GSTT2_HUMAN
ID GSTT2_HUMAN Reviewed; 244 AA.
AC P0CG30; 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 86.
DE RecName: Full=Glutathione S-transferase theta-2B;
DE EC=2.5.1.18 {ECO:0000269|PubMed:1417752};
DE AltName: Full=Glutathione S-transferase theta-2 {ECO:0000303|PubMed:7789971};
DE Short=GST class-theta-2 {ECO:0000303|PubMed:7789971};
GN Name=GSTT2B; Synonyms=GSTT2 {ECO:0000303|PubMed:7789971};
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=7789971; DOI=10.1016/0888-7543(95)80037-m;
RA Tan K.L., Webb G.C., Baker R.T., Board P.G.;
RT "Molecular cloning of a cDNA and chromosomal localization of a human theta-
RT class glutathione S-transferase gene (GSTT2) to chromosome 22.";
RL Genomics 25:381-387(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-139.
RA Coggan M.A., Board P.G.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [6]
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 [7]
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP SUBUNIT.
RX PubMed=9551553; DOI=10.1016/s0969-2126(98)00034-3;
RA Rossjohn J., McKinstry W.J., Oakley A.J., Verger D., Flanagan J.,
RA Chelvanayagam G., Tan K.-L., Board P.G., Parker M.W.;
RT "Human theta class glutathione transferase: the crystal structure reveals a
RT sulfate-binding pocket within a buried active site.";
RL Structure 6:309-322(1998).
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:0000269|PubMed:9551553}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1417752}.
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; L38503; AAB63956.1; -; mRNA.
DR EMBL; AF057176; AAC13317.1; -; Genomic_DNA.
DR EMBL; AF057173; AAC13317.1; JOINED; Genomic_DNA.
DR EMBL; AF057174; AAC13317.1; JOINED; Genomic_DNA.
DR EMBL; AF057175; AAC13317.1; JOINED; Genomic_DNA.
DR EMBL; CR456500; CAG30386.1; -; mRNA.
DR EMBL; AP000350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002415; AAH02415.1; -; mRNA.
DR CCDS; CCDS33617.1; -.
DR PIR; A56847; A56847.
DR RefSeq; NP_001074312.1; NM_001080843.3.
DR PDB; 1LJR; X-ray; 3.20 A; A/B=1-244.
DR PDB; 2LJR; X-ray; 3.20 A; A/B=1-244.
DR PDB; 3LJR; X-ray; 3.30 A; A/B=1-244.
DR PDB; 4MPG; X-ray; 1.95 A; A/B=1-244.
DR PDBsum; 1LJR; -.
DR PDBsum; 2LJR; -.
DR PDBsum; 3LJR; -.
DR PDBsum; 4MPG; -.
DR AlphaFoldDB; P0CG30; -.
DR SMR; P0CG30; -.
DR BioGRID; 109208; 3.
DR BioGRID; 575985; 10.
DR IntAct; P0CG30; 4.
DR STRING; 9606.ENSP00000290765; -.
DR DrugBank; DB03310; Glutathione disulfide.
DR GlyGen; P0CG30; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0CG30; -.
DR PhosphoSitePlus; P0CG30; -.
DR BioMuta; GSTT2B; -.
DR EPD; P0CG30; -.
DR jPOST; P0CG30; -.
DR MassIVE; P0CG30; -.
DR MaxQB; P0CG30; -.
DR PaxDb; P0CG30; -.
DR PeptideAtlas; P0CG30; -.
DR PRIDE; P0CG30; -.
DR Antibodypedia; 23874; 68 antibodies from 20 providers.
DR DNASU; 2953; -.
DR Ensembl; ENST00000290765.9; ENSP00000290765.4; ENSG00000133433.11.
DR Ensembl; ENST00000616938.1; ENSP00000478389.1; ENSG00000278695.1.
DR GeneID; 653689; -.
DR KEGG; hsa:653689; -.
DR MANE-Select; ENST00000290765.9; ENSP00000290765.4; NM_001080843.4; NP_001074312.1.
DR UCSC; uc002zyw.5; human.
DR CTD; 653689; -.
DR DisGeNET; 653689; -.
DR GeneCards; GSTT2B; -.
DR HGNC; HGNC:33437; GSTT2B.
DR HPA; ENSG00000133433; Group enriched (adrenal gland, breast).
DR neXtProt; NX_P0CG30; -.
DR OpenTargets; ENSG00000133433; -.
DR PharmGKB; PA162390358; -.
DR VEuPathDB; HostDB:ENSG00000133433; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000162786; -.
DR HOGENOM; CLU_011226_2_0_1; -.
DR InParanoid; P0CG30; -.
DR OMA; AYKVRLF; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; P0CG30; -.
DR TreeFam; TF325759; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; P0CG30; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR SignaLink; P0CG30; -.
DR BioGRID-ORCS; 653689; 292 hits in 988 CRISPR screens.
DR EvolutionaryTrace; P0CG30; -.
DR GeneWiki; GSTT2; -.
DR GenomeRNAi; 653689; -.
DR Pharos; P0CG30; Tbio.
DR PRO; PR:P0CG30; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P0CG30; protein.
DR Bgee; ENSG00000133433; Expressed in lower esophagus mucosa and 91 other tissues.
DR ExpressionAtlas; P0CG30; baseline and differential.
DR Genevisible; P0CG30; HS.
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:0005654; C:nucleoplasm; IDA:HPA.
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; 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 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; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1417752"
FT CHAIN 2..244
FT /note="Glutathione S-transferase theta-2B"
FT /id="PRO_0000395344"
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:0000269|PubMed:9551553"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9551553,
FT ECO:0007744|PDB:1LJR"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9551553,
FT ECO:0007744|PDB:1LJR"
FT BINDING 104..107
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9551553,
FT ECO:0007744|PDB:1LJR"
FT VARIANT 139
FT /note="M -> I (in dbSNP:rs1622002)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_033982"
FT CONFLICT 2
FT /note="G -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..158
FT /note="FLA -> P (in Ref. 2; AAC13317)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:4MPG"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4MPG"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:4MPG"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4MPG"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 89..105
FT /evidence="ECO:0007829|PDB:4MPG"
FT TURN 106..111
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 129..148
FT /evidence="ECO:0007829|PDB:4MPG"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:4MPG"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4MPG"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:4MPG"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 203..222
FT /evidence="ECO:0007829|PDB:4MPG"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:4MPG"
SQ SEQUENCE 244 AA; 27507 MW; DBAF5D00F8C2FFC3 CRC64;
MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS LGKLPTLKDG
DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG WHADCIRGTF GIPLWVQVLG
PLIGVQVPEE KVERNRTAMD QALQWLEDKF LGDRPFLAGQ QVTLADLMAL EELMQPVALG
YELFEGRPRL AAWRGRVEAF LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI
ARIP
