[1]	NUCLEOTIDE SEQUENCE [MRNA]. Drevet J.R., Gagne G., Tourvieille de Labrouhe D., Nicolas P., Dufaure J.-P., Ledoigt G., Roeckel-Drevet P.; Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H₂O.
SUBCELLULAR LOCATION: Cytoplasm (Potential).
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

Y14707; CAA75009.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T12633; T12633.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

O23968.

Protein family/group databases

PeroxiBase

2650; HaGPx06-1.

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).

Other

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

Keywords

Cytoplasm; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 180`	`180`	`Probable phospholipid hydroperoxide glutathione peroxidase.`	`PRO_0000066630`
`ACT_SITE`	`54 54`		`By similarity.`

Sequence information

Length: 180 AA [This is the length of the unprocessed precursor]

Molecular weight: 20174 Da [This is the MW of the unprocessed precursor]

CRC64: E33090EAAD2AADE0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATQTVFDFP DDVLQQPPMP ADNAFSDKDV KGQDVELSKY KGKVLLIVNV ASQCGFTNSN 

        70         80         90        100        110        120 
YPELTTLYQK YKDQGFEILA FPCNQFGGQE PGSNEEIQVF ACTRFKAEYP VFSKVNVNGK 

       130        140        150        160        170        180 
EADPLYKFLK SSKGGFLGDS IKWNFTKFLV DREGKVVDRY APTTSPLSIE KDIKKLLNVA

O23968 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