Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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.

Miscellaneous

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

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: CAFA
  • glutathione transferase activity Source: CAFA
  • protein homodimerization activity Source: CAFA

GO - Biological processi

  • aging Source: RGD
  • response to drug Source: RGD
  • response to nutrient levels Source: RGD
  • xenobiotic catabolic process Source: CAFA

Keywordsi

Molecular functionTransferase

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
Gene namesi
Name:Gsta1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2753. Gsta1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

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

GO - Molecular functioni

  • protein homodimerization activity Source: CAFA

Protein-protein interaction databases

MINTiMINT-4564141.

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[»]
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

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
PfamiView protein in Pfam
PF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.

Sequencei

Sequence statusi: Complete.

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.

Similar proteinsi

Entry informationi

Entry nameiGSTA1_RAT
AccessioniPrimary (citable) accession number: P00502
Secondary accession number(s): Q6AZ72
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 151 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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