Reviewed, UniProtKB/Swiss-Prot P30711 (GSTT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase theta-1
    EC=2.5.1.18
Alternative name(s):
    GST class-theta-1
    Glutathione transferase T1-1

Gene names

Name:

GSTT1

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	240 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. Acts on 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Found in erythrocyte. Expressed at low levels in liver. In lung, expressed at low levels in Clara cells and ciliated cells at the alveolar/bronchiolar junction. Absent from epithelial cells of larger bronchioles. Ref.9
Polymorphism	The GSTT1 gene is absent from 38% of the population. The presence or absence of the GSTT1 gene is coincident with the conjugator (GSST1+) and non-conjugator (GSTT1-) phenotypes respectively. The GSTT1+ phenotype can catalyze the glutathione conjugation of dichloromethane.
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 electronic annotation. Source: UniProtKB-SubCell
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.8

Chain

2 – 240

239

Glutathione S-transferase theta-1

PRO_0000185938

Regions

Domain

2 – 82

81

GST N-terminal

Domain

88 – 220

133

GST C-terminal

Sites

Active site

11

1

By similarity

Natural variations

Natural variant

21

1

A → T: dbSNP rs2266635.

VAR_014501

Natural variant

141

1

D → N: dbSNP rs2266633.

VAR_014502

Natural variant

169

1

V → I: dbSNP rs2266637. Ref.5

VAR_014503

Natural variant

173

1

E → K: dbSNP rs2234953.

VAR_014504

Experimental info

Sequence conflict

43 – 44

2

DA → SD AA sequence Ref.8

Sequence conflict

45

1

F → C in AAH07065. Ref.7

Sequence conflict

126

1

E → G in CAA55935. Ref.1

Secondary structure

1

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240

Helix Strand Turn

Details...

Beta strand

3 – 7

5

Helix

12 – 23

12

Beta strand

29 – 32

4

Helix

35 – 37

3

Helix

39 – 41

3

Helix

43 – 48

6

Beta strand

56 – 59

4

Beta strand

62 – 65

4

Helix

67 – 77

11

Helix

82 – 84

3

Helix

89 – 101

13

Helix

102 – 104

3

Helix

106 – 117

12

Helix

118 – 123

6

Helix

130 – 150

21

Turn

151 – 154

4

Beta strand

155 – 162

8

Helix

165 – 179

15

Helix

189 – 202

14

Helix

204 – 210

7

Helix

212 – 215

4

Helix

216 – 219

4

Helix

225 – 239

15

Sequences

	Sequence		Length	Mass (Da)
	P30711-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: BD19F2BFDEF9F619	FASTA	240	27,335
	10 20 30 40 50 60 MGLELYLDLL SQPCRAVYIF AKKNDIPFEL RIVDLIKGQH LSDAFAQVNP LKKVPALKDG 70 80 90 100 110 120 DFTLTESVAI LLYLTRKYKV PDYWYPQDLQ ARARVDEYLA WQHTTLRRSC LRALWHKVMF 130 140 150 160 170 180 PVFLGEPVSP QTLAATLAEL DVTLQLLEDK FLQNKAFLTG PHISLADLVA ITELMHPVGA 190 200 210 220 230 240 GCQVFEGRPK LATWRQRVEA AVGEDLFQEA HEVILKAKDF PPADPTIKQK LMPWVLAMIR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism." Pemble S., Schroeder K.R., Spencer S.R., Meyer D.J., Hallier E., Bolt H.M., Ketterer B., Taylor J.B. Biochem. J. 300:271-276(1994) [PubMed: 8198545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme." Jemth P., Mannervik B. Arch. Biochem. Biophys. 348:247-254(1997) [PubMed: 9434735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[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].
[4]	"Complete genomic structure of human glutathione S-transferase TT1." Iida A., Kondo K., Kitamura Y., Mishima C., Osawa S., Kitamoto T., Harigae C., Nakamura Y. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Thymus.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-169.
[6]	"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].
[7]	"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: Urinary bladder.
[8]	"Theta, a new class of glutathione transferases purified from rat and man." Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B. Biochem. J. 274:409-414(1991) [PubMed: 1848757] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-47. Tissue: Liver.
[9]	"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.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBLGenBankDDBJ

X79389 mRNA. Translation: CAA55935.1.
AF435971 mRNA. Translation: AAL31549.1.
AF240786 Genomic DNA. Translation: AAG02374.1.
AB057594 Genomic DNA. Translation: BAB39498.1.
BT019951 mRNA. Translation: AAV38754.1.
Z84718 Genomic DNA. No translation available.
BC007065 mRNA. Translation: AAH07065.1.

IPI

IPI00741097.

PIR

S44358.

RefSeq

NP_000844.2.

UniGene

Hs.268573
Hs.678440

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C3N	X-ray	1.50	A/B/C/D	2-239	[»]
2C3Q	X-ray	1.85	A/B/C/D	2-239	[»]
2C3T	X-ray	2.40	A/B/C/D	2-239	[»]

ModBase

Search...

Proteomic databases

PRIDE

P30711.

Genome annotation databases

Ensembl

ENSG00000184674. Homo sapiens. [Contig view]

GeneID

2952.

KEGG

hsa:2952.

Organism-specific databases

GeneCards

GC22M022706.

H-InvDB

HIX0060128.
HIX0060129.

HGNC

HGNC:4641. GSTT1.

MIM

600436. gene.

PharmGKB

PA183.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P30711.

HOVERGEN

P30711.

OMA

P30711. REAHEVI.

Enzyme and pathway databases

BRENDA

2.5.1.18. 247.

Gene expression databases

ArrayExpress

P30711.

Bgee

P30711.

CleanEx

HS_GSTT1.

GermOnline

ENSG00000184674. 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

11698.

SOURCE

Search...

Entry information

Entry name

GSTT1_HUMAN

Accession

Primary (citable) accession number: P30711
Secondary accession number(s): O00226 , Q5TZY2, Q969K8, Q96IY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 106 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)