NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan]
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating biology.";
Science 282:2012-2018(1998).

Comments

FUNCTION: May constitute a glutathionine peroxidase-like protective system against oxidative stresses (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 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

Z81070; CAB03004.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T21418; T21418.

NP_492598.1; -.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

O02621.

Protein family/group databases

PeroxiBase

3746; CelGPx01.

Organism-specific databases

WormBase

WBGene00009165; F26E4.12.

WormPep

F26E4.12; CE09696. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

O02621; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
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).

Genome annotation databases

Ensembl

F26E4.12; Caenorhabditis elegans. [Contig view]

GeneID

184981; -.

KEGG

cel:F26E4.12; -.

NMPDR

fig|6239.3.peg.2617; -.

Other

926638; -.

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

Keywords

Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 163`	`163`	`Probable glutathione peroxidase F26E4.12.`	`PRO_0000066646`
`ACT_SITE`	`36 36`		`By similarity.`

Sequence information

Length: 163 AA [This is the length of the unprocessed precursor]

Molecular weight: 18424 Da [This is the MW of the unprocessed precursor]

CRC64: 441535A92DC4330F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSVYDFNVK NANGDDVSLS DYKGKVLIIV NVASQCGLTN KNYTQLKELL DVYKKDGLEV 

        70         80         90        100        110        120 
LAFPCNQFAG QEPSCEIDIQ AFVADKFKFE PTLFQKIDVN GDKQSPLFKF LKNEKGGFMF 

       130        140        150        160 
DAIKWNFTKF LVGRDGKIIK RFGPTTDPKD MEKDIKEALG EKL

O02621 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