ID   GST2_HUMAN              Reviewed;         244 AA.
AC   P0CG29; O60665; P30712; Q6IPV7; Q9HD76;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Glutathione S-transferase theta-2;
DE            EC=2.5.1.18 {ECO:0000269|PubMed:1417752};
DE   AltName: Full=GST class-theta-2;
GN   Name=GSTT2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10975610; DOI=10.1097/00008571-200008000-00009;
RA   Sprenger R., Schlagenhaufer R., Kerb R., Bruhn C., Brockmoeller J.,
RA   Roots I., Brinkmann U.;
RT   "Characterization of the glutathione S-transferase GSTT1 deletion:
RT   discrimination of all genotypes by polymerase chain reaction indicates a
RT   trimodular genotype-phenotype correlation.";
RL   Pharmacogenetics 10:557-565(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Liver;
RX   PubMed=1417752; DOI=10.1042/bj2860929;
RA   Hussey A.J., Hayes J.D.;
RT   "Characterization of a human class-theta glutathione S-transferase with
RT   activity towards 1-menaphthyl sulphate.";
RL   Biochem. J. 286:929-935(1992).
RN   [4]
RP   TISSUE SPECIFICITY.
RC   TISSUE=Liver, and Lung;
RX   PubMed=8761485; DOI=10.1042/bj3180297;
RA   Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T.;
RT   "The distribution of theta-class glutathione S-transferases in the liver
RT   and lung of mouse, rat and human.";
RL   Biochem. J. 318:297-303(1996).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles (PubMed:1417752).
CC       Has a sulfatase activity (PubMed:1417752).
CC       {ECO:0000269|PubMed:1417752}.
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:0000269|PubMed:1417752};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30713}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1417752}.
CC       Nucleus {ECO:0000250|UniProtKB:P30713}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in liver. In lung,
CC       expressed at low levels in ciliated bronchiolar cells, alveolar
CC       macrophages and alveolar type II cells. {ECO:0000269|PubMed:8761485}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; AF240786; AAG02373.1; -; Genomic_DNA.
DR   EMBL; AP000351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A56847; A56847.
DR   RefSeq; NP_000845.2; NM_000854.4.
DR   PDB; 4MPF; X-ray; 2.10 A; A/B=1-244.
DR   PDBsum; 4MPF; -.
DR   AlphaFoldDB; P0CG29; -.
DR   SMR; P0CG29; -.
DR   IntAct; P0CG29; 2.
DR   MINT; P0CG29; -.
DR   ChEMBL; CHEMBL2142; -.
DR   DrugBank; DB00321; Amitriptyline.
DR   DrugBank; DB00291; Chlorambucil.
DR   DrugBank; DB03619; Deoxycholic acid.
DR   DrugBank; DB03310; Glutathione disulfide.
DR   DrugBank; DB04132; S-Hexylglutathione.
DR   iPTMnet; P0CG29; -.
DR   PhosphoSitePlus; P0CG29; -.
DR   BioMuta; GSTT2; -.
DR   DMDM; 300680960; -.
DR   jPOST; P0CG29; -.
DR   MassIVE; P0CG29; -.
DR   MaxQB; P0CG29; -.
DR   PeptideAtlas; P0CG29; -.
DR   ProteomicsDB; 52459; -.
DR   Pumba; P0CG29; -.
DR   DNASU; 2953; -.
DR   Ensembl; ENST00000618279.2; ENSP00000477540.1; ENSG00000277897.3.
DR   GeneID; 2953; -.
DR   KEGG; hsa:2953; -.
DR   MANE-Select; ENST00000618279.3; ENSP00000477540.1; NM_000854.5; NP_000845.2.
DR   UCSC; uc032qyg.2; human.
DR   AGR; HGNC:4642; -.
DR   CTD; 2953; -.
DR   DisGeNET; 2953; -.
DR   GeneCards; GSTT2; -.
DR   HGNC; HGNC:4642; GSTT2.
DR   MIM; 600437; gene.
DR   neXtProt; NX_P0CG29; -.
DR   InParanoid; P0CG29; -.
DR   OrthoDB; 1199296at2759; -.
DR   PhylomeDB; P0CG29; -.
DR   TreeFam; TF325759; -.
DR   PathwayCommons; P0CG29; -.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   SignaLink; P0CG29; -.
DR   BioGRID-ORCS; 2953; 13 hits in 966 CRISPR screens.
DR   GenomeRNAi; 2953; -.
DR   Pharos; P0CG29; Tdark.
DR   PRO; PR:P0CG29; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; P0CG29; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
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:SF4; GLUTATHIONE S-TRANSFERASE THETA-2-RELATED; 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   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   3D-structure; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1417752"
FT   CHAIN           2..244
FT                   /note="Glutathione S-transferase theta-2"
FT                   /id="PRO_0000185939"
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..224
FT                   /note="GST C-terminal"
FT   BINDING         40..41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   BINDING         104..107
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   CONFLICT        2
FT                   /note="G -> V (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           12..23
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   TURN            35..38
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           67..77
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           89..105
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   TURN            106..111
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           112..117
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           129..148
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   TURN            149..153
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           164..177
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   TURN            183..186
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           188..201
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           203..214
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           216..221
FT                   /evidence="ECO:0007829|PDB:4MPF"
FT   HELIX           230..241
FT                   /evidence="ECO:0007829|PDB:4MPF"
SQ   SEQUENCE   244 AA;  27506 MW;  DBA15D045262FFC3 CRC64;
     MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS LGKLPTLKDG
     DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG WHADCIRGTF GIPLWVQVLG
     PLIGVQVPKE KVERNRTAMD QALQWLEDKF LGDRPFLAGQ QVTLADLMAL EELMQPVALG
     YELFEGRPRL AAWRGRVEAF LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI
     ARIP
//