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P11352 (GPX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione peroxidase 1

Short name=GPx-1
Short name=GSHPx-1
EC=1.11.1.9
Alternative name(s):
Cellular glutathione peroxidase
Selenium-dependent glutathione peroxidase 1
Gene names
Name:Gpx1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.5

Subcellular location

Cytoplasm.

Post-translational modification

During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine (Ref.7).

Miscellaneous

In the absence of Sod1, Gpx1 in the liver undergoes a 40% reduction in catalytic activity as a result of the decomposition of Sec-47 to dehydroalanine (Ref.7).

Sequence similarities

Belongs to the glutathione peroxidase family.

Caution

Ref.4 sequence was originally thought to originate from human.

Biophysicochemical properties

Kinetic parameters:

KM=14 µM for H2O2 (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0) Ref.7

KM=29 µM for tert-butylperoxide (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)

Vmax=319 mM/min/mg enzyme toward H2O2 (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)

Vmax=182 mM/min/mg enzyme toward tert-butylperoxide (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   Molecular functionOxidoreductase
Peroxidase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUV protection

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

angiogenesis involved in wound healing

Inferred from mutant phenotype PubMed 16373599. Source: MGI

apoptotic process

Inferred from mutant phenotype PubMed 16962942. Source: MGI

blood vessel endothelial cell migration

Inferred from mutant phenotype PubMed 16373599. Source: MGI

cell proliferation

Inferred from mutant phenotype PubMed 14732290. Source: MGI

cell redox homeostasis

Inferred from electronic annotation. Source: Ensembl

endothelial cell development

Inferred from mutant phenotype PubMed 16373599. Source: MGI

fat cell differentiation

Inferred from mutant phenotype PubMed 16962942. Source: MGI

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

heart contraction

Inferred from mutant phenotype PubMed 12196344. Source: MGI

hydrogen peroxide catabolic process

Inferred from mutant phenotype PubMed 10754271PubMed 10915565PubMed 11545230PubMed 15182862PubMed 15827346PubMed 9788901. Source: MGI

interaction with symbiont

Inferred from genetic interaction PubMed 12751789. Source: MGI

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype PubMed 11562367PubMed 15663476. Source: MGI

lipid metabolic process

Inferred from mutant phenotype PubMed 10754271. Source: MGI

myoblast proliferation

Inferred from mutant phenotype PubMed 12368211PubMed 16962942. Source: MGI

myotube differentiation

Inferred from mutant phenotype PubMed 12368211PubMed 16962942. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16934683. Source: MGI

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response to antigenic stimulus

Inferred from genetic interaction PubMed 12751789. Source: MGI

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype PubMed 16373599. Source: MGI

negative regulation of release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 15663476. Source: MGI

protein oxidation

Inferred from mutant phenotype PubMed 10428770. Source: MGI

regulation of gene expression, epigenetic

Inferred from electronic annotation. Source: Ensembl

regulation of mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 11579147. Source: MGI

regulation of proteasomal protein catabolic process

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to folic acid

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from genetic interaction PubMed 15182862. Source: MGI

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: BHF-UCL

response to hydroperoxide

Inferred from mutant phenotype PubMed 16723478. Source: MGI

response to lipid hydroperoxide

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from mutant phenotype PubMed 10428770PubMed 10627575PubMed 10915565PubMed 11893559PubMed 12196344PubMed 15182862PubMed 16962942. Source: MGI

response to reactive oxygen species

Inferred from mutant phenotype PubMed 10915565PubMed 11562367PubMed 16373599PubMed 16962942PubMed 17145560. Source: MGI

