[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1006/bbrc.1993.1711; PubMed=8323565 [NCBI, ExPASy, EBI, Israel, Japan] Sunde R.A., Dyer J.A., Moran T., Evenson J.K., Sugimoto M.; "Phospholipid hydroperoxide glutathione peroxidase: full-length pig blastocyst cDNA sequence and regulation by selenium status."; Biochem. Biophys. Res. Commun. 193:905-911(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Heart, and Liver; PubMed=8125951 [NCBI, ExPASy, EBI, Israel, Japan] Brigelius-Flohe R., Aumann K.-D., Bloecker H., Gross G., Kloeppel K.-D., Maiorino M., Roveri A., Schuckelt R., Ursini F., Wingender E., Flohe L.; "Phospholipid-hydroperoxide glutathione peroxidase. Genomic DNA, cDNA, and deduced amino acid sequence."; J. Biol. Chem. 269:7342-7348(1994).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 40-197, AND PARTIAL PROTEIN SEQUENCE. TISSUE=Heart; PubMed=1778506 [NCBI, ExPASy, EBI, Israel, Japan] Schuckelt R., Brigelius-Flohe R., Maiorino M., Roveri A., Reumkens J., Strassburger W., Ursini F., Wolf B., Flohe L.; "Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme distinct from the classical glutathione peroxidase as evident from cDNA and amino acid sequencing."; Free Radic. Res. Commun. 14:343-361(1991).

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.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.

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

Name	Mitochondrial
Isoform ID	P36968-1
This is the isoform sequence displayed in this entry.

Name	Cytoplasmic
Isoform ID	P36968-2
Features which should be applied to build the isoform sequence: VSP_018744.

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

L12743; AAA31099.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L12743; AAA31098.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X76009; CAA53596.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X76008; CAA53595.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S80257; AAB21327.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JN0608; JN0608.

NP_999572.1; -.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

SMR

P36968; 36-197.

ModBase

P36968.

Protein family/group databases

PeroxiBase

3723; SscGPx04.

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.

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

P36968.

Genome annotation databases

GeneID

399537; -.

KEGG

ssc:399537; -.

Phylogenomic databases

HOVERGEN

P36968; -.

Other

ProtoNet

P36968.

UniRef

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

Keywords

Alternative initiation; Cytoplasm; Developmental protein; Direct protein sequencing; 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_0000013071`
`ACT_SITE`	`73 73`
`NON_STD`	`73 73`		`Selenocysteine.`
`VAR_SEQ`	`1 27`		`Missing (in isoform Cytoplasmic).`	`VSP_018744`

Sequence information

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

Molecular weight: 22337 Da [This is the MW of the unprocessed precursor]

CRC64: 34865B0BEBFA69D0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFSRLFRLL KPTLLCGTLA VPGLAGTMCA SRDDWRCARS MHEFSAKDID GHMVNLDKYR 

        70         80         90        100        110        120 
GYVCIVTNVA SQUGKTEVNY TQLVDLHARY AECGLRILAF PCNQFGRQEP GSDAEIKEFA 

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

       190 
GPMEEPQVIE KDLPCYL

P36968 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