[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. DOI=10.1016/j.cbpc.2005.05.002; PubMed=15967696 [NCBI, ExPASy, EBI, Israel, Japan] Fukuhara R., Kageyama T.; "Structure, gene expression, and evolution of primate glutathione peroxidases."; Comp. Biochem. Physiol. 141B:428-436(2005).

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
TISSUE SPECIFICITY: Exclusively expressed in the stomach and small intestine.
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

AB121003; BAE17012.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q4AEH8; 4-187.

ModBase

Q4AEH8.

Protein family/group databases

PeroxiBase

3705; MfGPx02.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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).

Phylogenomic databases

HOVERGEN

Q4AEH8; -.

Other

ProtoNet

Q4AEH8.

UniRef

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

Keywords

Cytoplasm; Oxidoreductase; Peroxidase; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 190`	`190`	`Glutathione peroxidase 2.`	`PRO_0000066621`
`ACT_SITE`	`40 40`		`By similarity.`
`NON_STD`	`40 40`		`Selenocysteine.`

Sequence information

Length: 190 AA [This is the length of the unprocessed precursor]

Molecular weight: 21970 Da [This is the MW of the unprocessed precursor]

CRC64: E63C54D365DF83B1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL NELQCRFPRR 

        70         80         90        100        110        120 
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK 

       130        140        150        160        170        180 
DKLPYPHDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEVEPFRRYS RTFPTINIEP 

       190 
DIKRLLKVAI

Q4AEH8 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