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Protein

Glutathione S-transferase alpha-5

Gene

Gsta5

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. Has substantial activity toward aflatoxin B1-8,9-epoxide.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91GlutathioneBy similarity
Binding sitei45 – 451GlutathioneBy 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. 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

Enzyme and pathway databases

ReactomeiREACT_251519. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase alpha-5 (EC:2.5.1.18)
Alternative name(s):
GST A5-5
Glutathione S-transferase Yc-2
Short name:
GST Yc2
Gene namesi
Name:Gsta5
Synonyms:Gstyc2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi2753. Gsta5.

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 – 221220Glutathione S-transferase alpha-5PRO_0000185796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41N6-succinyllysineBy similarity

Proteomic databases

PaxDbiP46418.
PRIDEiP46418.

Expressioni

Tissue specificityi

Liver, nasal mucosa and epididymis.

Developmental stagei

Liver from adult female rats contains about 10-fold greater levels of YC2 than is found in liver from adult male rats.

Inductioni

By ethoxyquin, oltipraz, butylated hydroxyanisole, and phenobarbitol.

Gene expression databases

ExpressionAtlasiP46418. baseline and differential.
GenevestigatoriP46418.

Interactioni

Subunit structurei

Heterodimer of YC1 and YC2.

Structurei

3D structure databases

ProteinModelPortaliP46418.
SMRiP46418. Positions 4-220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminalAdd
BLAST
Domaini85 – 207123GST 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.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
KOiK00799.
OMAiKDIPRLM.
OrthoDBiEOG79CZ0K.
PhylomeDBiP46418.
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.

P46418-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGKPVLHYF DGRGRMEPIR WLLAAAGVEF EENFLKTRDD LARLRSDGSL
60 70 80 90 100
MFEQVPMVEI DGMKLVQTKA ILNYIATKYN LYGKDMKERA LIDMYAEGVA
110 120 130 140 150
DLELMVLYYP YMPPGEKEAS LAKIKDKARN RYFPAYEKVL KSHGQDYLVG
160 170 180 190 200
NKLSRADVSL VELLYHVEEM DPGIVDNFPL LKALRTRVSN LPTVKKFLQP
210 220
GSQRKPFDDE KCVESAKKIF S
Length:221
Mass (Da):25,347
Last modified:January 23, 2007 - v2
Checksum:iEEDE9873765BFDB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78847 mRNA. Translation: CAA55404.1.
S72506 mRNA. Translation: AAP21065.1.
S82820 mRNA. Translation: AAB46796.1.
PIRiA54858.
RefSeqiNP_001009920.1. NM_001009920.2.
NP_001153211.1. NM_001159739.2.
UniGeneiRn.120929.

Genome annotation databases

EnsembliENSRNOT00000040950; ENSRNOP00000042770; ENSRNOG00000029711.
GeneIDi494500.
KEGGirno:494500.
UCSCiRGD:2753. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78847 mRNA. Translation: CAA55404.1.
S72506 mRNA. Translation: AAP21065.1.
S82820 mRNA. Translation: AAB46796.1.
PIRiA54858.
RefSeqiNP_001009920.1. NM_001009920.2.
NP_001153211.1. NM_001159739.2.
UniGeneiRn.120929.

3D structure databases

ProteinModelPortaliP46418.
SMRiP46418. Positions 4-220.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP46418.
PRIDEiP46418.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000040950; ENSRNOP00000042770; ENSRNOG00000029711.
GeneIDi494500.
KEGGirno:494500.
UCSCiRGD:2753. rat.

Organism-specific databases

CTDi2940.
RGDi2753. Gsta5.

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
KOiK00799.
OMAiKDIPRLM.
OrthoDBiEOG79CZ0K.
PhylomeDBiP46418.
TreeFamiTF105321.

Enzyme and pathway databases

ReactomeiREACT_251519. Glutathione conjugation.

Miscellaneous databases

NextBioi697639.
PROiP46418.

Gene expression databases

ExpressionAtlasiP46418. baseline and differential.
GenevestigatoriP46418.

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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of cDNAs from fetal rat liver encoding glutathione S-transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat liver resistant to the hepatocarcinogen aflatoxin B1."
    Hayes J.D., Nguyen T., Judah D.J., Petersson D.G., Neal G.E.
    J. Biol. Chem. 269:20707-20717(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344.
    Tissue: Liver.
  2. "Characterization of the rat glutathione S-transferase Yc2 subunit gene, GSTA5: identification of a putative antioxidant-responsive element in the 5'-flanking region of rat GSTA5 that may mediate chemoprotection against aflatoxin B1."
    Pulford D.J., Hayes J.D.
    Biochem. J. 318:75-84(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Ethoxyquin-induced resistance to aflatoxin B1 in the rat is associated with the expression of a novel alpha-class glutathione S-transferase subunit, Yc2, which possesses high catalytic activity for aflatoxin B1-8,9-epoxide."
    Hayes J.D., Judah D.J., McLellan L.I., Kerr L.A., Peacock S.D., Neal G.E.
    Biochem. J. 279:385-398(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Strain: Fischer 344.
    Tissue: Liver.

Entry informationi

Entry nameiGSTA5_RAT
AccessioniPrimary (citable) accession number: P46418
Secondary accession number(s): Q6LD91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.