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P24473

- GSTK1_RAT

UniProt

P24473 - GSTK1_RAT

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Protein

Glutathione S-transferase kappa 1

Gene

Gstk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Glutathione1 Publication
Binding sitei183 – 1831Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

GO - Molecular functioni

  1. glutathione peroxidase activity Source: Ensembl
  2. glutathione transferase activity Source: UniProtKB-EC
  3. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. epithelial cell differentiation Source: Ensembl
  2. glutathione metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Gstk1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi735188. Gstk1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: HGNC
  4. peroxisome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161S → A: Reduces catalytic activity about 30-fold. Reduces affinity for glutathione about 4-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 226225Glutathione S-transferase kappa 1PRO_0000185893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-succinyllysineBy similarity
Modified residuei49 – 491N6-succinyllysineBy similarity
Modified residuei68 – 681N6-acetyllysine; alternateBy similarity
Modified residuei68 – 681N6-succinyllysine; alternateBy similarity
Modified residuei74 – 741N6-acetyllysine; alternateBy similarity
Modified residuei74 – 741N6-succinyllysine; alternateBy similarity
Modified residuei85 – 851N6-acetyllysineBy similarity
Modified residuei93 – 931N6-acetyllysine; alternateBy similarity
Modified residuei93 – 931N6-succinyllysine; alternateBy similarity
Modified residuei116 – 1161N6-acetyllysine; alternateBy similarity
Modified residuei116 – 1161N6-succinyllysine; alternateBy similarity
Modified residuei144 – 1441N6-succinyllysineBy similarity
Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
Modified residuei165 – 1651N6-acetyllysineBy similarity
Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
Modified residuei177 – 1771N6-acetyllysine; alternateBy similarity
Modified residuei177 – 1771N6-succinyllysine; alternateBy similarity
Modified residuei193 – 1931N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP24473.
PRIDEiP24473.

PTM databases

PhosphoSiteiP24473.

Expressioni

Gene expression databases

ExpressionAtlasiP24473. baseline.
GenevestigatoriP24473.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP24473. 1 interaction.
MINTiMINT-4589693.
STRINGi10116.ENSRNOP00000022275.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Helixi17 – 2913Combined sources
Turni30 – 323Combined sources
Beta strandi33 – 419Combined sources
Helixi44 – 507Combined sources
Helixi60 – 7718Combined sources
Turni87 – 893Combined sources
Helixi90 – 945Combined sources
Helixi97 – 10913Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 12613Combined sources
Helixi135 – 14410Combined sources
Helixi149 – 1568Combined sources
Turni157 – 1604Combined sources
Helixi162 – 17716Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi193 – 1997Combined sources
Helixi203 – 2108Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R4WX-ray2.50A/B/C/D1-226[»]
ProteinModelPortaliP24473.
SMRiP24473. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24473.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 183Glutathione binding
Regioni200 – 2012Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Kappa family.Curated

Phylogenomic databases

eggNOGiCOG3917.
GeneTreeiENSGT00440000033697.
HOGENOMiHOG000219769.
HOVERGENiHBG051852.
InParanoidiP24473.
KOiK13299.
OMAiELWRRIW.
OrthoDBiEOG793B9B.
PhylomeDBiP24473.
TreeFamiTF105323.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFiPIRSF006386. HCCAis_GSTk. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24473-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGPAPRVLEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLKLR PALLAGIMKD
60 70 80 90 100
SGNQPPAMVP HKGQYILKEI PLLKQLFQVP MSVPKDFFGE HVKKGTVNAM
110 120 130 140 150
RFLTAVSMEQ PEMLEKVSRE LWMRIWSRDE DITESQNILS AAEKAGMATA
160 170 180 190 200
QAQHLLNKIS TELVKSKLRE TTGAACKYGA FGLPTTVAHV DGKTYMLFGS
210 220
DRMELLAYLL GEKWMGPVPP TLNARL
Length:226
Mass (Da):25,493
Last modified:January 23, 2007 - v3
Checksum:iD1E5514C5A65B3CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21G → C AA sequence (PubMed:1883325)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83436 mRNA. Translation: AAB50831.1.
PIRiS17164.
RefSeqiNP_852036.1. NM_181371.2.
UniGeneiRn.109452.

Genome annotation databases

EnsembliENSRNOT00000022275; ENSRNOP00000022275; ENSRNOG00000016484.
GeneIDi297029.
KEGGirno:297029.
UCSCiRGD:735188. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83436 mRNA. Translation: AAB50831.1 .
PIRi S17164.
RefSeqi NP_852036.1. NM_181371.2.
UniGenei Rn.109452.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1R4W X-ray 2.50 A/B/C/D 1-226 [» ]
ProteinModelPortali P24473.
SMRi P24473. Positions 2-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P24473. 1 interaction.
MINTi MINT-4589693.
STRINGi 10116.ENSRNOP00000022275.

PTM databases

PhosphoSitei P24473.

Proteomic databases

PaxDbi P24473.
PRIDEi P24473.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000022275 ; ENSRNOP00000022275 ; ENSRNOG00000016484 .
GeneIDi 297029.
KEGGi rno:297029.
UCSCi RGD:735188. rat.

Organism-specific databases

CTDi 373156.
RGDi 735188. Gstk1.

Phylogenomic databases

eggNOGi COG3917.
GeneTreei ENSGT00440000033697.
HOGENOMi HOG000219769.
HOVERGENi HBG051852.
InParanoidi P24473.
KOi K13299.
OMAi ELWRRIW.
OrthoDBi EOG793B9B.
PhylomeDBi P24473.
TreeFami TF105323.

Miscellaneous databases

EvolutionaryTracei P24473.
NextBioi 642014.
PROi P24473.

Gene expression databases

ExpressionAtlasi P24473. baseline.
Genevestigatori P24473.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR001853. DSBA-like_thioredoxin_dom.
IPR014440. HCCAis_GSTk.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF01323. DSBA. 1 hit.
[Graphical view ]
PIRSFi PIRSF006386. HCCAis_GSTk. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGSTK1_RAT
AccessioniPrimary (citable) accession number: P24473
Secondary accession number(s): O09034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3