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

P24473 (GSTK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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 kappa 1

EC=2.5.1.18
Alternative name(s):
GST 13-13
GST class-kappa
GSTK1-1
Short name=rGSTK1
Glutathione S-transferase subunit 13
Gene names
Name:Gstk1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Might confer protection against genotoxic and cytotoxic electrophiles in the mitochondrial compartment.

Catalytic activity

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

Subunit structure

Homodimer. Ref.3

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the GST superfamily. Kappa family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 226225Glutathione S-transferase kappa 1
PRO_0000185893

Regions

Region16 – 183Glutathione binding
Region200 – 2012Glutathione binding

Sites

Binding site531Glutathione
Binding site1831Glutathione; via amide nitrogen and carbonyl oxygen

Amino acid modifications

Modified residue361N6-succinyllysine By similarity
Modified residue491N6-succinyllysine By similarity
Modified residue681N6-acetyllysine; alternate By similarity
Modified residue681N6-succinyllysine; alternate By similarity
Modified residue741N6-acetyllysine; alternate By similarity
Modified residue741N6-succinyllysine; alternate By similarity
Modified residue851N6-acetyllysine By similarity
Modified residue931N6-acetyllysine; alternate By similarity
Modified residue931N6-succinyllysine; alternate By similarity
Modified residue1161N6-acetyllysine; alternate By similarity
Modified residue1161N6-succinyllysine; alternate By similarity
Modified residue1441N6-succinyllysine By similarity
Modified residue1581N6-acetyllysine; alternate By similarity
Modified residue1581N6-succinyllysine; alternate By similarity
Modified residue1651N6-acetyllysine By similarity
Modified residue1671N6-acetyllysine; alternate By similarity
Modified residue1671N6-succinyllysine; alternate By similarity
Modified residue1771N6-acetyllysine; alternate By similarity
Modified residue1771N6-succinyllysine; alternate By similarity
Modified residue1931N6-succinyllysine By similarity

Experimental info

Mutagenesis161S → A: Reduces catalytic activity about 30-fold. Reduces affinity for glutathione about 4-fold. Ref.3
Sequence conflict21G → C AA sequence Ref.2

Secondary structure

................................ 226
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24473 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D1E5514C5A65B3CC

FASTA22625,493
        10         20         30         40         50         60 
MGPAPRVLEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLKLR PALLAGIMKD SGNQPPAMVP 

        70         80         90        100        110        120 
HKGQYILKEI PLLKQLFQVP MSVPKDFFGE HVKKGTVNAM RFLTAVSMEQ PEMLEKVSRE 

       130        140        150        160        170        180 
LWMRIWSRDE DITESQNILS AAEKAGMATA QAQHLLNKIS TELVKSKLRE TTGAACKYGA 

       190        200        210        220 
FGLPTTVAHV DGKTYMLFGS DRMELLAYLL GEKWMGPVPP TLNARL 

« Hide

References

[1]"Glutathione S-transferase class Kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue."
Pemble S.E., Wardle A.F., Taylor J.B.
Biochem. J. 319:749-754(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"A novel glutathione transferase (13-13) isolated from the matrix of rat liver mitochondria having structural similarity to class theta enzymes."
Harris M.J., Meyer D.J., Coles B., Ketterer B.
Biochem. J. 278:137-141(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-34.
[3]"Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1."
Ladner J.E., Parsons J.F., Rife C.L., Gilliland G.L., Armstrong R.N.
Biochemistry 43:352-361(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, MUTAGENESIS OF SER-16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S83436 mRNA. Translation: AAB50831.1.
PIRS17164.
RefSeqNP_852036.1. NM_181371.2.
UniGeneRn.109452.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R4WX-ray2.50A/B/C/D1-226[»]
ProteinModelPortalP24473.
SMRP24473. Positions 2-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP24473. 1 interaction.
MINTMINT-4589693.
STRING10116.ENSRNOP00000022275.

Chemistry

DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP24473.

Proteomic databases

PaxDbP24473.
PRIDEP24473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022275; ENSRNOP00000022275; ENSRNOG00000016484.
GeneID297029.
KEGGrno:297029.
UCSCRGD:735188. rat.

Organism-specific databases

CTD373156.
RGD735188. Gstk1.

Phylogenomic databases

eggNOGCOG3917.
GeneTreeENSGT00440000033697.
HOGENOMHOG000219769.
HOVERGENHBG051852.
InParanoidP24473.
KOK13299.
OMAELWRRIW.
OrthoDBEOG793B9B.
PhylomeDBP24473.
TreeFamTF105323.

Gene expression databases

GenevestigatorP24473.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFPIRSF006386. HCCAis_GSTk. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP24473.
NextBio642014.
PROP24473.

Entry information

Entry nameGSTK1_RAT
AccessionPrimary (citable) accession number: P24473
Secondary accession number(s): O09034
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 110 of the entry and version 3 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