`117 130`	`14`
`HELIX`	`132 143`	`12`
`STRAND`	`146 149`	`4`
`HELIX`	`155 171`	`17`
`HELIX`	`172 175`	`4`
`HELIX`	`179 190`	`12`
`HELIX`	`192 198`	`7`
`HELIX`	`211 219`	`9`

Sequence information

Length: 222 AA [This is the length of the unprocessed precursor]

Molecular weight: 25607 Da [This is the MW of the unprocessed precursor]

CRC64: AE43A1BEBE8549CF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL MFDQVPMVEI 

        70         80         90        100        110        120 
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIMQLV ICPPDQKEAK 

       130        140        150        160        170        180 
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LELLLYVEEF DASLLTSFPL 

       190        200        210        220 
LKAFKSRISS LPNVKKFLQP GSQRKLPVDA KQIEEARKIF KF

P00502 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