Glutathione peroxidase 1 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P04041 (GPX1_RAT)

Last modified June 16, 2009. Version 88. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glutathione peroxidase 1
    EC=1.11.1.9
Alternative name(s):
    GSHPx-1
      Short name=GPx-1
    Cellular glutathione peroxidase

Gene names

Name:

Gpx1

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

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Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Protects the hemoglobin in erythrocytes from oxidative breakdown.
Catalytic activity	2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in liver and lung. Ref.4
Sequence similarities	Belongs to the glutathione peroxidase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Selenocysteine
Ligand	Selenium
Molecular function	Oxidoreductase Peroxidase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aging 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 response to estradiol stimulus Inferred from expression pattern. Source: RGD response to folic acid Inferred from expression pattern. Source: RGD response to glucose stimulus Inferred from expression pattern. Source: RGD response to lipid hydroperoxide Inferred from mutant phenotype. Source: RGD response to nicotine Inferred from expression pattern. Source: RGD response to selenium ion Inferred from expression pattern. Source: RGD
Cellular component	cytosol Ref.5 Traceable author statement. Source: RGD nucleus Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	glutathione binding Inferred from direct assay. Source: RGD glutathione peroxidase activity Ref.5 Inferred from direct assay. Source: RGD phospholipid-hydroperoxide glutathione peroxidase activity Inferred from mutant phenotype. Source: RGD selenium binding Ref.1 Inferred from mutant phenotype. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

Glutathione peroxidase 1

PRO_0000066617

Sites

Active site

Amino acid modifications

Non-standard residue

Selenocysteine Ref.7

Modified residue

146

N6-acetyllysine By similarity

Experimental info

Sequence conflict

24 – 25

GG → RE in AAB95647. Ref.1

Sequence conflict

154

C → S in AAB95647. Ref.1

Sequence conflict

178

S → T in AAB95647. Ref.1

Sequence conflict

198

P → S in AAB95647. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P04041-1 [UniParc].

Last modified February 26, 2008. Version 4.
Checksum: 093528A214615A11
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FASTA

201

22,305

        10         20         30         40         50         60 
MSAARLSAVA QSTVYAFSAR PLAGGEPVSL GSLRGKVLLI ENVASLUGTT TRDYTEMNDL 

        70         80         90        100        110        120 
QKRLGPRGLV VLGFPCNQFG HQENGKNEEI LNSLKYVRPG GGFEPNFTLF EKCEVNGEKA 

       130        140        150        160        170        180 
HPLFTFLRNA LPAPSDDPTA LMTDPKYIIW SPVCRNDISW NFEKFLVGPD GVPVRRYSRR 

       190        200 
FRTIDIEPDI EALLSKQPSN P

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References

[1]	"Determination of nucleotide sequence of cDNA coding rat glutathione peroxidase and diminished expression of the mRNA in selenium deficient rat liver." Yoshimura S., Takekoshi S., Watanabe K., Fujii-Kuriyama Y. Biochem. Biophys. Res. Commun. 154:1024-1028(1988) [PubMed: 3408482] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide sequence of a rat glutathione peroxidase cDNA." Ho Y.S., Howard A.J., Crapo J.D. Nucleic Acids Res. 16:5207-5207(1988) [PubMed: 3387231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[3]	"Expression of glutathione peroxidase I gene in selenium-deficient rats." Reddy A.P., Hsu B.L., Reddy P.S., Li N.Q., Thyagaraju K., Reddy C.C., Tam M.F., Tu C.P.D. Nucleic Acids Res. 16:5557-5568(1988) [PubMed: 2838821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning and characterization of the rat glutathione peroxidase gene." Ho Y.-S., Howard A.J. FEBS Lett. 301:5-9(1992) [PubMed: 1451786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley.
[5]	"Dietary selenium stabilizes glutathione peroxidase mRNA in rat liver." Christensen M.J., Burgener K.W. J. Nutr. 122:1620-1626(1992) [PubMed: 1640255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[6]	"Functional analysis of the 5'-flanking region of the rat glutathione peroxidase gene." Suemizu H. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82. Strain: Sprague-Dawley.
[7]	"Amino acid sequence around the active-site selenocysteine of rat liver glutathione peroxidase." Condell R.A., Tappel A.L. Biochim. Biophys. Acta 709:304-309(1982) [PubMed: 6217842] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-52, SELENOCYSTEINE AT SEC-47. Tissue: Liver.
[8]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 96-112 AND 165-176, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M21210 mRNA. Translation: AAB95647.2. X07365 mRNA. Translation: CAB43593.1. X12367 mRNA. Translation: CAA30928.1. S50336 Genomic DNA. Translation: AAA12407.2. S41066 mRNA. Translation: AAK72702.1. AB004231 Genomic DNA. Translation: BAA20399.2.
IPI	IPI00192301.
PIR	OPRTE. A30793.
RefSeq	NP_110453.3.
UniGene	Rn.11323
3D structure databases
HSSP	HSSP built from PDB template 1GP1 based on UniProtKB P00435.
SMR	P04041. Positions 13-195.
ModBase	Search...
Protein family/group databases
PeroxiBase	3730. RnoGPx01.
Proteomic databases
PRIDE	P04041.
Genome annotation databases
GeneID	24404.
KEGG	rno:24404.
Organism-specific databases
RGD	2729. Gpx1.
Phylogenomic databases
HOVERGEN	P04041.
Enzyme and pathway databases
BRENDA	1.11.1.9. 248.
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	603207.

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Entry information

Entry name

GPX1_RAT

Accession

Primary (citable) accession number: P04041
Secondary accession number(s): O08946, Q4PIY2, Q91WZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 88 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other Resources

Entry information

Relevant documents