[1]	NUCLEOTIDE SEQUENCE [MRNA]. Hara S., Imura N.; "Bovine phospholipid hydroperoxide glutathione peroxidase."; Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.

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	Q9N2J2-1
This is the isoform sequence displayed in this entry.

Name	Cytoplasmic
Isoform ID	Q9N2J2-2
Features which should be applied to build the isoform sequence: VSP_018738.

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

AB017534; BAA86034.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777195.1; -.

UniGene

Bt.49234

3D structure databases

SMR

Q9N2J2; 36-197.

ModBase

Q9N2J2.

Protein family/group databases

PeroxiBase

3637; BtGPx04-a.

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

Q9N2J2.

Genome annotation databases

Ensembl

ENSBTAG00000020778; Bos taurus. [Contig view]

GeneID

286809; -.

KEGG

bta:286809; -.

Phylogenomic databases

HOVERGEN

Q9N2J2; -.

Other

ProtoNet

Q9N2J2.

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_0000013065`
`ACT_SITE`	`73 73`		`By similarity.`
`NON_STD`	`73 73`		`Selenocysteine.`
`VAR_SEQ`	`1 27`		`Missing (in isoform Cytoplasmic).`	`VSP_018738`

Sequence information

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

Molecular weight: 22240 Da [This is the MW of the unprocessed precursor]

CRC64: 3C05FF92C4AA8824 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFSRLYRLL KPALLCGALA APGLASTMCA SRDDWRCARS MHEFSAKDID GRMVNLDKYR 

        70         80         90        100        110        120 
GHVCIVTNVA SQUGKTDVNY TQLVDLHARY AECGLRILAF PCNQFGRQEP GSNAEIKEFA 

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

       190 
GPMEEPLVIE KDLPCYL

Q9N2J2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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