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P46088 (GST_NOTSL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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

EC=2.5.1.18
Alternative name(s):
GST class-sigma
OrganismNototodarus sloanii (Wellington flying squid) (Ommastrephes sloanei)
Taxonomic identifier215440 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaOegopsinaOmmastrephidaeNototodarus

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High activity toward 1-chloro-2,4-dinitrobenzene. Not very efficient at catalyzing the addition of GSH to enones and epoxides. Ref.2

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.2

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm.

Tissue specificity

More abundant in the digestive gland than in the testis, mantle, or lens.

Sequence similarities

Belongs to the GST superfamily. Sigma 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
Direct protein sequencing
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

Chain1 – 203203Glutathione S-transferase
PRO_0000185920

Regions

Domain2 – 7978GST N-terminal
Domain81 – 203123GST C-terminal
Region49 – 513Glutathione binding
Region63 – 642Glutathione binding

Sites

Binding site81Glutathione
Binding site391Glutathione
Binding site431Glutathione

Natural variations

Natural variant1241C → Y.

Experimental info

Mutagenesis1071F → Y: Improves action on epones and epoxides.

Secondary structure

................................... 203
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46088 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F46F56682F1C9591

FASTA20322,919
        10         20         30         40         50         60 
MPKYTLHYFP LMGRAELCRF VLAAHGEEFT DRVVEMADWP NLKATMYSNA MPVLDIDGTK 

        70         80         90        100        110        120 
MSQSMCIARH LAREFGLDGK TSLEKYRVDE ITETLQDIFN DVVKIKFAPE AAKEAVQQNY 

       130        140        150        160        170        180 
EKSCKRLAPF LEGLLVSNGG GDGFFVGNSM TLADLHCYVA LEVPLKHTPE LLKDCPKIVA 

       190        200 
LRKRVAECPK IAAYLKKRPV RDF 

« Hide

References

[1]"Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods."
Tomarev S.I., Zinovieva R.D., Guo K., Piatigorsky J.
J. Biol. Chem. 268:4534-4542(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-60 AND 86-104.
Strain: Pacificus.
Tissue: Digestive gland.
[2]"Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods."
Ji X., von Rosenvinge E.C., Johnson W.W., Tomarev S.I., Piatigorsky J., Armstrong R.N., Gilliland G.L.
Biochemistry 34:5317-5328(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
[3]"Location of a potential transport binding site in a sigma class glutathione transferase by X-ray crystallography."
Ji X., von Rosenvinge E.C., Johnson W.W., Armstrong R.N., Gilliland G.L.
Proc. Natl. Acad. Sci. U.S.A. 93:8208-8213(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02054 expand/collapse EMBL AC list , L02053, L02052, L02051, L02050 Genomic DNA. Translation: AAA92066.1.
PIRA45463.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GSQX-ray2.40A2-203[»]
2GSQX-ray2.20A2-203[»]
ProteinModelPortalP46088.
SMRP46088. Positions 2-203.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR003083. S-crystallin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01269. SCRYSTALLIN.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46088.

Entry information

Entry nameGST_NOTSL
AccessionPrimary (citable) accession number: P46088
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references