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P11352

- GPX1_MOUSE

UniProt

P11352 - GPX1_MOUSE

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Protein

Glutathione peroxidase 1

Gene

Gpx1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Vmax=319 mM/min/mg enzyme toward H2O2 (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0)1 Publication

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

  1. glutathione binding Source: Ensembl
  2. glutathione peroxidase activity Source: MGI
  3. phospholipid-hydroperoxide glutathione peroxidase activity Source: Ensembl
  4. selenium binding Source: Ensembl

GO - Biological processi

  1. aging Source: Ensembl
  2. angiogenesis involved in wound healing Source: MGI
  3. apoptotic process Source: MGI
  4. blood vessel endothelial cell migration Source: MGI
  5. cell proliferation Source: MGI
  6. cell redox homeostasis Source: Ensembl
  7. endothelial cell development Source: MGI
  8. fat cell differentiation Source: MGI
  9. glutathione metabolic process Source: Ensembl
  10. heart contraction Source: MGI
  11. hydrogen peroxide catabolic process Source: MGI
  12. interaction with symbiont Source: MGI
  13. intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
  14. lipid metabolic process Source: MGI
  15. myoblast proliferation Source: MGI
  16. myotube differentiation Source: MGI
  17. negative regulation of apoptotic process Source: MGI
  18. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  19. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  20. negative regulation of inflammatory response to antigenic stimulus Source: MGI
  21. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
  22. negative regulation of release of cytochrome c from mitochondria Source: Ensembl
  23. positive regulation of protein kinase B signaling Source: MGI
  24. protein oxidation Source: MGI
  25. regulation of gene expression, epigenetic Source: Ensembl
  26. regulation of mammary gland epithelial cell proliferation Source: Ensembl
  27. regulation of neuron apoptotic process Source: MGI
  28. regulation of proteasomal protein catabolic process Source: Ensembl
  29. response to estradiol Source: Ensembl
  30. response to folic acid Source: Ensembl
  31. response to gamma radiation Source: MGI
  32. response to glucose Source: Ensembl
  33. response to hydrogen peroxide Source: BHF-UCL
  34. response to hydroperoxide Source: MGI
  35. response to lipid hydroperoxide Source: Ensembl
  36. response to nicotine Source: Ensembl
  37. response to oxidative stress Source: MGI
  38. response to reactive oxygen species Source: MGI
  39. response to selenium ion Source: Ensembl
  40. response to symbiotic bacterium Source: MGI
  41. response to toxic substance Source: MGI
  42. response to wounding Source: MGI
  43. response to xenobiotic stimulus Source: MGI
  44. sensory perception of sound Source: MGI
  45. skeletal muscle fiber development Source: MGI
  46. skeletal muscle tissue regeneration Source: MGI
  47. temperature homeostasis Source: MGI
  48. triglyceride metabolic process Source: MGI
  49. UV protection Source: Ensembl
  50. vasodilation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
REACT_196559. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_196569. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_206751. 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: Chromosome 9

Organism-specific databases

MGIiMGI:104887. Gpx1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: MGI
  4. 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.
GenevestigatoriP11352.

Interactioni

Subunit structurei

Homotetramer. Interacts with MIEN1.1 Publication

Protein-protein interaction databases

IntActiP11352. 6 interactions.
MINTiMINT-1855025.

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.
OMAiELMYNPI.
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. Reason: Number of sequencing artifacts.

Non-standard residue

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS23522.1.
PIRi A25106. OPMSE.
S05317.
RefSeqi NP_032186.2. NM_008160.6.
UniGenei Mm.1090.

3D structure databases

ProteinModelPortali P11352.
SMRi P11352. Positions 13-195.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11352. 6 interactions.
MINTi MINT-1855025.

Protein family/group databases

PeroxiBasei 3709. MmGPx01.

PTM databases

PhosphoSitei P11352.

2D gel databases

REPRODUCTION-2DPAGE IPI00319652.
P11352.
SWISS-2DPAGE P11352.

Proteomic databases

MaxQBi P11352.
PaxDbi P11352.
PRIDEi P11352.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000082429 ; ENSMUSP00000081010 ; ENSMUSG00000063856 .
GeneIDi 14775.
KEGGi mmu:14775.
UCSCi uc009rpf.3. mouse.

Organism-specific databases

CTDi 2876.
MGIi MGI:104887. Gpx1.

Phylogenomic databases

eggNOGi COG0386.
GeneTreei ENSGT00760000119230.
HOGENOMi HOG000277055.
HOVERGENi HBG004333.
InParanoidi P11352.
KOi K00432.
OMAi ELMYNPI.
OrthoDBi EOG7KQ23C.
PhylomeDBi P11352.
TreeFami TF105318.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
REACT_196559. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_196569. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_206751. Synthesis of 5-eicosatetraenoic acids.

Miscellaneous databases

ChiTaRSi GPX1. mouse.
NextBioi 286877.
PROi P11352.
SOURCEi Search...

Gene expression databases

Bgeei P11352.
CleanExi MM_GPX1.
Genevestigatori P11352.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
PANTHERi PTHR11592. PTHR11592. 1 hit.
Pfami PF00255. GSHPx. 1 hit.
[Graphical view ]
PIRSFi PIRSF000303. Glutathion_perox. 1 hit.
PRINTSi PR01011. GLUTPROXDASE.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 150 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