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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 – 91Glutathione
Binding sitei45 – 451Glutathione
Binding sitei55 – 551Glutathione; via amide nitrogen and carbonyl oxygen

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-1
PRO_0000185792Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 222221Glutathione S-transferase alpha-1, N-terminally processed
PRO_0000423205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By 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

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00502.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.

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

MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL    50
MFDQVPMVEI DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL 100
DLTEMIMQLV ICPPDQKEAK TALAKDRTKN RYLPAFEKVL KSHGQDYLVG 150
NRLTRVDIHL LELLLYVEEF DASLLTSFPL LKAFKSRISS LPNVKKFLQP 200
GSQRKLPVDA KQIEEARKIF KF 222
Length:222
Mass (Da):25,607
Last modified:January 23, 2007 - v3
Checksum:iAE43A1BEBE8549CF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521R → K1 Publication
Sequence conflicti152 – 1521R → K1 Publication
Sequence conflicti208 – 2081V → M in AAA41283. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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: July 9, 2014
This is version 131 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

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