ID F7DZD2_HORSE Unreviewed; 240 AA. AC F7DZD2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 10-JUN-2026, entry version 78. DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452}; DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000002027.1, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000002027.1, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002027.1, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O., RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T., RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T., RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S., RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G., RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R., RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000002027.1} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002027.1}; RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=RX + glutathione = an S-substituted glutathione + a halide CC anion + 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|ARBA:ARBA00047960}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family. CC {ECO:0000256|ARBA:ARBA00009899}. 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 RefSeq; XP_001489453.1; XM_001489403.5. DR AlphaFoldDB; F7DZD2; -. DR STRING; 9796.ENSECAP00000002027; -. DR PaxDb; 9796-ENSECAP00000002027; -. DR Ensembl; ENSECAT00000002830.3; ENSECAP00000002027.1; ENSECAG00000000612.4. DR GeneID; 100050322; -. DR KEGG; ecb:100050322; -. DR GeneTree; ENSGT00940000156366; -. DR HOGENOM; CLU_011226_2_0_1; -. DR OMA; CQYRVDE; -. DR OrthoDB; 422574at2759; -. DR Proteomes; UP000002281; Chromosome 8. DR Bgee; ENSECAG00000000612; Expressed in liver and 23 other cell types or tissues. DR ExpressionAtlas; F7DZD2; baseline. 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 FunFam; 1.20.1050.10:FF:000008; Glutathione S-transferase theta-1; 1. DR FunFam; 3.40.30.10:FF:000086; Glutathione S-transferase theta-1; 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; IPR051369; GST_Theta. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR43917; -; 1. DR PANTHER; PTHR43917:SF9; GLUTATHIONE S-TRANSFERASE THETA-1; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01153; Main.4:_Theta-like; 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 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F7DZD2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 1..82 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 88..222 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 240 AA; 27051 MW; B37F58F774558FC1 CRC64; MGLELYLDLL SQPCRAVYIF AKKNGIPFEL RTVELLKGQH FSADFAQLNP LKKVPVLKDG DFTLTESVAI LLYLTRKYKT PDHWYPQDLQ ARARVDEYLA WQHTALRRNC LRTLWHKLML PVFMGEPVAP EMLAATLAEL DGSLQLLEDK FLQNKAFFAG PHISLADLVA ITELMHAVGA GCQVFEGRPK LAAWRQRVEA AVGAVLFQEA HEVILKVKDS PPADPTIKQK LRPSILALIQ //