[1]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-87. STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion; Xiao H.S., Han Z.G., Zhang F.X., Huang Q.H., Lu Y.J., Bao L., Fu G., Guo C., Yan Q., Jin S.X., Zhu Z.D., Xu X.R., Li N.G., Chen Z., Zhang X.; "Distinct gene expression profiles of rat dorsal root ganglion induced by peripheral nerve axotomy."; Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-190. STRAIN=Sprague-Dawley; TISSUE=Ileum; PubMed=8889548 [NCBI, ExPASy, EBI, Israel, Japan] Bonaldo M.F., Lennon G., Soares M.B.; "Normalization and subtraction: two approaches to facilitate gene discovery."; Genome Res. 6:791-806(1996).
[3]	PROTEIN SEQUENCE OF 7-27; 91-101; 121-138; 140-168 AND 175-181, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. STRAIN=CD Charles River; TISSUE=Gastrointestinal tract epithelium; DOI=10.1016/S0304-4165(98)00032-4; PubMed=9685647 [NCBI, ExPASy, EBI, Israel, Japan] Esworthy R.S., Swiderek K.M., Ho Y.-S., Chu F.-F.; "Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine."; Biochim. Biophys. Acta 1381:213-226(1998).

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
TISSUE SPECIFICITY: Mucosal epithelium of the gastrointestinal tract.
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

BG664050; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]
BQ196649; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

UniGene

Rn.3503

3D structure databases

SMR

P83645; 4-187.

ModBase

P83645.

Protein family/group databases

PeroxiBase

3731; RnoGPx02.

Organism-specific databases

RGD

727780; Gpx2.

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:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
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).

ProtoNet

P83645.

Genome annotation databases

Ensembl

ENSRNOG00000038455; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P83645; -.

Other

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 190`	`190`	`Glutathione peroxidase 2.`	`PRO_0000066624`
`ACT_SITE`	`40 40`		`By similarity.`
`NON_STD`	`40 40`		`Selenocysteine.`
`CONFLICT`	`91 91`		`H -> P (in Ref. 3; AA sequence).`

Sequence information

Length: 190 AA [This is the length of the unprocessed precursor]

Molecular weight: 22014 Da [This is the MW of the unprocessed precursor]

CRC64: 9A69384CBEF81E70 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAYIAKSFYD LSAIGLDGEK IDFNTFRGRA VLIENVASLU GTTTRDYTQL NELQCRFPRR 

        70         80         90        100        110        120 
LVVLGFPCNQ FGHQENCQNE EILNSLKYVR HGGGFQPTFS LTQKCDVNGQ NQHPVFAYLK 

       130        140        150        160        170        180 
DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV SWNFEKFLIG PEGEPFRRYS RTFQTINIEP 

       190 
DIKRLLKVAI

P83645 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