[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

FUNCTION: Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H₂O.
SUBCELLULAR LOCATION: Mitochondrion (By similarity). Cytoplasm (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.

Name	Mitochondrial
Isoform ID	Q4AEH0-1
This is the isoform sequence displayed in this entry.

Name	Cytoplasmic
Isoform ID	Q4AEH0-2
Features which should be applied to build the isoform sequence: VSP_018742.

TISSUE SPECIFICITY: Expressed very intensively in the testis and weakly in lung, heart, and cerebellum.
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

AB121012; BAE17020.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q4AEH0; 36-197.

ModBase

Q4AEH0.

Protein family/group databases

PeroxiBase

3708; MfGPx04.

Ontologies

GO:0047066;	Molecular function: phospholipid-hydroperoxide glutathione peroxidase activity (inferred from electronic annotation from EC).
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.

PROSITE

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

BLOCKS

Q4AEH0.

Phylogenomic databases

HOVERGEN

Q4AEH0; -.

Other

ProtoNet

Q4AEH0.

UniRef

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

Keywords

Alternative initiation; Cytoplasm; Developmental protein; Mitochondrion; Oxidoreductase; Peroxidase; Selenium; Selenocysteine; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 197`		`Phospholipid hydroperoxide glutathione peroxidase, mitochondrial.`	`PRO_0000042611`
`ACT_SITE`	`73 73`		`By similarity.`
`NON_STD`	`73 73`		`Selenocysteine.`
`VAR_SEQ`	`1 27`		`Missing (in isoform Cytoplasmic).`	`VSP_018742`

Sequence information

Length: 197 AA [This is the length of the unprocessed precursor]

Molecular weight: 22187 Da [This is the MW of the unprocessed precursor]

CRC64: D2C65F9DADAC0098 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNLGRLCRLL KPALLCGALA APGLAGTMCA SRDDWRCARS MHEFSAKDID GHMVNLDKYR 

        70         80         90        100        110        120 
GFVCIVTNVA SQUGKTEVNY TQLVDLHARY AECGVRILAF PCNQFGKQEP GSNEKIKEFA 

       130        140        150        160        170        180 
AGYNVKFDMF SKICVNGDDA HPLWKWMKIQ PKGKGILGNA IKWNFTKFLI DKNGCVVKRY 

       190 
GPMEEPLVIE KDLPHYF

Q4AEH0 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