[1]	NUCLEOTIDE SEQUENCE [MRNA]. 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).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; The German cDNA consortium; Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the glutathione peroxidase family.
SEQUENCE CAUTION:
- Sequence=CAH90226.1; Type=Erroneous termination; Positions=40; Note=Translated as Sec
- Sequence=CAH90226.1; Type=Frameshift; Positions=183;

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

AB121001; BAE17010.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR857983; CAH90226.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q4AEI0; 4-187.

ModBase

Q4AEI0.

Protein family/group databases

PeroxiBase

3726; PpyGPx02.

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).

BLOCKS

Q4AEI0.

Phylogenomic databases

HOVERGEN

Q4AEI0; -.

Other

ProtoNet

Q4AEI0.

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_0000066623`
`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: 21984 Da [This is the MW of the unprocessed precursor]

CRC64: 48904FB5D91F5FA1 [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 PGSGYQPTFT LVQKCEVNGQ NEHPVFAYLK 

       130        140        150        160        170        180 
DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP 

       190 
DIKRLLKVAI

Q4AEI0 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