[1]	NUCLEOTIDE SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. TISSUE=Testis; PubMed=11344099 [NCBI, ExPASy, EBI, Israel, Japan] Pfeifer H., Conrad M., Roethlein D., Kyriakopoulos A., Brielmeier M., Bornkamm G.W., Behne D.; "Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation."; FASEB J. 15:1236-1238(2001).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=129/SvJ; TISSUE=Liver; DOI=10.1016/S0006-291X(03)00734-4; PubMed=12745070 [NCBI, ExPASy, EBI, Israel, Japan] Imai H., Hirao F., Sakamoto T., Sekine K., Mizukura Y., Saito M., Kitamoto T., Hayasaka M., Hanaoka K., Nakagawa Y.; "Early embryonic lethality caused by targeted disruption of the mouse PHGPx gene."; Biochem. Biophys. Res. Commun. 305:278-286(2003).
[3]	FUNCTION. DOI=10.1016/S0891-5849(02)01360-6; PubMed=12566075 [NCBI, ExPASy, EBI, Israel, Japan] Yant L.J., Ran Q., Rao L., Van Remmen H., Shibatani T., Belter J.G., Motta L., Richardson A., Prolla T.A.; "The selenoprotein GPX4 is essential for mouse development and protects from radiation and oxidative damage insults."; Free Radic. Biol. Med. 34:496-502(2003).

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. Stabilizes the condensed chromatin in sperm nuclei and is necessary for male fertility.
CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H₂O.
SUBCELLULAR LOCATION: Nucleus.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name Nuclear

Isoform ID Q91XR9-1

This is the isoform sequence displayed in this entry.

Name Mitochondrial

Isoform ID O70325-1

This isoform is stored in UniProtKB/Swiss-Prot entry O70325.
TISSUE SPECIFICITY: Expressed exclusively in sperm.
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

AF274027; AAK74112.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030643; BAC06509.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001032830.2; -.

UniGene

Mm.359573

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

SMR

Q91XR9; 92-253.

ModBase

Q91XR9.

Protein family/group databases

PeroxiBase

3865; MmGPx04-b.

Organism-specific databases

MGI

MGI:104767; Gpx4.

Gene expression databases

CleanEx

MM_GPX4; -.

GermOnline

ENSMUSG00000075706; Mus musculus.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from MGI).
GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
GO:0005635;	Cellular component: nuclear envelope (inferred from direct assay from MGI).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from direct assay from MGI).
GO:0006325;	Biological process: establishment and/or maintenance of chromatin architecture (inferred from direct assay from MGI).
GO:0007283;	Biological process: spermatogenesis (inferred from direct assay from MGI).
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.

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

Q91XR9.

Genome annotation databases

Ensembl

ENSMUSG00000075706; Mus musculus. [Contig view]

GeneID

625249; -.

KEGG

mmu:625249; -.

Phylogenomic databases

HOGENOM

Q91XR9; -.

HOVERGEN

Q91XR9; -.

Other

Gpx4; Mus musculus.

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

Keywords

Alternative splicing; Developmental protein; Nucleus; Oxidoreductase; Peroxidase; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 253`	`253`	`Phospholipid hydroperoxide glutathione peroxidase, nuclear.`	`PRO_0000066625`
`ACT_SITE`	`129 129`		`By similarity.`
`NON_STD`	`129 129`		`Selenocysteine (By similarity).`

Sequence information

Length: 253 AA [This is the length of the unprocessed precursor]

Molecular weight: 29252 Da [This is the MW of the unprocessed precursor]

CRC64: C55E282753231653 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGRAAARKRG RCRQRGGSPR GRRRRGPGRQ SPRKRPGPRR RKARARRRRR ARPRRMEPIP 

        70         80         90        100        110        120 
EPFNPGPLLQ EPPQYCNSSE FLGLCASRDD WRCARSMHEF SAKDIDGHMV CLDKYRGFVC 

       130        140        150        160        170        180 
IVTNVASQUG KTDVNYTQLV DLHARYAECG LRILAFPCNQ FGRQEPGSNQ EIKEFAAGYN 

       190        200        210        220        230        240 
VKFDMYSKIC VNGDDAHPLW KWMKVQPKGR GMLGNAIKWN FTKFLIDKNG CEVKRYGPME 

       250 
EPQVIERDLP CYL

Q91XR9 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