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

Z83119; CAB05581.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T23936; T23936.

NP_497078.1; -.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

O62327.

Protein family/group databases

PeroxiBase

3747; CelGPx02.

Organism-specific databases

WormBase

WBGene00011045; R05H10.5.

WormPep

R05H10.5; CE18107. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

O62327; -.

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

R05H10.5; Caenorhabditis elegans. [Contig view]

GeneID

187630; -.

KEGG

cel:R05H10.5; -.

NMPDR

fig|6239.3.peg.8304; -.

Other

935924; -.

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 R05H10.5.`	`PRO_0000066647`
`ACT_SITE`	`36 36`		`By similarity.`

Sequence information

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

Molecular weight: 18152 Da [This is the MW of the unprocessed precursor]

CRC64: 8D5FE6DF96D212CA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASVHGITVK NAQGEDTPLS NYQGKVLIIV NVASQCGLTN SNYNQFKELL DVYKKDGLEV 

        70         80         90        100        110        120 
LAFPCNQFGG QEPSCEIDIA AFVADKFKFE PTLFQKIDVN GDNTAPLYKF LKQEKGGFLV 

       130        140        150        160 
DAIKWNFTKF LVGRDGHVIK RFSPTTEPKD MKKDIEAALQ AKL

O62327 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