[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Puerto Rican; DOI=10.1016/0166-6851(92)90042-I; PubMed=1625700 [NCBI, ExPASy, EBI, Israel, Japan] Williams D.L., Pierce R.J., Cookson E., Capron A.; "Molecular cloning and sequencing of glutathione peroxidase from Schistosoma mansoni."; Mol. Biochem. Parasitol. 52:127-130(1992).
[2]	SEQUENCE REVISION TO 43. Williams D.L., Pierce R.J., Cookson E., Capron A.; Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NMRI; DOI=10.1006/expr.1995.1038; PubMed=7895842 [NCBI, ExPASy, EBI, Israel, Japan] Mei H., Loverde P.T.; "Schistosoma mansoni: cloning the gene encoding glutathione peroxidase."; Exp. Parasitol. 80:319-322(1995).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Puerto Rican; DOI=10.1016/0378-1119(94)90798-6; PubMed=8125294 [NCBI, ExPASy, EBI, Israel, Japan] Roche C., Williams D.L., Khalife J., Lepresle T., Capron A., Pierce R.J.; "Cloning and characterization of the gene encoding Schistosoma mansoni glutathione peroxidase."; Gene 138:149-152(1994).

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
INDUCTION: Activity increases significantly as worms mature in their host and is positively correlated to the resistance to antioxidants.
SIMILARITY: Belongs to the glutathione peroxidase family.

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

M86510; AAA29885.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L37762; AAC14468.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L14328; AAB08485.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

Q00277.

Protein family/group databases

PeroxiBase

3745; SmamGPx01.

Ontologies

GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR11592; Glut_peroxidase; 1.

Pfam

PF00255; GSHPx; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000303; Glutathion_perox; 1.

PRINTS

PR01011; GLUTPROXDASE.

PROSITE

PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q00277.

Other

UniRef

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

Keywords

Oxidoreductase; Peroxidase; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 169`	`169`	`Glutathione peroxidase.`	`PRO_0000066645`
`ACT_SITE`	`43 43`		`By similarity.`
`NON_STD`	`43 43`		`Selenocysteine.`

Sequence information

Length: 169 AA [This is the length of the unprocessed precursor]

Molecular weight: 19471 Da [This is the MW of the unprocessed precursor]

CRC64: 4B787788913F84B0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSSHKSWNS IYEFTVKDIN GVDVSLEKYR GHVCLIVNVA CKUGATDKNY RQLQEMHTRL 

        70         80         90        100        110        120 
VGKGLRILAF PCNQFGGQEP WAEAEIKKFV TEKYGVQFDM FSKIKVNGSD ADDLYKFLKS 

       130        140        150        160 
RQHGTLTNNI KWNFSKFLVD RQGQPVKRYS PTTAPYDIEG DIMELLEKK

Q00277 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