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Protein

Glutathione peroxidase 1

Gene

Gpx1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protects the hemoglobin in erythrocytes from oxidative breakdown.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Kineticsi

  1. KM=14 µM for H2O2 (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)1 Publication
  2. KM=29 µM for tert-butylperoxide (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)1 Publication
  1. Vmax=319 mM/min/mg enzyme toward H2O2 (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)1 Publication
  2. Vmax=182 mM/min/mg enzyme toward tert-butylperoxide (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei47 – 471
Sitei47 – 471Subject to oxidation and hydroselenide loss to dehydroalanine

GO - Molecular functioni

GO - Biological processi

  • aging Source: Ensembl
  • angiogenesis involved in wound healing Source: MGI
  • apoptotic process Source: MGI
  • blood vessel endothelial cell migration Source: MGI
  • cell proliferation Source: MGI
  • cell redox homeostasis Source: MGI
  • endothelial cell development Source: MGI
  • fat cell differentiation Source: MGI
  • glutathione metabolic process Source: MGI
  • heart contraction Source: MGI
  • hydrogen peroxide catabolic process Source: MGI
  • interaction with symbiont Source: MGI
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
  • lipid metabolic process Source: MGI
  • myoblast proliferation Source: MGI
  • myotube differentiation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • negative regulation of inflammatory response to antigenic stimulus Source: MGI
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
  • negative regulation of release of cytochrome c from mitochondria Source: MGI
  • positive regulation of protein kinase B signaling Source: MGI
  • protein oxidation Source: MGI
  • regulation of gene expression, epigenetic Source: MGI
  • regulation of mammary gland epithelial cell proliferation Source: MGI
  • regulation of neuron apoptotic process Source: MGI
  • regulation of proteasomal protein catabolic process Source: MGI
  • response to estradiol Source: Ensembl
  • response to folic acid Source: Ensembl
  • response to gamma radiation Source: MGI
  • response to glucose Source: Ensembl
  • response to hydrogen peroxide Source: BHF-UCL
  • response to hydroperoxide Source: MGI
  • response to lipid hydroperoxide Source: Ensembl
  • response to nicotine Source: Ensembl
  • response to oxidative stress Source: MGI
  • response to reactive oxygen species Source: MGI
  • response to selenium ion Source: MGI
  • response to symbiotic bacterium Source: MGI
  • response to toxic substance Source: MGI
  • response to wounding Source: MGI
  • response to xenobiotic stimulus Source: MGI
  • sensory perception of sound Source: MGI
  • skeletal muscle fiber development Source: MGI
  • skeletal muscle tissue regeneration Source: MGI
  • temperature homeostasis Source: MGI
  • triglyceride metabolic process Source: MGI
  • UV protection Source: MGI
  • vasodilation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_277717. Purine catabolism.
REACT_298121. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_308972. Detoxification of Reactive Oxygen Species.
REACT_325938. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_327774. Synthesis of 5-eicosatetraenoic acids.

Protein family/group databases

PeroxiBasei3709. MmGPx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 1 (EC:1.11.1.9)
Short name:
GPx-1
Short name:
GSHPx-1
Alternative name(s):
Cellular glutathione peroxidase
Selenium-dependent glutathione peroxidase 1
Gene namesi
Name:Gpx1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:104887. Gpx1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • extracellular exosome Source: MGI
  • Lewy body Source: Ensembl
  • mitochondrion Source: MGI
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Glutathione peroxidase 1PRO_0000066613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei62 – 621N6-acetyllysine; alternate1 Publication
Modified residuei62 – 621N6-succinyllysine; alternate1 Publication
Modified residuei86 – 861N6-acetyllysine; alternate1 Publication
Modified residuei86 – 861N6-succinyllysine; alternate1 Publication
Modified residuei112 – 1121N6-acetyllysine; alternate1 Publication
Modified residuei112 – 1121N6-succinyllysine; alternate1 Publication
Modified residuei119 – 1191N6-acetyllysine1 Publication
Modified residuei146 – 1461N6-acetyllysine; alternate1 Publication
Modified residuei146 – 1461N6-succinyllysine; alternate1 Publication

Post-translational modificationi

During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11352.
PaxDbiP11352.
PRIDEiP11352.

