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Protein

Glutathione S-transferase alpha-1

Gene

Gsta1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei9Glutathione1 Publication1
Binding sitei45Glutathione1 Publication1

GO - Molecular functioni

  • drug binding Source: RGD
  • glutathione binding Source: RGD
  • glutathione transferase activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • response to drug Source: RGD
  • response to nutrient levels Source: RGD
  • xenobiotic catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase alpha-1 (EC:2.5.1.18)
Alternative name(s):
GST 1-1
GST 1a-1a
GST A1-1
GST B
Glutathione S-transferase Ya-1
Short name:
GST Ya1
Ligandin
Cleaved into the following chain:
Gene namesi
Name:Gsta1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2753. Gsta1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • nuclear outer membrane Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2390.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001857921 – 222Glutathione S-transferase alpha-1Add BLAST222
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004232052 – 222Glutathione S-transferase alpha-1, N-terminally processedAdd BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei4N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00502.
PRIDEiP00502.

PTM databases

iPTMnetiP00502.
PhosphoSitePlusiP00502.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

MINTiMINT-4564141.
STRINGi10116.ENSRNOP00000043510.

Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Helixi16 – 25Combined sources10
Beta strandi31 – 35Combined sources5
Helixi38 – 46Combined sources9
Beta strandi57 – 60Combined sources4
Beta strandi63 – 67Combined sources5
Helixi68 – 79Combined sources12
Helixi86 – 109Combined sources24
Helixi114 – 116Combined sources3
Helixi117 – 130Combined sources14
Helixi132 – 143Combined sources12
Beta strandi146 – 149Combined sources4
Helixi155 – 171Combined sources17
Helixi172 – 175Combined sources4
Helixi179 – 190Combined sources12
Helixi192 – 198Combined sources7
Helixi211 – 219Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EV4X-ray2.20A/C/D2-222[»]
1EV9X-ray2.20A/C/D2-222[»]
DisProtiDP00731.
ProteinModelPortaliP00502.
SMRiP00502.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00502.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 83GST N-terminalAdd BLAST81
Domaini85 – 208GST C-terminalAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 55Glutathione binding1 Publication2
Regioni67 – 68Glutathione binding1 Publication2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP00502.
KOiK00799.
PhylomeDBiP00502.
TreeFamiTF105321.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00502-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL
60 70 80 90 100
MFDQVPMVEI DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL
110 120 130 140 150
DLTEMIMQLV ICPPDQKEAK TALAKDRTKN RYLPAFEKVL KSHGQDYLVG
160 170 180 190 200
NRLTRVDIHL LELLLYVEEF DASLLTSFPL LKAFKSRISS LPNVKKFLQP
210 220
GSQRKLPVDA KQIEEARKIF KF
Length:222
Mass (Da):25,607
Last modified:January 23, 2007 - v3
Checksum:iAE43A1BEBE8549CF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti152R → K (PubMed:6201485).Curated1
Sequence conflicti152R → K (PubMed:6273441).Curated1
Sequence conflicti208V → M in AAA41283 (PubMed:6201485).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01931 mRNA. Translation: AAA41283.1.
BC078706 mRNA. Translation: AAH78706.1.
PIRiA24735.
A92479. XURTG.
RefSeqiNP_058709.2. NM_017013.4.
UniGeneiRn.144550.
Rn.40574.

Genome annotation databases

GeneIDi24422.
KEGGirno:24422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01931 mRNA. Translation: AAA41283.1.
BC078706 mRNA. Translation: AAH78706.1.
PIRiA24735.
A92479. XURTG.
RefSeqiNP_058709.2. NM_017013.4.
UniGeneiRn.144550.
Rn.40574.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EV4X-ray2.20A/C/D2-222[»]
1EV9X-ray2.20A/C/D2-222[»]
DisProtiDP00731.
ProteinModelPortaliP00502.
SMRiP00502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564141.
STRINGi10116.ENSRNOP00000043510.

Chemistry databases

ChEMBLiCHEMBL2390.

PTM databases

iPTMnetiP00502.
PhosphoSitePlusiP00502.

Proteomic databases

PaxDbiP00502.
PRIDEiP00502.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24422.
KEGGirno:24422.

Organism-specific databases

CTDi2939.
RGDi2753. Gsta1.

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP00502.
KOiK00799.
PhylomeDBiP00502.
TreeFamiTF105321.

Miscellaneous databases

EvolutionaryTraceiP00502.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSTA1_RAT
AccessioniPrimary (citable) accession number: P00502
Secondary accession number(s): Q6AZ72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In addition to its enzymatic activity, the homodimer of Ya chains, called ligandin, binds various organic anions, xenobiotics, and azocarcinogen dyes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.