GSTA4_RAT
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 03-AUG-2022, entry version 165.
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}.
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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.ENSRNOP00000012346; -.
DR iPTMnet; P14942; -.
DR PhosphoSitePlus; P14942; -.
DR jPOST; P14942; -.
DR PaxDb; P14942; -.
DR PRIDE; P14942; -.
DR Ensembl; ENSRNOT00000090146; ENSRNOP00000075572; ENSRNOG00000030449.
DR GeneID; 300850; -.
DR KEGG; rno:300850; -.
DR UCSC; RGD:1309970; rat.
DR CTD; 2941; -.
DR RGD; 1309970; Gsta4.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000161750; -.
DR InParanoid; P14942; -.
DR OMA; AKPKLWY; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P14942; -.
DR TreeFam; TF105321; -.
DR PRO; PR:P14942; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000030449; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; P14942; baseline and differential.
DR Genevisible; P14942; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
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 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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01266; GSTRNSFRASEA.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
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
