NUCLEOTIDE SEQUENCE [MRNA], SELENOCYSTEINE AT SEC-75, AND MASS SPECTROMETRY.
STRAIN=2137;
DOI=10.1074/jbc.M202912200; PubMed=11973339 [NCBI, ExPASy, EBI, Israel, Japan]
Fu L.-H., Wang X.-F., Eyal Y., She Y.-M., Donald L.J., Standing K.G., Ben-Hayyim G.;
"A selenoprotein in the plant kingdom. Mass spectrometry confirms that an opal codon (UGA) encodes selenocysteine in Chlamydomonas reinhardtii glutathione peroxidase.";
J. Biol. Chem. 277:25983-25991(2002).

Comments

CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBCELLULAR LOCATION: Mitochondrion (Probable).
MASS SPECTROMETRY: Mass=18496; Method=MALDI; Range=28-201; Source=PubMed:11973339;.
MASS SPECTROMETRY: Mass=18571; Method=Electrospray; Range=28-201; Source=PubMed:11973339;.
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

AY051144; AAL14348.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001701658.1; -.

UniGene

Cre.4579

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

P83564.

Protein family/group databases

PeroxiBase

2590; CreGPx02.

Ontologies

GO:0005739;	Cellular component: mitochondrion (non-traceable author statement from UniProtKB).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from direct assay from UniProtKB).
GO:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from direct assay 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).

ProtoNet

P83564.

Genome annotation databases

GeneID

5727250; -.

KEGG

cre:CHLREDRAFT_206090; -.

Other

UniRef

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

Keywords

Mitochondrion; Oxidoreductase; Peroxidase; Selenium; Selenocysteine; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 27`	`27`	`Mitochondrion (Potential).`
`CHAIN`	`28 201`	`174`	`Glutathione peroxidase, mitochondrial.`	`PRO_0000013089`
`NON_STD`	`75 75`		`Selenocysteine.`

Sequence information

Length: 201 AA [This is the length of the unprocessed precursor]

Molecular weight: 21499 Da [This is the MW of the unprocessed precursor]

CRC64: 1030F45EBA62C219 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLLTRKNVAV RPARAARRDV RAMSLLGNLF GGGSKPTSST SNFHQLSALD IDKKNVDFKS 

        70         80         90        100        110        120 
LNNRVVLVVN VASKUGLTAA NYKEFATLLG KYPATDLTIV AFPCNQFGGQ EPGTNAEIKA 

       130        140        150        160        170        180 
FASARGFSGA GALLMDKVDV NGANASPVYN FLKVAAGDTS DIGWNFGKFL VRPDGTVFGR 

       190        200 
YAPTTGPLSL EKYIVELINS R

P83564 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