NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1007/BF00027124; PubMed=8467085 [NCBI, ExPASy, EBI, Israel, Japan]
Holland D., Ben-Hayyim G., Faltin Z., Camoin L., Strosberg A.D., Eshdat Y.;
"Molecular characterization of salt-stress-associated protein in citrus: protein and cDNA sequence homology to mammalian glutathione peroxidases.";
Plant Mol. Biol. 21:923-927(1993).

Comments

FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H₂O.
SUBCELLULAR LOCATION: Cytoplasm (Potential).
INDUCTION: By salt stress.
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

X66377; CAA47018.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33618; S33618.

3D structure databases

HSSP

P00435; 1GP1. [HSSP ENTRY / PDB]

ModBase

Q06652.

Protein family/group databases

PeroxiBase

2618; CsGPx06.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0047066;	Molecular function: phospholipid-hydroperoxide glutathione peroxidase activity (inferred from electronic annotation from EC).
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.
IPR001452; SH3.
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.
PR00452; SH3DOMAIN.

PROSITE

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

Other

ProtoNet

Q06652.

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 167`	`167`	`Probable phospholipid hydroperoxide glutathione peroxidase.`	`PRO_0000066627`
`ACT_SITE`	`41 41`		`By similarity.`

Sequence information

Length: 167 AA [This is the length of the unprocessed precursor]

Molecular weight: 18596 Da [This is the MW of the unprocessed precursor]

CRC64: DB6BBDDC363F3260 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASQSKTSVH DFTVKDAKGQ DVDLSIYKGK LLLIVNVASQ CGLTNSNYTE LSQLYDKYKN 

        70         80         90        100        110        120 
QGLEILAFPC NQFGAQEPGD NEQIQEFACT RFKAEFPIFD KVDVNGDNAA PLYKHLKSSK 

       130        140        150        160 
GGLFGDSIKW NFSKFLVDKE GNVVERYAPT TSPLSIEKDI KKLLETA

Q06652 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