Reviewed, UniProtKB/Swiss-Prot P00502 (GSTA1_RAT)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase alpha-1
    EC=2.5.1.18
Alternative name(s):
    Glutathione S-transferase Ya-1
      Short name=GST Ya1
    Ligandin
    GST 1a-1a
    GST B
    GST 1-1
    GST A1-1

Gene names

Name:

Gsta1

Organism

Rattus norvegicus (Rat)

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	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.
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.
Sequence similarities	Belongs to the GST superfamily. Alpha family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	response to drug Non-traceable author statement. Source: RGD xenobiotic catabolic process Inferred from direct assay. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD nuclear outer membrane Inferred from direct assay. Source: RGD
Molecular function	drug binding Inferred from direct assay. Source: RGD glutathione binding Inferred from direct assay. Source: RGD glutathione transferase activity Inferred from direct assay. 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

Chain

2 – 222

221

Glutathione S-transferase alpha-1

PRO_0000185792

Regions

Domain

3 – 83

81

GST N-terminal

Domain

85 – 208

124

GST C-terminal

Experimental info

Sequence conflict

152

1

R → K Ref.1

Sequence conflict

152

1

R → K Ref.3

Sequence conflict

208

1

V → M in AAA41283. Ref.1

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Helix

16 – 25

10

Beta strand

31 – 35

5

Helix

38 – 46

9

Beta strand

57 – 60

4

Beta strand

63 – 67

5

Helix

68 – 79

12

Helix

86 – 109

24

Helix

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

211 – 219

9

Sequences

	Sequence		Length	Mass (Da)
	P00502-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AE43A1BEBE8549CF	FASTA	222	25,607
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone." Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C., Tu C.-P.D. J. Biol. Chem. 259:5536-5542(1984) [PubMed: 6201485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	"Rat glutathione S-transferase. Cloning of double-stranded cDNA and induction of its mRNA." Kalinyak J.E., Taylor J.M. J. Biol. Chem. 257:523-530(1982) [PubMed: 6273441] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-197.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

K01931 mRNA. Translation: AAA41283.1.
BC078706 mRNA. Translation: AAH78706.1.

IPI

IPI00231638.

PIR

A24735.
XURTG. A92479.

RefSeq

NP_058709.2.

UniGene

Rn.144550

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EV4	X-ray	2.20	A/C/D	2-219	[»]
1EV9	X-ray	2.20	A/C/D	2-221	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P00502.

Proteomic databases

PRIDE

P00502.

Genome annotation databases

Ensembl

ENSRNOT00000044944; ENSRNOP00000043510; ENSRNOG00000000201; Rattus norvegicus. [Genome view]

GeneID

24422.

KEGG

rno:24422.

UCSC

NM_017013. rat.

Organism-specific databases

CTD

24422.

RGD

2753. Gsta1.

Phylogenomic databases

HOVERGEN

P00502.

OMA

QSHGQDY.

Enzyme and pathway databases

BRENDA

2.5.1.18. 248.

Gene expression databases

ArrayExpress

P00502.

Genevestigator

P00502.

GermOnline

ENSRNOG00000000201. Rattus norvegicus.

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.
IPR012335. Thioredoxin_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.

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

603283.

Entry information

Entry name

GSTA1_RAT

Accession

Primary (citable) accession number: P00502
Secondary accession number(s): Q6AZ72

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)