Glutathione peroxidase 1 - Rattus norvegicus (Rat)

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P04041 (GPX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutathione peroxidase 1
Short name=GPx-1
Short name=GSHPx-1
EC=1.11.1.9

Alternative name(s):
Cellular glutathione peroxidase

Gene names

Name:

Gpx1

Organism

Rattus norvegicus (Rat) [Reference proteome]

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	201 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protects the hemoglobin in erythrocytes from oxidative breakdown.
Catalytic activity	2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
Subunit structure	Homotetramer. Interacts with MIEN1 By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in liver and lung. Ref.5
Post-translational modification	During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine By similarity.
Sequence similarities	Belongs to the glutathione peroxidase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Selenocysteine
Molecular function	Oxidoreductase Peroxidase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from expression pattern PubMed 17021340. Source: RGD glutathione metabolic process Inferred from direct assay PubMed 16140890. Source: RGD hydrogen peroxide catabolic process Inferred from direct assay PubMed 16140890. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 17211248. Source: RGD response to folic acid Inferred from expression pattern PubMed 16251605. Source: RGD response to glucose stimulus Inferred from expression pattern PubMed 15039483. Source: RGD response to lipid hydroperoxide Inferred from mutant phenotype PubMed 12934674. Source: RGD response to nicotine Inferred from expression pattern PubMed 18343235. Source: RGD response to selenium ion Inferred from expression pattern PubMed 19234057. Source: RGD
Cellular_component	cytosol Traceable author statement Ref.6. Source: RGD nucleus Inferred from direct assay PubMed 12516874. Source: RGD
Molecular_function	glutathione binding Inferred from direct assay PubMed 16140890. Source: RGD glutathione peroxidase activity Inferred from direct assay PubMed 16140890 Ref.6. Source: RGD phospholipid-hydroperoxide glutathione peroxidase activity Inferred from mutant phenotype PubMed 12934674. Source: RGD selenium binding Inferred from mutant phenotype PubMed 16140890. Source: RGD
Complete GO annotation...

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

Site

Subject to oxidation and hydroselenide loss to dehydroalanine By similarity

Amino acid modifications

Non-standard residue

Selenocysteine Ref.8

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

Sequences

Sequence

Length

Mass (Da)

Tools

P04041 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	Reddy A.P., Hsu B.L., Reddy P.S., Li N.Q., Thyagaraju K., Reddy C.C., Tam M.F., Tu C.P.D. Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 47.
[5]	"Cloning and characterization of the rat glutathione peroxidase gene." Ho Y.-S., Howard A.J. FEBS Lett. 301:5-9(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley.
[6]	"Dietary selenium stabilizes glutathione peroxidase mRNA in rat liver." Christensen M.J., Burgener K.W. J. Nutr. 122:1620-1626(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[7]	"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.
[8]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-52, SELENOCYSTEINE AT SEC-47. Tissue: Liver.
[9]	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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M21210 mRNA. Translation: AAB95647.2. X07365 mRNA. Translation: CAB43593.1. X12367 mRNA. Translation: CAA30928.2. 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. NM_030826.3.
UniGene	Rn.11323.
3D structure databases
ProteinModelPortal	P04041.
ModBase	Search...
Protein family/group databases
PeroxiBase	3730. RnoGPx01.
PTM databases
PhosphoSite	P04041.
Proteomic databases
PRIDE	P04041.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24404.
KEGG	rno:24404.
Organism-specific databases
CTD	2876.
RGD	2729. Gpx1.
Phylogenomic databases
HOVERGEN	HBG004333.
KO	K00432.
Gene expression databases
Genevestigator	P04041.
Family and domain databases
Gene3D	3.40.30.10. 1 hit.
InterPro	IPR000889. Glutathione_peroxidase. IPR012336. Thioredoxin-like_fold. [Graphical view]
PANTHER	PTHR11592. PTHR11592. 1 hit.
Pfam	PF00255. GSHPx. 1 hit. [Graphical view]
PIRSF	PIRSF000303. Glutathion_perox. 1 hit.
PRINTS	PR01011. GLUTPROXDASE.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS00460. GLUTATHIONE_PEROXID_1. 1 hit. PS00763. GLUTATHIONE_PEROXID_2. 1 hit. PS51355. GLUTATHIONE_PEROXID_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	603207.

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:	April 3, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents