[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=CD-1; TISSUE=Testis; DOI=10.1016/S0378-1119(97)00321-1; PubMed=9370288 [NCBI, ExPASy, EBI, Israel, Japan] Nam S.-Y., Nakamuta N., Kurohmaru M., Hayashi Y.; "Cloning and sequencing of the cDNA encoding a phospholipid hydroperoxide glutathione peroxidase."; Gene 198:245-249(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=C57BL/6N; DOI=10.1016/S0014-5793(99)00221-5; PubMed=10100845 [NCBI, ExPASy, EBI, Israel, Japan] Borchert A., Schnurr K., Thiele B.J., Kuehn H.; "Cloning of the mouse phospholipid hydroperoxide glutathione peroxidase gene."; FEBS Lett. 446:223-227(1999).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. STRAIN=BALB/c, and C57BL/6J; TISSUE=Myocardium, and Testis; DOI=10.1007/s003359901053; PubMed=10341094 [NCBI, ExPASy, EBI, Israel, Japan] Knopp E.A., Arndt T.L., Eng K.L., Caldwell M., LeBoeuf R.C., Deeb S.S., O'Brien K.D.; "Murine phospholipid hydroperoxide glutathione peroxidase: cDNA sequence, tissue expression, and mapping."; Mamm. Genome 10:601-605(1999).
[4]	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).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=C57BL/6J; TISSUE=Testis; DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan] Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; "The transcriptional landscape of the mammalian genome."; Science 309:1559-1563(2005).
[6]	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.
CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H₂O.
SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing and alternative initiation.

Name	Mitochondrial
Isoform ID	O70325-1
This is the isoform sequence displayed in this entry.

Name	Nuclear
Isoform ID	Q91XR9-1
This isoform is stored in UniProtKB/Swiss-Prot entry Q91XR9.

Name	Cytoplasmic
Isoform ID	O70325-2
Note: Produced by alternative initiation at Met-28 of isoform Mitochondrial.
Features which should be applied to build the isoform sequence: VSP_018743.

TISSUE SPECIFICITY: Present primarily in testis.
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

D87896; BAA22780.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ012104; CAB42657.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045768; AAC15832.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045769; AAC15833.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF044056; AAC14560.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030643; BAC06507.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030643; BAC06508.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030728; BAC06511.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK006441; BAC55251.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_032188.3; -.

UniGene

Mm.359573

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

SMR

O70325; 36-197.

ModBase

O70325.

Protein family/group databases

PeroxiBase

3714; MmGPx04-a.
3867; MmGPx04-c.

Organism-specific databases

MGI

MGI:104767; Gpx4.

Gene expression databases

CleanEx

MM_GPX4; -.

GermOnline

ENSMUSG00000065948; 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:0047066;	Molecular function: phospholipid-hydroperoxide glutathione peroxidase activity (inferred from electronic annotation from EC).
GO:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006325;	Biological process: establishment or maintenance of chromatin architecture (inferred from direct assay from MGI).
GO:0007275;	Biological process: multicellular organismal development (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).
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.

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).

Genome annotation databases

Ensembl

ENSMUSG00000075706; Mus musculus. [Contig view]

GeneID

625249; -.

Phylogenomic databases

HOGENOM

O70325; -.

HOVERGEN

O70325; -.

Other

418158; -.

Gpx4; Mus musculus.

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

Keywords

Alternative initiation; Alternative splicing; 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_0000013069`
`ACT_SITE`	`73 73`
`NON_STD`	`73 73`		`Selenocysteine.`
`VAR_SEQ`	`1 27`		`Missing (in isoform Cytoplasmic).`	`VSP_018743`
`CONFLICT`	`39 39`		`R -> A (in Ref. 1; BAA22780).`

Sequence information

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

Molecular weight: 22229 Da [This is the MW of the unprocessed precursor]

CRC64: 5CED4991A484F31C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSWGRLSRLL KPALLCGALA APGLAGTMCA SRDDWRCARS MHEFSAKDID GHMVCLDKYR 

        70         80         90        100        110        120 
GFVCIVTNVA SQUGKTDVNY TQLVDLHARY AECGLRILAF PCNQFGRQEP GSNQEIKEFA 

       130        140        150        160        170        180 
AGYNVKFDMY SKICVNGDDA HPLWKWMKVQ PKGRGMLGNA IKWNFTKFLI DKNGCVVKRY 

       190 
GPMEEPQVIE KDLPCYL

O70325 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