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to symbiotic bacterium

Inferred from genetic interaction PubMed 12751789. Source: MGI

response to toxic substance

Inferred from mutant phenotype PubMed 10627575. Source: MGI

response to wounding

Inferred from mutant phenotype PubMed 11579147. Source: MGI

response to xenobiotic stimulus

Inferred from mutant phenotype PubMed 10915565. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 11545230. Source: MGI

skeletal muscle fiber development

Inferred from mutant phenotype PubMed 16962942. Source: MGI

skeletal muscle tissue regeneration

Inferred from mutant phenotype PubMed 16962942. Source: MGI

temperature homeostasis

Inferred from genetic interaction PubMed 11518697. Source: MGI

triglyceride metabolic process

Inferred from mutant phenotype PubMed 12117267. Source: MGI

vasodilation

Inferred from mutant phenotype PubMed 11893559PubMed 12196344. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015PubMed 9126277. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionendopeptidase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

glutathione binding

Inferred from electronic annotation. Source: Ensembl

glutathione peroxidase activity

Inferred from direct assay PubMed 12521604PubMed 12646716. Source: MGI

phospholipid-hydroperoxide glutathione peroxidase activity

Inferred from electronic annotation. Source: Ensembl

selenium binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Glutathione peroxidase 1
PRO_0000066613

Sites

Active site471
Site471Subject to oxidation and hydroselenide loss to dehydroalanine

Amino acid modifications

Non-standard residue471Selenocysteine
Modified residue71Phosphoserine Ref.6
Modified residue621N6-acetyllysine; alternate Ref.9
Modified residue621N6-succinyllysine; alternate Ref.8
Modified residue861N6-acetyllysine; alternate Ref.9
Modified residue861N6-succinyllysine; alternate Ref.8
Modified residue1121N6-acetyllysine; alternate Ref.9
Modified residue1121N6-succinyllysine; alternate Ref.8
Modified residue1191N6-acetyllysine Ref.9
Modified residue1461N6-acetyllysine; alternate Ref.9
Modified residue1461N6-succinyllysine; alternate Ref.8

Sequences

Sequence LengthMass (Da)Tools
P11352 [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

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Embryonic liver, Kidney and Liver.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"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] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[5]"SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family."
Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A., Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.
Biochemistry 46:6871-6882(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIEN1.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein."
Wang S.K., Weaver J.D., Zhang S., Lei X.G.
Free Radic. Biol. Med. 51:197-204(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SELENOCYSTEINE AT SEC-47, PARTIAL LOSS OF SELENIUM IN ABSENCE OF SOD1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Liver.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112 AND LYS-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112; LYS-119 AND LYS-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
BC086649 mRNA. Translation: AAH86649.1.
X15667 mRNA. Translation: CAB43535.1. Sequence problems.
PIROPMSE. A25106.
S05317.
RefSeqNP_032186.2. NM_008160.6.
UniGeneMm.1090.

3D structure databases

ProteinModelPortalP11352.
SMRP11352. Positions 13-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11352. 6 interactions.
MINTMINT-1855025.

Protein family/group databases

PeroxiBase3709. MmGPx01.

PTM databases

PhosphoSiteP11352.

2D gel databases

REPRODUCTION-2DPAGEIPI00319652.
P11352.
SWISS-2DPAGEP11352.

Proteomic databases

PaxDbP11352.
PRIDEP11352.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000082429; ENSMUSP00000081010; ENSMUSG00000063856.
GeneID14775.
KEGGmmu:14775.
UCSCuc009rpf.3. mouse.

Organism-specific databases

CTD2876.
MGIMGI:104887. Gpx1.

Phylogenomic databases

eggNOGCOG0386.
GeneTreeENSGT00740000115226.
HOGENOMHOG000277055.
HOVERGENHBG004333.
InParanoidP11352.
KOK00432.
OMACEVNGEK.
OrthoDBEOG7KQ23C.
PhylomeDBP11352.
TreeFamTF105318.

Gene expression databases

BgeeP11352.
CleanExMM_GPX1.
GenevestigatorP11352.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11592. PTHR11592. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPX1. mouse.
NextBio286877.
PROP11352.
SOURCESearch...

Entry information

Entry nameGPX1_MOUSE
AccessionPrimary (citable) accession number: P11352
Secondary accession number(s): P12079 expand/collapse secondary AC list , Q544W3, Q5RJH8, Q9CR54
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 26, 2008
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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