GST2_HUMAN
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 03-AUG-2022, entry version 83.
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; 1.
DR ChEMBL; CHEMBL2142; -.
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 PaxDb; P0CG29; -.
DR PeptideAtlas; P0CG29; -.
DR PRIDE; P0CG29; -.
DR ProteomicsDB; 52459; -.
DR DNASU; 2953; -.
DR Ensembl; ENST00000618279.2; ENSP00000477540.1; ENSG00000277897.2.
DR GeneID; 2953; -.
DR KEGG; hsa:2953; -.
DR UCSC; uc032qyg.2; human.
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; 1231780at2759; -.
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 936 CRISPR screens.
DR GenomeRNAi; 2953; -.
DR Pharos; P0CG29; Tdark.
DR PRO; PR:P0CG29; -.
DR Proteomes; UP000005640; Chromosome 22.
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 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; PF02798; GST_N; 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 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
