[1]	NUCLEOTIDE SEQUENCE [MRNA]. Venkatakrishnaiah L., James E.; Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. DOI=10.1006/expr.1998.4217; PubMed=9501847 [NCBI, ExPASy, EBI, Israel, Japan] Tripp C.A., Frank R.S., Selkirk M.E., Tang L., Mika-Grieve M., Frank G.R., Grieve R.B.; "Dirofilaria immitis: molecular cloning and expression of a cDNA encoding a selenium-independent secreted glutathione peroxidase."; Exp. Parasitol. 88:43-50(1998).

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Secreted, extracellular space (By similarity).
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

U04693; AAA16224.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U87457; AAB58573.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U87458; AAB58574.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

P52033.

Protein family/group databases

PeroxiBase

3752; DiGPx01.

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).

Other

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

Keywords

Glycoprotein; Oxidoreductase; Peroxidase; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`CHAIN`	`20 221`	`202`	`Glutathione peroxidase.`	`PRO_0000013094`
`ACT_SITE`	`72 72`		`By similarity.`
`CARBOHYD`	`28 28`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`87 87`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`90 90`		`N-linked (GlcNAc...) (Potential).`

Sequence information

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

Molecular weight: 25453 Da [This is the MW of the unprocessed precursor]

CRC64: 88FFF848D567CF28 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFIQLLILSY AILLQLIATQ VADKQLPNLT KQCEPTSQTI YDFHVPTLDG SEKSLAEYRG 

        70         80         90        100        110        120 
KVLLLVNVAT YCAYTFQYND FNPMLENNSN GTLKILAFPC NQFLLQEPAE NHELLNGLKY 

       130        140        150        160        170        180 
VRPGNGWEPH GNMHIFGKVE VNGDDHHPLY KFLKEHCPQT VPIIGDRHQL MYNPIGTNDI 

       190        200        210        220 
IWNFEKFLID KKGHPRYRFH PSAWVQGSVI APFIDELERE I

P52033 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