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Reviewed, UniProtKB/Swiss-Prot P11352 (GPX1_MOUSE)

Last modified June 16, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence similarities

Belongs to the glutathione peroxidase family.

Caution

Ref.3 sequence was originally thought to originate from human.

Sequence caution

The sequence CAB43535.1 differs from that shown. Reason: Miscellaneous discrepancy. Number of sequencing artifacts.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   LigandSelenium
   Molecular functionOxidoreductase
Peroxidase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processangiogenesis involved in wound healing

Inferred from mutant phenotype. Source: MGI

apoptosis

Inferred from mutant phenotype. Source: MGI

blood vessel endothelial cell migration

Inferred from mutant phenotype. Source: MGI

endothelial cell development

Inferred from mutant phenotype. Source: MGI

fat cell differentiation

Inferred from mutant phenotype. Source: MGI

heart contraction

Inferred from mutant phenotype. Source: MGI

hydrogen peroxide catabolic process

Inferred from mutant phenotype. Source: MGI

induction of apoptosis by oxidative stress

Inferred from mutant phenotype. Source: MGI

interaction with symbiont

Inferred from genetic interaction. Source: MGI

myoblast proliferation

Inferred from mutant phenotype. Source: MGI

myotube differentiation

Inferred from mutant phenotype. Source: MGI

negative regulation of apoptosis

Inferred from mutant phenotype. Source: MGI

negative regulation of inflammatory response to antigenic stimulus

Inferred from genetic interaction. Source: MGI

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of protein kinase B signaling cascade

Inferred from mutant phenotype. Source: MGI

protein amino acid oxidation

Inferred from mutant phenotype. Source: MGI

regulation of neuron apoptosis

Inferred from mutant phenotype. Source: MGI

response to gamma radiation

Inferred from genetic interaction. Source: MGI

response to hydroperoxide

Inferred from mutant phenotype. Source: MGI

response to symbiotic bacterium

Inferred from genetic interaction. Source: MGI

response to toxin

Inferred from mutant phenotype. Source: MGI

response to xenobiotic stimulus

Inferred from mutant phenotype. Source: MGI

sensory perception of sound

Inferred from mutant phenotype. Source: MGI

skeletal muscle regeneration

Inferred from mutant phenotype. Source: MGI

temperature homeostasis

Inferred from genetic interaction. Source: MGI

triglyceride metabolic process

Inferred from mutant phenotype. Source: MGI

vasodilation

Inferred from mutant phenotype. Source: MGI

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionglutathione peroxidase activity

Inferred from direct assay. Source: MGI

selenium binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Glutathione peroxidase 1
PRO_0000066613

Sites

Active site471

Amino acid modifications

Non-standard residue471Selenocysteine
Modified residue1461N6-acetyllysine Ref.4
Modified residue2011Phosphoserine Ref.5

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Sequences

Sequence LengthMass (Da)Tools
P11352-1 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 401D065165D8AF5C

FASTA20122,329
        10         20         30         40         50         60 
MCAARLSAAA QSTVYAFSAR PLTGGEPVSL GSLRGKVLLI ENVASLUGTT IRDYTEMNDL 

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

       130        140        150        160        170        180 
HPLFTFLRNA LPTPSDDPTA LMTDPKYIIW SPVCRNDIAW NFEKFLVGPD GVPVRRYSRR 

       190        200 
FRTIDIEPDI ETLLSQQSGN S

« Hide

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References

« Hide 'large scale' references
[1]"The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA."
Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., Harrison P.R.
EMBO J. 5:1221-1227(1986) [PubMed: 3015592] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SELENOCYSTEINE AT SEC-47.
Tissue: Erythrocyte.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Embryonic liver, Kidney and Liver.
[3]"A human cDNA sequence for a novel glutathione peroxidase-related selenopeptide, GPRP."
Dunn D.K., Howells D.D., Richardson J., Goldfarb P.S.
Nucleic Acids Res. 17:6390-6390(1989) [PubMed: 2771650] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X03920 Genomic DNA. Translation: CAA27558.1.
AK002245 mRNA. Translation: BAC55244.1.
AK010999 mRNA. Translation: BAC55252.1.
AK011019 mRNA. Translation: BAC55253.1.
AK028171 mRNA. Translation: BAC55257.1.
AK150548 mRNA. Translation: BAE29650.1.
AK154833 mRNA. Translation: BAE32862.1.
AK160388 mRNA. Translation: BAE35760.1.
X15667 mRNA. Translation: CAB43535.1. Sequence problems.
IPIIPI00319652.
PIROPMSE. A25106.
S05317.
RefSeqNP_032186.2.
UniGeneMm.1090

3D structure databases

HSSPHSSP built from PDB template 1GP1 based on UniProtKB P00435.
SMRP11352. Positions 13-195.
ModBaseSearch...

Protein family/group databases

PeroxiBase3709. MmGPx01.

PTM databases

PhosphoSiteP11352.

2-D gel databases

SWISS-2DPAGEP11352.
REPRODUCTION-2DPAGEP11352.

Genome annotation databases

EnsemblENSMUSG00000063856. Mus musculus. [Contig view]
GeneID14775.
KEGGmmu:14775.

Organism-specific databases

MGIMGI:104887. Gpx1.

Phylogenomic databases

HOGENOMP11352.
HOVERGENP11352.
OMAP11352. VPVRRYS.

Enzyme and pathway databases

BRENDA1.11.1.9. 244.

Gene expression databases

ArrayExpressP11352.
BgeeP11352.
CleanExMM_GPX1.
GermOnlineENSMUSG00000063856. Mus musculus.

Family and domain databases

InterProIPR000889. Glutathione_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR11592. Glut_peroxidase. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio286877.
SOURCESearch...

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Entry information

Entry nameGPX1_MOUSE
AccessionPrimary (citable) accession number: P11352
Secondary accession number(s): P12079, Q544W3, Q9CR54
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 26, 2008
Last modified: June 16, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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