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P14942 (GSTA4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase alpha-4

EC=2.5.1.18
Alternative name(s):
GST 8-8
GST A4-4
GST K
Glutathione S-transferase Yk
Short name=GST Yk
Gene names
Name:Gsta4
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Alpha family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processxenobiotic metabolic process

Inferred from direct assay. Source: RGD

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondrug binding

Inferred from direct assay. Source: RGD

glutathione binding

Inferred from direct assay. Source: RGD

glutathione transferase activity

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Glutathione S-transferase alpha-4
PRO_0000185795

Regions

Domain3 – 8381GST N-terminal
Domain85 – 208124GST C-terminal
Region54 – 552Glutathione binding By similarity
Region67 – 682Glutathione binding By similarity

Sites

Binding site91Glutathione By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1

Experimental info

Sequence conflict181S → V AA sequence Ref.1
Sequence conflict481G → D AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P14942 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: E0E42852DBA37E58

FASTA22225,510
        10         20         30         40         50         60 
MEVKPKLYYF QGRGRMESIR WLLATAGVEF EEEFLETREQ YEKLQKDGCL LFGQVPLVEI 

        70         80         90        100        110        120 
DGMLLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ DLMMMIIGAP FKAPQEKEES 

       130        140        150        160        170        180 
LALAVKRAKN RYFPVFEKIL KDHGEAFLVG NQLSWADIQL LEAILMVEEV SAPVLSDFPL 

       190        200        210        220 
LQAFKTRISN IPTIKKFLQP GSQRKPPPDG HYVDVVRTVL KF 

« Hide

References

[1]"Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases."
Alin P., Jensson H., Cederlund E., Joernvall H., Mannervik B.
Biochem. J. 261:531-539(1989) [PubMed: 2775231] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Cloning and heterologous expression of cDNA encoding class alpha rat glutathione transferase 8-8, an enzyme with high catalytic activity towards genotoxic alpha,beta-unsaturated carbonyl compounds."
Stenberg G., Ridderstroem M., Engstroem A., Pemble S.E., Mannervik B.
Biochem. J. 284:313-319(1992) [PubMed: 1599415] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Hepatoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62660 mRNA. Translation: CAB46530.1.
IPIIPI00210542.
PIRXURT8C. S23433.
RefSeqNP_001100310.1. NM_001106840.1.
UniGeneRn.57528.

3D structure databases

ProteinModelPortalP14942.
SMRP14942. Positions 4-222.
ModBaseSearch...

Protein-protein interaction databases

STRINGP14942.

Proteomic databases

PRIDEP14942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012348; ENSRNOP00000012346; ENSRNOG00000030449.
GeneID300850.
KEGGrno:300850.
NMPDRfig|10116.3.peg.28966.

Organism-specific databases

CTD2941.
RGD1309970. Gsta4.

Phylogenomic databases

eggNOGroNOG04634.
GeneTreeENSGT00550000074445.
HOVERGENHBG053749.
InParanoidP14942.
OMAMYVEGIS.
OrthoDBEOG4N5VXR.
PhylomeDBP14942.

Gene expression databases

ArrayExpressP14942.
GenevestigatorP14942.
GermOnlineENSRNOG00000030449. Rattus norvegicus.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK00799.
PANTHERPTHR11571:SF4. GST_alpha. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio647640.

Entry information

Entry nameGSTA4_RAT
AccessionPrimary (citable) accession number: P14942
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 1, 1992
Last modified: November 16, 2011
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families