[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0166-6851(91)90140-2; PubMed=1775156 [NCBI, ExPASy, EBI, Israel, Japan] Wright M.D., Harrison R.A., Melder A.M., Newport G.R., Mitchell G.F.; "Another 26-kilodalton glutathione S-transferase of Schistosoma mansoni."; Mol. Biochem. Parasitol. 49:177-179(1991).

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

M73624; -; NOT_ANNOTATED_CDS; mRNA.

[EMBL / GenBank / DDBJ]

PIR

A45556; A45556.

3D structure databases

HSSP

P08515; 1GTA. [HSSP ENTRY / PDB]

SMR

P35661; 2-218.

ModBase

P35661.

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

P35661.

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`
`CHAIN`	`1 218`	`218`	`Glutathione S-transferase class-mu 26 kDa isozyme.`	`PRO_0000185811`
`DOMAIN`	`1 83`	`83`	`GST N-terminal.`
`DOMAIN`	`85 203`	`119`	`GST C-terminal.`
`ACT_SITE`	`7 7`		`By similarity.`

Sequence information

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

Molecular weight: 25411 Da [This is the MW of the unprocessed precursor]

CRC64: D8D3EE9028B36185 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPKLGYWKI KGLVQPTRLL LEYLGERYEE RLYDRNDGDV WRNEKFKLGL DFPNLPYYID 

        70         80         90        100        110        120 
GDVKLTQSMA ILRYIADKHN MLGGCPKERA EISMLEGAIL DIRYGVSRIA YNKEFETLKV 

       130        140        150        160        170        180 
DFLNQLPGML KMFEDRLSHN TYLNGDKVTH PDFMLYDALD VVLYMDPKCL DNFPKLISFK 

       190        200        210 
QRIENLPPIK NYLNSNRYIK WPLQGWSATF GGGDAPPK

P35661 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