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P11352

- GPX1_MOUSE

UniProt

P11352 - GPX1_MOUSE

Protein

Glutathione peroxidase 1

Gene

Gpx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
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    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. endopeptidase inhibitor activity Source: Ensembl
    2. glutathione binding Source: Ensembl
    3. glutathione peroxidase activity Source: MGI
    4. phospholipid-hydroperoxide glutathione peroxidase activity Source: Ensembl
    5. protein binding Source: UniProtKB
    6. 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

    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. mitochondrion Source: MGI
    3. nucleus Source: Ensembl

    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.
    GeneTreeiENSGT00740000115226.
    HOGENOMiHOG000277055.
    HOVERGENiHBG004333.
    InParanoidiP11352.
    KOiK00432.
    OMAiELMYNPI.
    OrthoDBiEOG7KQ23C.
    PhylomeDBiP11352.
    TreeFamiTF105318.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000889. Glutathione_peroxidase.
    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

    MCAARLSAAA QSTVYAFSAR PLTGGEPVSL GSLRGKVLLI ENVASLUGTT    50
    IRDYTEMNDL QKRLGPRGLV VLGFPCNQFG HQENGKNEEI LNSLKYVRPG 100
    GGFEPNFTLF EKCEVNGEKA HPLFTFLRNA LPTPSDDPTA LMTDPKYIIW 150
    SPVCRNDIAW NFEKFLVGPD GVPVRRYSRR FRTIDIEPDI ETLLSQQSGN 200
    S 201
    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 ENSGT00740000115226.
    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.
    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

    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 1, 2014
    This is version 149 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