[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-4894(92)90051-B; PubMed=1740183 [NCBI, ExPASy, EBI, Israel, Japan] Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.; "Molecular characterization of cDNA sequences encoding glutathione S-transferases of Fasciola hepatica."; Exp. Parasitol. 74:232-237(1992).
[2]	ERRATUM. DOI=10.1006/expr.1993.1097; PubMed=8224094 [NCBI, ExPASy, EBI, Israel, Japan] Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.; Exp. Parasitol. 77:385-385(1993).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-218. Crameri S.; Patent number WO9008819, 09-AUG-1990.

Comments

FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
FUNCTION: GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the GST superfamily. Mu family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M77680; AAA29139.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
A00994; CAA00119.1; -; Unassigned_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P31670; 1FHE. [HSSP ENTRY / PDB]

SMR

P31671; 2-215.

ModBase

P31671.

Ontologies

GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P31671.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 218`	`217`	`Glutathione S-transferase class-mu 26 kDa isozyme 7.`	`PRO_0000185809`
`DOMAIN`	`2 83`	`82`	`GST N-terminal.`
`DOMAIN`	`85 203`	`119`	`GST C-terminal.`
`ACT_SITE`	`7 7`		`By similarity.`
`CONFLICT`	`36 43`		`NDREKWLG -> MIGRNGWA (in Ref. 3; CAA00119).`
`CONFLICT`	`189 197`		`IKEYMKSER -> SRYMSRA (in Ref. 3; CAA00119).`

Sequence information

Length: 218 AA [This is the length of the unprocessed precursor]

Molecular weight: 25327 Da [This is the MW of the unprocessed precursor]

CRC64: 30D9EC6CDE6D592E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPAKLGYWKI RGLQQPVRLF LEYLGEEYEE HLYGRNDREK WLGDKFNMGL DLPNLPYYID 

        70         80         90        100        110        120 
DKCKLTQSVA IMRYIADKHG MLGSTPEERA RISMIEGAAM DLRIGFGLTC YNPKFEELKG 

       130        140        150        160        170        180 
DYLKGLPTTL KMWSDFLGDR QYLIGSSVSH VDFMVYEALD CIRYLAPQCL DDFPKLKEFK 

       190        200        210 
SRIEDLPKIK EYMKSERFIK WPLHSWTSPF GGGDAPPA

P31671 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools