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 24-JAN-2024, entry version 113.
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; 10116-ENSRNOP00000055115; -.
DR Ensembl; ENSRNOT00000058314.5; ENSRNOP00000055115.3; ENSRNOG00000038300.5.
DR Ensembl; ENSRNOT00055035837; ENSRNOP00055029094; ENSRNOG00055020987.
DR Ensembl; ENSRNOT00060029664; ENSRNOP00060023881; ENSRNOG00060017367.
DR Ensembl; ENSRNOT00065043055; ENSRNOP00065035254; ENSRNOG00065025034.
DR GeneID; 686922; -.
DR KEGG; rno:686922; -.
DR UCSC; RGD:1591294; rat.
DR AGR; RGD:1591294; -.
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; 1199296at2759; -.
DR PhylomeDB; Q4V8E6; -.
DR PRO; PR:Q4V8E6; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000038300; Expressed in testis and 3 other cell types or 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 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; IPR040077; GST_C_Theta.
DR InterPro; IPR040075; GST_N_Theta.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43917; -; 1.
DR PANTHER; PTHR43917:SF13; GLUTATHIONE S-TRANSFERASE THETA-4-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 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.
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
//
