Reviewed, UniProtKB/Swiss-Prot P30712 (GSTT2_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase theta-2
    EC=2.5.1.18
Alternative name(s):
    GST class-theta-2

Gene names

Name:

GSTT2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed at low levels in liver. In lung, expressed at low levels in ciliated bronchiolar cells, alveolar macrophages and alveolar type II cells. Ref.8
Sequence similarities	Belongs to the GST superfamily. Theta family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	glutathione transferase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 244

243

Glutathione S-transferase theta-2

PRO_0000185939

Regions

Domain

2 – 82

81

GST N-terminal

Domain

88 – 224

137

GST C-terminal

Sites

Active site

11

1

By similarity

Natural variations

Natural variant

129

1

E → K: dbSNP rs140195. Ref.3

VAR_033981

Natural variant

139

1

M → I: dbSNP rs1622002. Ref.2

VAR_033982

Experimental info

Sequence conflict

2

1

G → V AA sequence Ref.7

Sequence conflict

156 – 158

3

FLA → P in AAC13317. Ref.2

Secondary structure

1

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244

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Helix

12 – 23

12

Beta strand

29 – 32

4

Turn

35 – 38

4

Helix

39 – 41

3

Helix

43 – 46

4

Beta strand

56 – 59

4

Beta strand

62 – 65

4

Helix

67 – 77

11

Helix

82 – 84

3

Helix

89 – 105

17

Turn

106 – 109

4

Helix

112 – 117

6

Helix

119 – 122

4

Helix

129 – 149

21

Beta strand

152 – 156

5

Beta strand

159 – 161

3

Helix

164 – 178

15

Turn

183 – 186

4

Helix

188 – 201

14

Helix

203 – 210

8

Helix

212 – 221

10

Helix

230 – 241

12

Sequences

	Sequence		Length	Mass (Da)
	P30712-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DBAF5D00F8C2FFC3	FASTA	244	27,507
	10 20 30 40 50 60 MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS LGKLPTLKDG 70 80 90 100 110 120 DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG WHADCIRGTF GIPLWVQVLG 130 140 150 160 170 180 PLIGVQVPEE KVERNRTAMD QALQWLEDKF LGDRPFLAGQ QVTLADLMAL EELMQPVALG 190 200 210 220 230 240 YELFEGRPRL AAWRGRVEAF LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a cDNA and chromosomal localization of a human theta-class glutathione S-transferase gene (GSTT2) to chromosome 22." Tan K.L., Webb G.C., Baker R.T., Board P.G. Genomics 25:381-387(1995) [PubMed: 7789971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	Coggan M.A., Board P.G. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-139.
[3]	"Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation." Sprenger R., Schlagenhaufer R., Kerb R., Bruhn C., Brockmoeller J., Roots I., Brinkmann U. Pharmacogenetics 10:557-565(2000) [PubMed: 10975610] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-129.
[4]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Characterization of a human class-theta glutathione S-transferase with activity towards 1-menaphthyl sulphate." Hussey A.J., Hayes J.D. Biochem. J. 286:929-935(1992) [PubMed: 1417752] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Tissue: Liver.
[8]	"The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human." Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T. Biochem. J. 318:297-303(1996) [PubMed: 8761485] [Abstract] Cited for: TISSUE SPECIFICITY. Tissue: Liver and Lung.
[9]	"Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site." Rossjohn J., McKinstry W.J., Oakley A.J., Verger D., Flanagan J., Chelvanayagam G., Tan K.-L., Board P.G., Parker M.W. Structure 6:309-322(1998) [PubMed: 9551553] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L38503 mRNA. Translation: AAB63956.1.
AF057176 , AF057173, AF057174, AF057175 Genomic DNA. Translation: AAC13317.1.
AF240786 Genomic DNA. Translation: AAG02373.1.
CR456500 mRNA. Translation: CAG30386.1.
Z84718 Genomic DNA. No translation available.
BC002415 mRNA. Translation: AAH02415.1.

IPI

IPI00419250.

PIR

A56847.

RefSeq

NP_000845.1.
NP_001074312.1.

UniGene

Hs.654462
Hs.656498

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LJR	X-ray	3.20	A/B	1-244	[»]
2LJR	X-ray	3.20	A/B	1-244	[»]
3LJR	X-ray	3.30	A/B	1-244	[»]

ModBase

Search...

Proteomic databases

PRIDE

P30712.

Genome annotation databases

Ensembl

ENSG00000133433. Homo sapiens. [Contig view]

GeneID

2953.
653689.

KEGG

hsa:2953.
hsa:653689.

NMPDR

fig|9606.3.peg.21406.

Organism-specific databases

GeneCards

GC22M022631.
GC22P022652.

H-InvDB

HIX0016304.
HIX0041206.

HGNC

HGNC:4642. GSTT2.

HPA

HPA000750.

MIM

600437. gene.

PharmGKB

PA29030.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P30712.

HOVERGEN

P30712.

OMA

P30712. PSRALYI.

Enzyme and pathway databases

BRENDA

2.5.1.18. 247.

Gene expression databases

Bgee

P30712.

CleanEx

HS_GSTT2.

GermOnline

ENSG00000133433. Homo sapiens.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

11702.

SOURCE

Search...

Entry information

Entry name

GSTT2_HUMAN

Accession

Primary (citable) accession number: P30712
Secondary accession number(s): O60665, Q6IPV7, Q9HD76

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)