[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Epididymis; PubMed=1913244 [NCBI, ExPASy, EBI, Israel, Japan] Ghyselinck N.B., Rigaudiere N., Dufaure J.-P.; "Androgen-dependent protein secreted by mouse caput epididymis shows high homologies with different glutathione peroxidases."; C. R. Acad. Sci. III, Sci. Vie 313:1-6(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1210/me.7.2.258; PubMed=8469239 [NCBI, ExPASy, EBI, Israel, Japan] Ghyselinck N.B., Dufaure I., Lareyre J.J., Rigaudiere N., Mattei M.-G., Dufaure J.-P.; "Structural organization and regulation of the gene for the androgen-dependent glutathione peroxidase-like protein specific to the mouse epididymis."; Mol. Endocrinol. 7:258-272(1993).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 47-221. TISSUE=Epididymis; DOI=10.1093/nar/18.23.7144; PubMed=2263479 [NCBI, ExPASy, EBI, Israel, Japan] Ghyselinck N.B., Dufaure J.-P.; "A mouse cDNA sequence for epididymal androgen-regulated proteins related to glutathione peroxidase."; Nucleic Acids Res. 18:7144-7144(1990).

Comments

FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathionine peroxidase-like protective system against peroxide damage in sperm membrane lipids.
CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Epididymis.
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

M68896; AAA37729.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X53780; CAA37796.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A47367; A47367.

UniGene

Mm.1332

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

P21765.

Protein family/group databases

PeroxiBase

5578; MmGPx05.

Organism-specific databases

MGI

MGI:104886; Gpx5.

Gene expression databases

ArrayExpress

P21765; -.

CleanEx

MM_GPX5; -.

GermOnline

ENSMUSG00000004344; Mus musculus.

Ontologies

GO:0005576;	Cellular component: extracellular region (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).

ProtoNet

P21765.

Genome annotation databases

Ensembl

ENSMUSG00000004344; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P21765; -.

HOVERGEN

P21765; -.

Other

SOURCE

Gpx5; Mus musculus.

UniRef

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

Keywords

Oxidoreductase; Peroxidase; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`CHAIN`	`22 221`	`200`	`Epididymal secretory glutathione peroxidase.`	`PRO_0000013078`
`ACT_SITE`	`73 73`		`By similarity.`
`CONFLICT`	`53 53`		`D -> H (in Ref. 3; CAA37796).`
`CONFLICT`	`103 103`		`Q -> E (in Ref. 2).`
`CONFLICT`	`170 170`		`S -> F (in Ref. 2).`

Sequence information

Length: 221 AA [This is the length of the unprocessed precursor]

Molecular weight: 25382 Da [This is the MW of the unprocessed precursor]

CRC64: DE5F8BD6CD22D6F9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVTELRVFYL VPLLLASYVQ TTPRPEKMKM DCYKDVKGTI YDYEALSLNG KEDIPFKQYR 

        70         80         90        100        110        120 
GKHVLFVNVA TYCGLTIQYP ELNALQEDLK PFGLVILGFP CNQFGKQEPG DNLEILPGLK 

       130        140        150        160        170        180 
YVRPGKGFLP NFQLFAKGDV NGENEQKIFT FLKRSCPHPS ETVVMSKHTS WEPIKVHDIR 

       190        200        210        220 
WNFEKFLVGP DGVPVMRWFH QAPVSTVKSD IMAYLSHFKT I

P21765 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