GSTK1_RAT
ID GSTK1_RAT Reviewed; 226 AA.
AC P24473; O09034;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Glutathione S-transferase kappa 1;
DE EC=2.5.1.18 {ECO:0000269|PubMed:14717589};
DE AltName: Full=GST 13-13;
DE AltName: Full=GST class-kappa;
DE AltName: Full=GSTK1-1;
DE Short=rGSTK1;
DE AltName: Full=Glutathione S-transferase subunit 13;
GN Name=Gstk1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8920976; DOI=10.1042/bj3190749;
RA Pemble S.E., Wardle A.F., Taylor J.B.;
RT "Glutathione S-transferase class Kappa: characterization by the cloning of
RT rat mitochondrial GST and identification of a human homologue.";
RL Biochem. J. 319:749-754(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-34, AND SUBCELLULAR LOCATION.
RX PubMed=1883325; DOI=10.1042/bj2780137;
RA Harris M.J., Meyer D.J., Coles B., Ketterer B.;
RT "A novel glutathione transferase (13-13) isolated from the matrix of rat
RT liver mitochondria having structural similarity to class theta enzymes.";
RL Biochem. J. 278:137-141(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT,
RP AND MUTAGENESIS OF SER-16.
RX PubMed=14717589; DOI=10.1021/bi035832z;
RA Ladner J.E., Parsons J.F., Rife C.L., Gilliland G.L., Armstrong R.N.;
RT "Parallel evolutionary pathways for glutathione transferases: structure and
RT mechanism of the mitochondrial class kappa enzyme rGSTK1-1.";
RL Biochemistry 43:352-361(2004).
CC -!- FUNCTION: Glutathione S-transferase that catalyzes the conjugation of
CC glutathione to exogenous and endogenous compounds.
CC {ECO:0000269|PubMed:14717589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:14717589};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14717589}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:1883325}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC {ECO:0000305}.
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DR EMBL; S83436; AAB50831.1; -; mRNA.
DR PIR; S17164; S17164.
DR RefSeq; NP_852036.1; NM_181371.2.
DR PDB; 1R4W; X-ray; 2.50 A; A/B/C/D=1-226.
DR PDBsum; 1R4W; -.
DR AlphaFoldDB; P24473; -.
DR SMR; P24473; -.
DR IntAct; P24473; 1.
DR MINT; P24473; -.
DR STRING; 10116.ENSRNOP00000022275; -.
DR CarbonylDB; P24473; -.
DR iPTMnet; P24473; -.
DR PhosphoSitePlus; P24473; -.
DR jPOST; P24473; -.
DR PaxDb; P24473; -.
DR PRIDE; P24473; -.
DR Ensembl; ENSRNOT00000022275; ENSRNOP00000022275; ENSRNOG00000016484.
DR GeneID; 297029; -.
DR KEGG; rno:297029; -.
DR UCSC; RGD:735188; rat.
DR CTD; 373156; -.
DR RGD; 735188; Gstk1.
DR eggNOG; ENOG502R0HS; Eukaryota.
DR GeneTree; ENSGT00440000033697; -.
DR HOGENOM; CLU_069253_1_1_1; -.
DR InParanoid; P24473; -.
DR OMA; AAFHHMW; -.
DR OrthoDB; 1320977at2759; -.
DR PhylomeDB; P24473; -.
DR TreeFam; TF105323; -.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR EvolutionaryTrace; P24473; -.
DR PRO; PR:P24473; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000016484; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; P24473; baseline and differential.
DR Genevisible; P24473; RN.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:RGD.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
DR CDD; cd03021; DsbA_GSTK; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR044088; GSTK.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1883325"
FT CHAIN 2..226
FT /note="Glutathione S-transferase kappa 1"
FT /id="PRO_0000185893"
FT BINDING 16..18
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:14717589"
FT BINDING 53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:14717589"
FT BINDING 183
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:14717589"
FT BINDING 200..201
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:14717589"
FT MOD_RES 36
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 49
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 68
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 74
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 93
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 116
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 167
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 167
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 177
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 177
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 193
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MUTAGEN 16
FT /note="S->A: Reduces catalytic activity about 30-fold.
FT Reduces affinity for glutathione about 4-fold."
FT /evidence="ECO:0000269|PubMed:14717589"
FT CONFLICT 2
FT /note="G -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:1R4W"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1R4W"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:1R4W"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:1R4W"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:1R4W"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:1R4W"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1R4W"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:1R4W"
SQ SEQUENCE 226 AA; 25493 MW; D1E5514C5A65B3CC CRC64;
MGPAPRVLEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLKLR PALLAGIMKD SGNQPPAMVP
HKGQYILKEI PLLKQLFQVP MSVPKDFFGE HVKKGTVNAM RFLTAVSMEQ PEMLEKVSRE
LWMRIWSRDE DITESQNILS AAEKAGMATA QAQHLLNKIS TELVKSKLRE TTGAACKYGA
FGLPTTVAHV DGKTYMLFGS DRMELLAYLL GEKWMGPVPP TLNARL
