NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
TISSUE=Epididymis;
PubMed=1386734 [NCBI, ExPASy, EBI, Israel, Japan]
Perry A.C.F., Jones R., Niang L.S.P., Jackson R.M., Hall L.;
"Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon.";
Biochem. J. 285:863-870(1992).

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

X62404; CAA44274.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S24328; S24328.

NP_001099208.1; -.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

P30710.

Protein family/group databases

PeroxiBase

3735; RnoGPx05.

Organism-specific databases

RGD

69227; Gpx5.

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).

Genome annotation databases

GeneID

113919; -.

KEGG

rno:113919; -.

Phylogenomic databases

HOVERGEN

P30710; -.

Other

NextBio

618026; -.

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_0000013080`
`ACT_SITE`	`73 73`		`By similarity.`

Sequence information

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

Molecular weight: 25385 Da [This is the MW of the unprocessed precursor]

CRC64: 0D9D3FAAC9F12D16 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIQLRVFYL VPLLLASYVQ TTPRLEKMKM DCYKDVKGTI YNYEALSLNG KERIPFKQYA 

        70         80         90        100        110        120 
GKHVLFVNVA TYCGLTIQYP ELNALQDDLK QFGLVILGFP CNQFGKQEPG DNTEILPGLK 

       130        140        150        160        170        180 
YVRPGKGFLP NFQLFAKGDV NGEKEQEIFT FLKRSCPHPS ETVVTSKHTF WEPIKVHDIR 

       190        200        210        220 
WNFEKFLVGP NGVPVMRWFH QAPVSTVKSD ILAYLNQFKT I

P30710 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