[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Testis; DOI=10.1074/jbc.270.45.26993; PubMed=7592947 [NCBI, ExPASy, EBI, Israel, Japan] Pushpa-Rekha T.R., Burdsall A.L., Oleksa L.M., Chisolm G.M., Driscoll D.M.; "Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites."; J. Biol. Chem. 270:26993-26999(1995).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Wistar; Maiorino M., Scapin M., Ursini F., Biasolo M., Bosello V., Flohe L.; "Distinct promoters determine alternative transcription of gpx-4 into PHGPx variants."; Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 17-197. STRAIN=Sprague-Dawley; TISSUE=Brain; PubMed=8749327 [NCBI, ExPASy, EBI, Israel, Japan] Imai H., Sumi D., Hanamoto A., Arai M., Sugiyama A., Chiba N., Kuchino Y., Nakagawa Y.; "Molecular cloning and functional expression of a cDNA for rat phospholipid hydroperoxide glutathione peroxidase: 3'-untranslated region of the gene is necessary for functional expression."; J. Biochem. 118:1061-1067(1995).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 21-197. STRAIN=Sprague-Dawley; TISSUE=Liver; Sunde R.A., Dyer J.A., Moran T.V., Evenson J.K.; "Rat liver phospholipid hydroperoxide glutathione peroxidase."; Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
[5]	CHARACTERIZATION. TISSUE=Testis; PubMed=1556123 [NCBI, ExPASy, EBI, Israel, Japan] Roveri A., Casasco A., Maiorino M., Dalan P., Calligaro A., Ursini F.; "Phospholipid hydroperoxide glutathione peroxidase of rat testis. Gonadotropin dependence and immunocytochemical identification."; J. Biol. Chem. 267:6142-6146(1992).

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. Cytoplasm.

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

Name	Mitochondrial
Isoform ID	P36970-1
This is the isoform sequence displayed in this entry.

Name	Nuclear
Isoform ID	Q91XR8-1
This isoform is stored in UniProtKB/Swiss-Prot entry Q91XR8.

Name	Cytoplasmic
Isoform ID	P36970-2
Note: Produced by alternative initiation at Met-28 of isoform Mitochondrial.
Features which should be applied to build the isoform sequence: VSP_018746.

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

U37427; AAC52503.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ537598; CAD61276.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ537598; CAD61277.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X82679; CAA57996.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L24896; AAA41842.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JC4332; JC4332.

NP_058861.3; -.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

SMR

P36970; 36-197.

ModBase

P36970.

Protein family/group databases

PeroxiBase

3733; RnoGPx04-a.
3812; RnoGPx04-b.

Organism-specific databases

RGD

69226; Gpx4.

Gene expression databases

ArrayExpress

P36970; -.

Ontologies

GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
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: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).
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).

ProtoNet

P36970.

Genome annotation databases

Ensembl

ENSRNOG00000013604; Rattus norvegicus. [Contig view]

GeneID

29328; -.

Phylogenomic databases

HOVERGEN

P36970; -.

Other

NextBio

608793; -.

UniRef

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_0000013073`
`ACT_SITE`	`73 73`
`NON_STD`	`73 73`		`Selenocysteine.`
`VAR_SEQ`	`1 27`		`Missing (in isoform Cytoplasmic).`	`VSP_018746`
`CONFLICT`	`45 45`		`A -> S (in Ref. 1; AAC52503 and 2; CAD61276/CAD61277).`

Sequence information

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

Molecular weight: 22225 Da [This is the MW of the unprocessed precursor]

CRC64: 83FF001A5A42F814 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSWGRLSRLL KPALLCGALA VPGLAGTMCA SRDDWRCARS MHEFAAKDID GHMVCLDKYR 

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

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

       190 
GPMEEPQVIE KDLPCYL

P36970 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