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

P80894 (GSTA1_ANTST) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 62. 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

EC=2.5.1.18
Alternative name(s):
GST class-alpha

Cleaved into the following chain:

  1. Glutathione S-transferase, N-terminally processed
OrganismAntechinus stuartii (Brown marsupial mouse)
Taxonomic identifier9283 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDasyuromorphiaDasyuridaeAntechinus

Protein attributes

Sequence length221 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.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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 termDirect protein sequencing
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

Chain1 – 221221Glutathione S-transferase
PRO_0000185803
Initiator methionine11Removed; alternate By similarity
Chain2 – 221220Glutathione S-transferase, N-terminally processed
PRO_0000421784

Regions

Domain3 – 8280GST N-terminal
Domain84 – 208125GST C-terminal
Region53 – 542Glutathione binding By similarity
Region66 – 672Glutathione binding By similarity

Sites

Binding site91Glutathione By similarity

Amino acid modifications

Modified residue11N-acetylmethionine

Sequences

Sequence LengthMass (Da)Tools
P80894 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 03B185BCC44B570F

FASTA22125,534
        10         20         30         40         50         60 
MAGEQNIKYF NIKGRMEAIR WLLAVAGVEF EEKFFETKEQ LQKLKETVLL FQQVPMVEID 

        70         80         90        100        110        120 
GMKLVQTRAI LHYIAEKYNL LGKDMKEHAQ IIMYSEGTMD LMELIMIYPF LKGEEKKQRL 

       130        140        150        160        170        180 
VEIANKAKGR YFPAFENVLK THGQNFLVGN QLSMADVQLF EAILMVEEKV PDALSGFPLL 

       190        200        210        220 
QAFKTRISNI PTVKTFLAPG SKRKPVPDAK YVEDIIKIFY F 

« Hide

References

[1]"Characterization of a marsupial glutathione transferase, a class Alpha enzyme from Brown Antechinus (Antechinus stuartii)."
Bolton R.M., Curstedt L., Cederlund E., Hjelmqvist L., Mannervik B., Ahokas J.T., Joernvall H.
FEBS Lett. 406:216-219(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases

ProteinModelPortalP80894.
SMRP80894. Positions 2-219.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG053749.

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]
PANTHERPTHR11571:SF4. PTHR11571:SF4. 1 hit.
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...

Entry information

Entry nameGSTA1_ANTST
AccessionPrimary (citable) accession number: P80894
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 16, 2013
This is version 62 of the entry and version 1 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