ID GSTA4_RAT Reviewed; 222 AA. AC P14942; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 2. DT 27-MAR-2024, entry version 173. DE RecName: Full=Glutathione S-transferase alpha-4; DE EC=2.5.1.18; DE AltName: Full=GST 8-8; DE AltName: Full=GST A4-4; DE AltName: Full=GST K; DE AltName: Full=Glutathione S-transferase Yk; DE Short=GST Yk; GN Name=Gsta4; 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 PROTEIN SEQUENCE, AND ACETYLATION AT MET-1. RC TISSUE=Liver; RX PubMed=2775231; DOI=10.1042/bj2610531; RA Alin P., Jensson H., Cederlund E., Joernvall H., Mannervik B.; RT "Cytosolic glutathione transferases from rat liver. Primary structure of RT class alpha glutathione transferase 8-8 and characterization of low- RT abundance class Mu glutathione transferases."; RL Biochem. J. 261:531-539(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Hepatoma; RX PubMed=1599415; DOI=10.1042/bj2840313; RA Stenberg G., Ridderstroem M., Engstroem A., Pemble S.E., Mannervik B.; RT "Cloning and heterologous expression of cDNA encoding class alpha rat RT glutathione transferase 8-8, an enzyme with high catalytic activity towards RT genotoxic alpha,beta-unsaturated carbonyl compounds."; RL Biochem. J. 284:313-319(1992). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. 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 -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X62660; CAB46530.1; -; mRNA. DR PIR; S23433; XURT8C. DR RefSeq; NP_001100310.1; NM_001106840.1. DR AlphaFoldDB; P14942; -. DR SMR; P14942; -. DR BioGRID; 256738; 1. DR IntAct; P14942; 2. DR STRING; 10116.ENSRNOP00000075572; -. DR iPTMnet; P14942; -. DR PhosphoSitePlus; P14942; -. DR jPOST; P14942; -. DR PaxDb; 10116-ENSRNOP00000012346; -. DR Ensembl; ENSRNOT00000090146.2; ENSRNOP00000075572.1; ENSRNOG00000030449.6. DR Ensembl; ENSRNOT00055002316; ENSRNOP00055001785; ENSRNOG00055001419. DR Ensembl; ENSRNOT00055007434; ENSRNOP00055005580; ENSRNOG00055004669. DR Ensembl; ENSRNOT00060033640; ENSRNOP00060027537; ENSRNOG00060019394. DR Ensembl; ENSRNOT00065027821; ENSRNOP00065021941; ENSRNOG00065016685. DR GeneID; 300850; -. DR KEGG; rno:300850; -. DR UCSC; RGD:1309970; rat. DR AGR; RGD:1309970; -. DR CTD; 2941; -. DR RGD; 1309970; Gsta4. DR eggNOG; KOG1695; Eukaryota. DR GeneTree; ENSGT00940000161750; -. DR InParanoid; P14942; -. DR OrthoDB; 3412208at2759; -. DR PhylomeDB; P14942; -. DR TreeFam; TF105321; -. DR PRO; PR:P14942; -. DR Proteomes; UP000002494; Chromosome 8. DR Bgee; ENSRNOG00000030449; Expressed in ovary and 20 other cell types or tissues. DR ExpressionAtlas; P14942; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004364; F:glutathione transferase activity; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0015643; F:toxic substance binding; IPI:RGD. DR GO; GO:0071285; P:cellular response to lithium ion; IEP:RGD. DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD. DR GO; GO:0009635; P:response to herbicide; IEP:RGD. DR GO; GO:0035094; P:response to nicotine; IEP:RGD. DR GO; GO:0010043; P:response to zinc ion; IEP:RGD. DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD. DR CDD; cd03208; GST_C_Alpha; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR003080; GST_alpha. DR InterPro; IPR004046; GST_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF101; GLUTATHIONE S-TRANSFERASE A4; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01266; GSTRNSFRASEA. DR SFLD; SFLDG01205; AMPS.1; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. DR Genevisible; P14942; RN. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Reference proteome; KW Transferase. FT CHAIN 1..222 FT /note="Glutathione S-transferase alpha-4" FT /id="PRO_0000185795" FT DOMAIN 3..83 FT /note="GST N-terminal" FT DOMAIN 85..208 FT /note="GST C-terminal" FT BINDING 9 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:P13745" FT BINDING 54..55 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:P30711" FT BINDING 67..68 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:P13745" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:2775231" FT CONFLICT 18 FT /note="S -> V (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 48 FT /note="G -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 222 AA; 25510 MW; E0E42852DBA37E58 CRC64; MEVKPKLYYF QGRGRMESIR WLLATAGVEF EEEFLETREQ YEKLQKDGCL LFGQVPLVEI DGMLLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ DLMMMIIGAP FKAPQEKEES LALAVKRAKN RYFPVFEKIL KDHGEAFLVG NQLSWADIQL LEAILMVEEV SAPVLSDFPL LQAFKTRISN IPTIKKFLQP GSQRKPPPDG HYVDVVRTVL KF //