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P04903

- GSTA2_RAT

UniProt

P04903 - GSTA2_RAT

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Protein

Glutathione S-transferase alpha-2

Gene

Gsta2

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

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91GlutathioneBy similarity

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. xenobiotic catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase alpha-2 (EC:2.5.1.18)
Alternative name(s):
GST 1b-1b
GST A2-2
Glutathione S-transferase Ya-2
Short name:
GST Ya2
Gene namesi
Name:Gsta2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2754. Gsta2.

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
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 222221Glutathione S-transferase alpha-2PRO_0000185793Add
BLAST

Proteomic databases

PaxDbiP04903.
PRIDEiP04903.

Expressioni

Gene expression databases

GenevestigatoriP04903.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP04903.
SMRiP04903. Positions 2-221.
ModBaseiSearch...
MobiDBiSearch...

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
Regioni54 – 552Glutathione bindingBy similarity
Regioni67 – 682Glutathione bindingBy similarity

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.
InParanoidiP04903.
KOiK00799.
PhylomeDBiP04903.

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.

P04903-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGKPVLHYF NARGRMECIR WLLAAAGVEF EEKLIQSPED LEKLKKDGNL
60 70 80 90 100
MFDQVPMVEI DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYSEGIL
110 120 130 140 150
DLTEMIIQLV ICPPDQREAK TALAKDRTKN RYLPAFEKVL KSHGQDYLVG
160 170 180 190 200
NRLTRVDIHL LELLLYVEEF DASLLTSFPL LKAFKSRISS LPNVKKFLQP
210 220
GSQRKPAMDA KQIEEARKVF KF
Length:222
Mass (Da):25,559
Last modified:January 23, 2007 - v2
Checksum:iAA342417E9857A9F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K00136 mRNA. Translation: AAA41282.1.
M25891 mRNA. Translation: AAA41290.1.
M14991
, M14986, M14987, M14988, M14989, M14990 Genomic DNA. Translation: AAA41295.1.
X00520 mRNA. Translation: CAA25203.1.
M27446 mRNA. Translation: AAA41291.1.
PIRiA24735.
A26653.
A92479. XURTG.
RefSeqiNP_001010921.1. NM_001010921.1.
UniGeneiRn.40574.

Genome annotation databases

GeneIDi494499.
KEGGirno:494499.
UCSCiRGD:2754. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K00136 mRNA. Translation: AAA41282.1 .
M25891 mRNA. Translation: AAA41290.1 .
M14991
, M14986 , M14987 , M14988 , M14989 , M14990 Genomic DNA. Translation: AAA41295.1 .
X00520 mRNA. Translation: CAA25203.1 .
M27446 mRNA. Translation: AAA41291.1 .
PIRi A24735.
A26653.
A92479. XURTG.
RefSeqi NP_001010921.1. NM_001010921.1.
UniGenei Rn.40574.

3D structure databases

ProteinModelPortali P04903.
SMRi P04903. Positions 2-221.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P04903.
PRIDEi P04903.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 494499.
KEGGi rno:494499.
UCSCi RGD:2754. rat.

Organism-specific databases

CTDi 221357.
RGDi 2754. Gsta2.

Phylogenomic databases

eggNOGi NOG266414.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
InParanoidi P04903.
KOi K00799.
PhylomeDBi P04903.

Miscellaneous databases

NextBioi 697636.

Gene expression databases

Genevestigatori P04903.

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

  1. "Rat liver glutathione S-transferases. Complete nucleotide sequence of a glutathione S-transferase mRNA and the regulation of the Ya, Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital."
    Pickett C.B., Telakowski-Hopkins C.A., Ding G.J.-F., Argenbright L., Lu A.Y.H.
    J. Biol. Chem. 259:5182-5188(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Expression and sequence analysis of rat liver glutathione S-transferase genes."
    Pickett C.B., Telakowsi-Hopkins C.A., Ding G.J.-F., Ding V.D.-H.
    Adv. Exp. Med. Biol. 197:185-193(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structural analysis of a rat liver glutathione S-transferase Ya gene."
    Telakowski-Hopkins C.A., Rothkopf G.S., Pickett C.B.
    Proc. Natl. Acad. Sci. U.S.A. 83:9393-9397(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Construction and characterization of a plasmid containing complementary DNA to mRNA encoding the N-terminal amino acid sequence of the rat glutathione transferase Ya subunit."
    Taylor J.B., Craig R.K., Beale D., Ketterer B.
    Biochem. J. 219:223-231(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-129.
  5. "Expression of a cDNA encoding a rat liver glutathione S-transferase Ya subunit in Escherichia coli."
    Wang R.W., Pickett C.B., Lu A.Y.H.
    Arch. Biochem. Biophys. 269:536-543(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
    Tissue: Liver.
  6. "Cloning and sequence analysis of a cDNA plasmid for one of the rat liver glutathione S-transferase subunits."
    Tu C.-P.D., Weiss M.J., Karakawa W.W., Reddy C.C.
    Nucleic Acids Res. 10:5407-5419(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-222.

Entry informationi

Entry nameiGSTA2_RAT
AccessioniPrimary (citable) accession number: P04903
Secondary accession number(s): Q63715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 111 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3