2D gel databases

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

PTM databases

PhosphoSiteiP11352.

Expressioni

Gene expression databases

BgeeiP11352.
CleanExiMM_GPX1.
GenevisibleiP11352. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with MIEN1.1 Publication

Protein-protein interaction databases

BioGridi200037. 1 interaction.
IntActiP11352. 6 interactions.
MINTiMINT-1855025.
STRINGi10090.ENSMUSP00000081010.

Structurei

3D structure databases

ProteinModelPortaliP11352.
SMRiP11352. Positions 13-195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP11352.
KOiK00432.
OMAiCEVNGEK.
OrthoDBiEOG7KQ23C.
PhylomeDBiP11352.
TreeFamiTF105318.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11352-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCAARLSAAA QSTVYAFSAR PLTGGEPVSL GSLRGKVLLI ENVASLUGTT
60 70 80 90 100
IRDYTEMNDL QKRLGPRGLV VLGFPCNQFG HQENGKNEEI LNSLKYVRPG
110 120 130 140 150
GGFEPNFTLF EKCEVNGEKA HPLFTFLRNA LPTPSDDPTA LMTDPKYIIW
160 170 180 190 200
SPVCRNDIAW NFEKFLVGPD GVPVRRYSRR FRTIDIEPDI ETLLSQQSGN

S
Length:201
Mass (Da):22,329
Last modified:February 26, 2008 - v2
Checksum:i401D065165D8AF5C
GO

Sequence cautioni

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

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei47 – 471Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23522.1.
PIRiA25106. OPMSE.
S05317.
RefSeqiNP_032186.2. NM_008160.6.
UniGeneiMm.1090.

Genome annotation databases

EnsembliENSMUST00000082429; ENSMUSP00000081010; ENSMUSG00000063856.
GeneIDi14775.
KEGGimmu:14775.
UCSCiuc009rpf.3. mouse.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23522.1.
PIRiA25106. OPMSE.
S05317.
RefSeqiNP_032186.2. NM_008160.6.
UniGeneiMm.1090.

3D structure databases

ProteinModelPortaliP11352.
SMRiP11352. Positions 13-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200037. 1 interaction.
IntActiP11352. 6 interactions.
MINTiMINT-1855025.
STRINGi10090.ENSMUSP00000081010.

Protein family/group databases

PeroxiBasei3709. MmGPx01.

PTM databases

PhosphoSiteiP11352.

2D gel databases

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

Proteomic databases

MaxQBiP11352.
PaxDbiP11352.
PRIDEiP11352.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000082429; ENSMUSP00000081010; ENSMUSG00000063856.
GeneIDi14775.
KEGGimmu:14775.
UCSCiuc009rpf.3. mouse.

Organism-specific databases

CTDi2876.
MGIiMGI:104887. Gpx1.

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP11352.
KOiK00432.
OMAiCEVNGEK.
OrthoDBiEOG7KQ23C.
PhylomeDBiP11352.
TreeFamiTF105318.

Enzyme and pathway databases

ReactomeiREACT_277717. Purine catabolism.
REACT_298121. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_308972. Detoxification of Reactive Oxygen Species.
REACT_325938. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_327774. Synthesis of 5-eicosatetraenoic acids.

Miscellaneous databases

ChiTaRSiGpx1. mouse.
NextBioi286877.
PROiP11352.
SOURCEiSearch...

Gene expression databases

BgeeiP11352.
CleanExiMM_GPX1.
GenevisibleiP11352. MM.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiGPX1_MOUSE
AccessioniPrimary (citable) accession number: P11352
Secondary accession number(s): P12079
, Q544W3, Q5RJH8, Q9CR54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 26, 2008
Last modified: June 24, 2015
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.1 Publication

Caution

PubMed:2771650 sequence was originally thought to originate from human.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.