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P00502

- GSTA1_RAT

UniProt

P00502 - GSTA1_RAT

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Protein

Glutathione S-transferase alpha-1

Gene

Gsta1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Glutathione1 Publication
Binding sitei45 – 451Glutathione1 Publication
Binding sitei55 – 551Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

GO - Molecular functioni

  1. drug binding Source: RGD
  2. glutathione binding Source: RGD
  3. glutathione transferase activity Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. response to drug Source: RGD
  3. response to nutrient levels Source: RGD
  4. 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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2753. Gsta1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. nuclear outer membrane Source: RGD
  3. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Glutathione S-transferase alpha-1PRO_0000185792Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 222221Glutathione S-transferase alpha-1, N-terminally processedPRO_0000423205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00502.
PRIDEiP00502.

PTM databases

PhosphoSiteiP00502.

Expressioni

Gene expression databases

GenevestigatoriP00502.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

MINTiMINT-4564141.
STRINGi10116.ENSRNOP00000043510.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Helixi16 – 2510Combined sources
Beta strandi31 – 355Combined sources
Helixi38 – 469Combined sources
Beta strandi57 – 604Combined sources
Beta strandi63 – 675Combined sources
Helixi68 – 7912Combined sources
Helixi86 – 10924Combined sources
Helixi114 – 1163Combined sources
Helixi117 – 13014Combined sources
Helixi132 – 14312Combined sources
Beta strandi146 – 1494Combined sources
Helixi155 – 17117Combined sources
Helixi172 – 1754Combined sources
Helixi179 – 19012Combined sources
Helixi192 – 1987Combined sources
Helixi211 – 2199Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EV4X-ray2.20A/C/D2-222[»]
1EV9X-ray2.20A/C/D2-222[»]
DisProtiDP00731.
ProteinModelPortaliP00502.
SMRiP00502. Positions 2-221.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00502.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminalAdd
BLAST
Domaini85 – 208124GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 682Glutathione binding

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

eggNOGiNOG266414.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP00502.
KOiK00799.
OrthoDBiEOG79CZ0K.
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]
PfamiPF00043. GST_C. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521R → K(PubMed:6201485)Curated
Sequence conflicti152 – 1521R → K(PubMed:6273441)Curated
Sequence conflicti208 – 2081V → M in AAA41283. (PubMed:6201485)Curated

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.

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 .
PIRi A24735.
A92479. XURTG.
RefSeqi NP_058709.2. NM_017013.4.
UniGenei Rn.144550.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EV4 X-ray 2.20 A/C/D 2-222 [» ]
1EV9 X-ray 2.20 A/C/D 2-222 [» ]
DisProti DP00731.
ProteinModelPortali P00502.
SMRi P00502. Positions 2-221.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4564141.
STRINGi 10116.ENSRNOP00000043510.

Chemistry

ChEMBLi CHEMBL2390.

PTM databases

PhosphoSitei P00502.

Proteomic databases

PaxDbi P00502.
PRIDEi P00502.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24422.
KEGGi rno:24422.

Organism-specific databases

CTDi 2939.
RGDi 2753. Gsta1.

Phylogenomic databases

eggNOGi NOG266414.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
InParanoidi P00502.
KOi K00799.
OrthoDBi EOG79CZ0K.
PhylomeDBi P00502.
TreeFami TF105321.

Miscellaneous databases

EvolutionaryTracei P00502.
NextBioi 603283.

Gene expression databases

Genevestigatori P00502.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01266. GSTRNSFRASEA.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-197.
  4. "Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y."
    Adman E.T., Le Trong I., Stenkamp R.E., Nieslanik B.S., Dietze E.C., Tai G., Ibarra C., Atkins W.M.
    Proteins 42:192-200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, SUBUNIT.

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 26, 2014
This is version 133 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

External Data

Dasty 3