NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Liver;
DOI=10.1111/j.1600-0684.2006.00158.x; PubMed=16764674 [NCBI, ExPASy, EBI, Israel, Japan]
Atanasova S., von Ahsen N., Schlumbohm C., Wieland E., Oellerich M., Armstrong V.;
"Marmoset glutathione peroxidases: cDNA sequences, molecular evolution, and gene expression.";
J. Med. Primatol. 35:155-164(2006).

Comments

FUNCTION: Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H₂O.
SUBCELLULAR LOCATION: Mitochondrion (By similarity). Cytoplasm (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.

Name	Mitochondrial
Isoform ID	Q32QL6-1
This is the isoform sequence displayed in this entry.

Name	Cytoplasmic
Isoform ID	Q32QL6-2
Features which should be applied to build the isoform sequence: VSP_031257.

TISSUE SPECIFICITY: Expressed in testis. Also expressed in liver, lung, kidney and spinal cord.
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

AY966404; AAY33855.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q32QL6; 36-197.

ModBase

Q32QL6.

Ontologies

GO:0047066;	Molecular function: phospholipid-hydroperoxide glutathione peroxidase activity (inferred from electronic annotation from EC).
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.

PROSITE

PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q32QL6.

Phylogenomic databases

HOVERGEN

Q32QL6; -.

Other

ProtoNet

Q32QL6.

UniRef

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

Keywords

Alternative initiation; Cytoplasm; Developmental protein; Mitochondrion; Oxidoreductase; Peroxidase; Selenium; Selenocysteine; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 197`		`Phospholipid hydroperoxide glutathione peroxidase, mitochondrial.`	`PRO_0000318641`
`ACT_SITE`	`73 73`		`By similarity.`
`NON_STD`	`73 73`		`Selenocysteine.`
`VAR_SEQ`	`1 27`		`Missing (in isoform Cytoplasmic).`	`VSP_031257`

Sequence information

Length: 197 AA [This is the length of the unprocessed precursor]

Molecular weight: 22054 Da [This is the MW of the unprocessed precursor]

CRC64: 76B48360040EF055 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLGRLCRLL KPALLCGALA APGLAGTMCA SQDDWRSARS MHEFSAKDID GHTVNLDKYR 

        70         80         90        100        110        120 
GFVCIVTNVA SQUGKTQVNY TQLVDLHARY AECGLRILAF PCNQFGKQEP GSNEEIKEFA 

       130        140        150        160        170        180 
AGYNVKFDMF SKICVNGDDA HPLWKWMKIQ PKGKGTLGNA IKWNFTKFLV DKNGCVVKRY 

       190 
GPMEEPQVIE KDLPCYF

Q32QL6 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