ID   GSTT4_RAT               Reviewed;         240 AA.
AC   Q4V8E6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glutathione S-transferase theta-4 {ECO:0000305};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P30711};
DE   AltName: Full=GST class-theta-4;
GN   Name=Gstt4 {ECO:0000312|RGD:1591294};
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000250|UniProtKB:P30711}.
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:0000250|UniProtKB:P30711};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta 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; BC097423; AAH97423.1; -; mRNA.
DR   RefSeq; NP_001103145.1; NM_001109675.1.
DR   AlphaFoldDB; Q4V8E6; -.
DR   SMR; Q4V8E6; -.
DR   STRING; 10116.ENSRNOP00000055115; -.
DR   iPTMnet; Q4V8E6; -.
DR   PhosphoSitePlus; Q4V8E6; -.
DR   PaxDb; Q4V8E6; -.
DR   PRIDE; Q4V8E6; -.
DR   Ensembl; ENSRNOT00000058314; ENSRNOP00000055115; ENSRNOG00000038300.
DR   GeneID; 686922; -.
DR   KEGG; rno:686922; -.
DR   UCSC; RGD:1591294; rat.
DR   CTD; 25774; -.
DR   RGD; 1591294; Gstt4.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000161301; -.
DR   HOGENOM; CLU_011226_2_0_1; -.
DR   InParanoid; Q4V8E6; -.
DR   OMA; IQQPMSK; -.
DR   OrthoDB; 1231780at2759; -.
DR   PhylomeDB; Q4V8E6; -.
DR   PRO; PR:Q4V8E6; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000038300; Expressed in testis and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   CDD; cd03183; GST_C_Theta; 1.
DR   CDD; cd03050; GST_N_Theta; 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; IPR040077; GST_C_Theta.
DR   InterPro; IPR040075; GST_N_Theta.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
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   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..240
FT                   /note="Glutathione S-transferase theta-4"
FT                   /id="PRO_0000329077"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..218
FT                   /note="GST C-terminal"
FT   BINDING         40
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
SQ   SEQUENCE   240 AA;  27970 MW;  2D4B938412854822 CRC64;
     MGLELYMDLL SAPCRAVYIF ARKNGIPFDF QFVDLLKGHH HSKEYIEINP LRKVPSLRDG
     KFILSESVAI LCYLCRKYSA PSHWYPPDLH MRARVDEFMA WQHTAIQVPM SKILWIKLII
     PMITGEEVPT ERLDKTLDEV NKNIKQFEEK FLQDKLFITG DHISLADLVA LVEMMQPMGT
     NHNVFISSKL AEWRMRVELA IGSGLFWEAH DRLVKLPSWD CSTLDPSIKM KICEFLQKYK