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P26697 (GSTA3_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. 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 3

EC=2.5.1.18
Alternative name(s):
GST class-alpha
GST-CL3
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conjugation of GSH to a wide variety of electrophilic alkylating agents. Also involved in the metabolism of lipid hydroperoxides, prostaglandins and leukotriene A4 and in binding of non-substrate hydrophobic ligands such as bile acids, a number of drugs and thyroid hormones. This GST does not exhibit peroxidase activity.

Catalytic activity

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

Subunit structure

Homodimer or heterodimer (with a subunit from group CL-4).

Subcellular location

Cytoplasm.

Miscellaneous

The variations were found from AA sequencing and imply there are multiple forms of CL-3.

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
   Coding sequence diversityPolymorphism
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 229228Glutathione S-transferase 3
PRO_0000185800

Regions

Domain3 – 8381GST N-terminal
Domain85 – 207123GST C-terminal
Region54 – 552Glutathione binding
Region67 – 682Glutathione binding

Sites

Binding site91Glutathione

Amino acid modifications

Modified residue21Blocked amino end (Ala)

Natural variations

Natural variant451L → V.
Natural variant471S → A.
Natural variant491I → F.
Natural variant491I → V.
Natural variant521F → R.
Natural variant129 – 1302TS → AN.
Natural variant135 – 1362AY → VF.
Natural variant1551W → R.
Natural variant158 – 1592IH → VV.
Natural variant1631A → T.
Natural variant1661M → A.
Natural variant1681E → V.

Secondary structure

.................................... 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26697 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EA30D949034BD8DB

FASTA22926,326
        10         20         30         40         50         60 
MAAKPVLYYF NGRGKMESIR WLLAAAGVEF EEVFLETREQ YEKLLQSGIL MFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIAGKYN LYGKDLKERA LIDMYVGGTD DLMGFLLSFP FLSAEDKVKQ 

       130        140        150        160        170        180 
CAFVVEKATS RYFPAYEKVL KDHGQDFLVG NRLSWADIHL LEAILMVEEK KSDALSGFPL 

       190        200        210        220 
LQAFKKRISS IPTIKKFLAP GSKRKPISDD KYVETVRRVL RMYYDVKPH 

« Hide

References

[1]"Cloning and expression of a chick liver glutathione S-transferase CL 3 subunit with the use of a baculovirus expression system."
Chang L.-H., Fan J.-Y., Liu L.-F., Tsai S.-P., Tam M.F.
Biochem. J. 281:545-551(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: White leghorn.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M38219 mRNA. Translation: AAA62731.1.
PIRS19734.
RefSeqNP_990743.1. NM_205412.1.
UniGeneGga.788.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VF1X-ray1.77A1-229[»]
1VF2X-ray2.15A/B1-229[»]
1VF3X-ray2.15A/B1-229[»]
1VF4X-ray2.45A1-229[»]
ProteinModelPortalP26697.
SMRP26697. Positions 2-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000036177.

Proteomic databases

PaxDbP26697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396380.
KEGGgga:396380.

Phylogenomic databases

eggNOGNOG266414.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidP26697.
KOK00799.
PhylomeDBP26697.

Enzyme and pathway databases

SABIO-RKP26697.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26697.
NextBio20816422.

Entry information

Entry nameGSTA3_CHICK
AccessionPrimary (citable) accession number: P26697
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 98 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references