Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P20136 (GSTM2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

EC=2.5.1.18
Alternative name(s):
GST class-mu
GST-CL2
GSTM1-1
Gene names
Name:GSTM2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.5

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 220219Glutathione S-transferase 2
PRO_0000185838

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding
Region46 – 505Glutathione binding
Region59 – 602Glutathione binding
Region72 – 732Glutathione binding

Sites

Binding site1161Substrate By similarity

Experimental info

Mutagenesis1081R → E: Reduced affinity for glutathione. Ref.5
Mutagenesis1081R → L: Reduced catalytic activity. Ref.5
Mutagenesis2101W → F: Reduced affinity for glutathione. Ref.5
Mutagenesis2101W → H, I or P: Reduced catalytic activity. Ref.5

Secondary structure

..................................... 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20136 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: A7A7D843CE54E6F9

FASTA22025,893
        10         20         30         40         50         60 
MVVTLGYWDI RGLAHAIRLL LEYTETPYQE RRYKAGPAPD FDPSDWTNEK EKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGDVKL TQSNAILRYI ARKHNMCGET EVEKQRVDVL ENHLMDLRMA FARLCYSPDF 

       130        140        150        160        170        180 
EKLKPAYLEQ LPGKLRQLSR FLGSRSWFVG DKLTFVDFLA YDVLDQQRMF VPDCPELQGN 

       190        200        210        220 
LSQFLQRFEA LEKISAYMRS GRFMKAPIFW YTALWNNKKE 

« Hide

References

[1]"Nucleotide sequence of a class mu glutathione S-transferase from chicken liver."
Liu L.-F., Tam M.F.
Biochim. Biophys. Acta 1090:343-344(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: White leghorn.
Tissue: Liver.
[2]"Characterization of glutathione S-transferases from day-old chick livers."
Chang L.-H., Chuang L.-F., Tsai C.-P., Tu C.-P.D., Tam M.F.
Biochemistry 29:744-750(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-35.
Tissue: Liver.
[3]Liu L.-F.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 130.
[4]"The three-dimensional structure of an avian class-mu glutathione S-transferase, cGSTM1-1 at 1.94-A resolution."
Sun Y.-J., Kuan I.-C., Tam M.F., Hsiao C.-D.
J. Mol. Biol. 278:239-252(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
[5]"Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1."
Chern M.K., Wu T.C., Hsieh C.H., Chou C.C., Liu L.F., Kuan I.C., Yeh Y.H., Hsiao C.D., Tam M.F.
J. Mol. Biol. 300:1257-1269(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-108 AND TRP-210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58248 mRNA. Translation: CAA41202.1.
PIRS18464.
RefSeqNP_990421.1. NM_205090.1.
UniGeneGga.4223.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C72X-ray2.80A/B/C/D2-220[»]
1GSUX-ray1.94A/B2-220[»]
ProteinModelPortalP20136.
SMRP20136. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP20136.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395976.
KEGGgga:395976.

Organism-specific databases

CTD2946.

Phylogenomic databases

HOVERGENHBG106842.
KOK00799.
PhylomeDBP20136.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20136.
NextBio20816041.

Entry information

Entry nameGSTM2_CHICK
AccessionPrimary (citable) accession number: P20136
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references