ID Q9WU21_RAT Unreviewed; 218 AA. AC Q9WU21; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494}; DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494}; GN Name=Gstm3 {ECO:0000313|RGD:620381}; GN Synonyms=Gstm3l {ECO:0000313|RGD:620381}, Gstm4 GN {ECO:0000313|RGD:620381}, GstYb4 {ECO:0000313|EMBL:AAD22630.1}; 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 {ECO:0000313|EMBL:AAD22630.1}; RN [1] {ECO:0000313|EMBL:AAD22630.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAD22630.1}; RX PubMed=3403534; RA Lai H.-C.J., Qian B., Grove G., Tu C.-P.D.; RT "Gene expression of rat glutathione S-transferases. Evidence for gene RT conversion in the evolution of the Yb multigene family."; RL J. Biol. Chem. 263:11389-11395(1988). RN [2] {ECO:0000313|EMBL:AAD22630.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAD22630.1}; RA Qian B., Tu C.P.; RT "The Rat Glutathione S-Transferase Yb4 genomic clone sequence."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. 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:0000256|RuleBase:RU003494}; CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. CC {ECO:0000256|ARBA:ARBA00005861, ECO:0000256|RuleBase:RU003494}. 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; AF106661; AAD22630.1; -; Genomic_DNA. DR PIR; B29231; B29231. DR RefSeq; NP_065415.1; NM_020540.1. DR AlphaFoldDB; Q9WU21; -. DR iPTMnet; Q9WU21; -. DR PhosphoSitePlus; Q9WU21; -. DR GeneID; 57298; -. DR KEGG; rno:57298; -. DR UCSC; RGD:620381; rat. DR AGR; RGD:620381; -. DR RGD; 620381; Gstm3. DR OrthoDB; 5488107at2759; -. DR PhylomeDB; Q9WU21; -. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IEA:UniProt. DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD. DR GO; GO:0009617; P:response to bacterium; ISO:RGD. DR CDD; cd03209; GST_C_Mu; 1. DR CDD; cd03075; GST_N_Mu; 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; IPR004046; GST_C. DR InterPro; IPR003081; GST_mu. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF219; GLUTATHIONE S-TRANSFERASE MU 3; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01267; GSTRNSFRASEM. 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; Q9WU21; RN. PE 3: Inferred from homology; KW Transferase {ECO:0000256|RuleBase:RU003494, ECO:0000313|EMBL:AAD22630.1}. FT DOMAIN 1..88 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 90..208 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 218 AA; 25644 MW; 4E9C22F9AEEAC6C4 CRC64; MAMILGYWNV RGLTHPIRLL LEYTDSNYEE KRYVMGDAPN FDRSQWLSEK FNLGLDIPNL PYLIDGSHKV TQSNAILRYL GRKHNLCGET EEERIRVDTL ENQVMDTRIH LMIVCCSPDF EKQKPEFLKS IPEKMKIYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPECLDAFPN LKDFLARFEG LKKISAYMKS SSFLPRPVFT KIPQWGTD //