[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/j.cbpc.2005.05.002; PubMed=15967696 [NCBI, ExPASy, EBI, Israel, Japan] Fukuhara R., Kageyama T.; "Structure, gene expression, and evolution of primate glutathione peroxidases."; Comp. Biochem. Physiol. 141B:428-436(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; The German cDNA consortium; Submitted (MAR-2005) 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 + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Secreted in plasma.
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

AB121006; BAE17014.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR857195; CAH89494.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q5RFG3.

Protein family/group databases

PeroxiBase

3727; PpyGPx03.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from sequence or structural similarity from UniProtKB).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008430;	Molecular function: selenium binding (inferred from sequence or structural similarity from UniProtKB).
GO:0051289;	Biological process: protein homotetramerization (inferred from sequence or structural similarity from UniProtKB).
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

Q5RFG3.

Phylogenomic databases

HOVERGEN

Q5RFG3; -.

Other

ProtoNet

Q5RFG3.

UniRef

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

Keywords

Oxidoreductase; Peroxidase; Secreted; Selenium; Selenocysteine; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`CHAIN`	`25 226`	`202`	`Glutathione peroxidase 3.`	`PRO_0000042615`
`ACT_SITE`	`73 73`		`By similarity.`
`NON_STD`	`73 73`		`Selenocysteine.`

Sequence information

Length: 226 AA [This is the length of the unprocessed precursor]

Molecular weight: 25562 Da [This is the MW of the unprocessed precursor]

CRC64: D7F77A1692493D98 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARLLQASCL LSLLLAGFVP QSRGQEKSKM DCHGGISGTI YEYGALTIDG EEYIPFKQYA 

        70         80         90        100        110        120 
GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP CNQFGKQEPG ENSEILPTLK 

       130        140        150        160        170        180 
YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR 

       190        200        210        220 
WNFEKFLVGP DGIPIMRWHH RTTVSNVKMD ILSYMRRQAA LGVKRK

Q5RFG3 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