Reviewed, UniProtKB/Swiss-Prot P23764 (GPX3_RAT)

Names and origin

Protein names

Recommended name:
    Glutathione peroxidase 3
    EC=1.11.1.9
Alternative name(s):
    GSHPx-3
      Short name=GPx-3
    Plasma glutathione peroxidase
    GSHPx-P

Gene names

Name:

Gpx3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
Catalytic activity	2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
Subunit structure	Homotetramer.
Subcellular location	Secreted.
Tissue specificity	Secreted in plasma.
Sequence similarities	Belongs to the glutathione peroxidase family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Selenocysteine
Domain	Signal
Ligand	Selenium
Molecular function	Oxidoreductase Peroxidase
Gene Ontology (GO)
Biological process	female pregnancy Inferred from expression pattern. Source: RGD glutathione metabolic process Inferred from direct assay. Source: RGD hydrogen peroxide catabolic process Inferred from direct assay. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB response to corticosterone stimulus Inferred from expression pattern. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to molecule of fungal origin Inferred from expression pattern. Source: RGD response to organic cyclic substance Inferred from expression pattern. Source: RGD response to selenium ion Inferred from expression pattern. Source: RGD
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB soluble fraction Inferred from direct assay. Source: RGD
Molecular function	glutathione binding Inferred from direct assay. Source: RGD glutathione peroxidase activity Inferred from sequence or structural similarity. Source: UniProtKB selenium binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 226	202	Glutathione peroxidase 3		PRO_0000013064
Sites
	Active site	73	1
Amino acid modifications
	Non-standard residue	73	1	Selenocysteine
Experimental info
	Sequence conflict	2	1	A → S in BAA00587. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23764-1 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: 414BF56F8F553F88	FASTA	226	25,424
	10 20 30 40 50 60 MARILRASCL LSLLLAGFVP PGRGQEKSKT DCHGGMSGTI YEYGALTIDG EEYIPFKQYA 70 80 90 100 110 120 GKYILFVNVA SYUGLTDQYL ELNALQEELG PFGLVILGFP CNQFGKQEPG ENSEILPSLK 130 140 150 160 170 180 YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTA ELLGSPGRLF WEPMKIHDIR 190 200 210 220 WNFEKFLVGP DGIPIMRWYH RTTVSNVKMD ILSYMRRQAA LGARGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tissue specific expression of the plasma glutathione peroxidase gene in rat kidney." Yoshimura S., Watanabe K., Suemizu H., Onozawa T., Mizoguchi J., Tsuda K., Hatta H., Moriuchi T. J. Biochem. 109:918-923(1991) [PubMed: 1939013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00680 mRNA. Translation: BAA00587.2. BC062227 mRNA. Translation: AAH62227.1.
IPI	IPI00476458.
PIR	JX0176.
RefSeq	NP_071970.2.
UniGene	Rn.108074
3D structure databases
HSSP	HSSP built from PDB template 1GP1 based on UniProtKB P00435.
ModBase	Search...
Protein-protein interaction databases
STRING	P23764.
Protein family/group databases
PeroxiBase	3732. RnoGPx03.
Genome annotation databases
Ensembl	ENSRNOT00000036496; ENSRNOP00000031350; ENSRNOG00000021809; Rattus norvegicus. [Genome view]
GeneID	64317.
KEGG	rno:64317.
Organism-specific databases
CTD	64317.
RGD	69224. Gpx3.
Phylogenomic databases
HOVERGEN	P23764.
Enzyme and pathway databases
BRENDA	1.11.1.9. 248.
Gene expression databases
ArrayExpress	P23764.
Genevestigator	P23764.
Family and domain databases
InterPro	IPR000889. Glutathione_peroxidase. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR11592. Glut_peroxidase. 1 hit.
Pfam	PF00255. GSHPx. 1 hit. [Graphical view]
PIRSF	PIRSF000303. Glutathion_perox. 1 hit.
PRINTS	PR01011. GLUTPROXDASE.
PROSITE	PS00460. GLUTATHIONE_PEROXID_1. 1 hit. PS00763. GLUTATHIONE_PEROXID_2. 1 hit. PS51355. GLUTATHIONE_PEROXID_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	613000.

Entry information

Entry name

GPX3_RAT

Accession

Primary (citable) accession number: P23764
Secondary accession number(s): Q6P6H2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	February 26, 2008
Last modified:	October 13, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)