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P24270

- CATA_MOUSE

UniProt

P24270 - CATA_MOUSE

Protein

Catalase

Gene

Cat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.

    Catalytic activityi

    2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

    Cofactori

    Heme group.
    NADP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei75 – 751PROSITE-ProRule annotation
    Active sitei148 – 1481PROSITE-ProRule annotation
    Metal bindingi358 – 3581Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. aminoacylase activity Source: MGI
    2. catalase activity Source: MGI
    3. heme binding Source: Ensembl
    4. metal ion binding Source: UniProtKB-KW
    5. NADP binding Source: Ensembl
    6. oxidoreductase activity, acting on peroxide as acceptor Source: MGI

    GO - Biological processi

    1. aerobic respiration Source: MGI
    2. cellular response to growth factor stimulus Source: Ensembl
    3. cholesterol metabolic process Source: MGI
    4. hemoglobin metabolic process Source: MGI
    5. hydrogen peroxide catabolic process Source: MGI
    6. kidney development Source: Ensembl
    7. menopause Source: Ensembl
    8. negative regulation of apoptotic process Source: Ensembl
    9. negative regulation of NF-kappaB transcription factor activity Source: MGI
    10. positive regulation of cell division Source: UniProtKB-KW
    11. positive regulation of NF-kappaB transcription factor activity Source: MGI
    12. positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
    13. protein homotetramerization Source: Ensembl
    14. response to hyperoxia Source: Ensembl
    15. response to hypoxia Source: Ensembl
    16. response to oxidative stress Source: MGI
    17. response to vitamin E Source: Ensembl
    18. triglyceride metabolic process Source: MGI
    19. ureteric bud development Source: Ensembl
    20. UV protection Source: Ensembl

    Keywords - Molecular functioni

    Mitogen, Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase (EC:1.11.1.6)
    Gene namesi
    Name:Cat
    Synonyms:Cas-1, Cas1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:88271. Cat.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum Source: Ensembl
    3. Golgi apparatus Source: Ensembl
    4. lysosome Source: Ensembl
    5. mitochondrial intermembrane space Source: Ensembl
    6. mitochondrion Source: MGI
    7. peroxisomal membrane Source: MGI
    8. peroxisome Source: UniProtKB
    9. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111Q → H: Acatalasemia.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 527526CatalasePRO_0000084902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei13 – 131N6-succinyllysine1 Publication
    Modified residuei221 – 2211N6-succinyllysine1 Publication
    Modified residuei233 – 2331N6-acetyllysine1 Publication
    Modified residuei306 – 3061N6-acetyllysine; alternate1 Publication
    Modified residuei306 – 3061N6-succinyllysine; alternate1 Publication
    Modified residuei417 – 4171Phosphoserine1 Publication
    Modified residuei430 – 4301N6-acetyllysine; alternate1 Publication
    Modified residuei430 – 4301N6-succinyllysine; alternate1 Publication
    Modified residuei434 – 4341Phosphoserine1 Publication
    Modified residuei449 – 4491N6-acetyllysine; alternate2 Publications
    Modified residuei449 – 4491N6-succinyllysine; alternate1 Publication
    Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
    Modified residuei480 – 4801N6-succinyllysine; alternate1 Publication
    Modified residuei499 – 4991N6-acetyllysine1 Publication
    Modified residuei522 – 5221N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP24270.
    PaxDbiP24270.
    PRIDEiP24270.

    2D gel databases

    SWISS-2DPAGEP24270.

    PTM databases

    PhosphoSiteiP24270.

    Expressioni

    Gene expression databases

    ArrayExpressiP24270.
    BgeeiP24270.
    CleanExiMM_CAT.
    GenevestigatoriP24270.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP24270. 3 interactions.
    MINTiMINT-1859622.

    Structurei

    3D structure databases

    ProteinModelPortaliP24270.
    SMRiP24270. Positions 4-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    Phylogenomic databases

    eggNOGiCOG0753.
    GeneTreeiENSGT00390000018100.
    HOGENOMiHOG000087852.
    HOVERGENiHBG003986.
    InParanoidiQ3TXQ6.
    KOiK03781.
    OMAiEVEQMAY.
    OrthoDBiEOG7V7660.
    TreeFamiTF300540.

    Family and domain databases

    Gene3Di2.40.180.10. 1 hit.
    InterProiIPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024711. Catalase_clade1/3.
    IPR011614. Catalase_core.
    IPR002226. Catalase_haem_BS.
    IPR010582. Catalase_immune_responsive.
    [Graphical view]
    PANTHERiPTHR11465. PTHR11465. 1 hit.
    PfamiPF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSiPR00067. CATALASE.
    SMARTiSM01060. Catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56634. SSF56634. 1 hit.
    PROSITEiPS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P24270-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL    50
    LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF 100
    EHIGKRTPIA VRFSTVTGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT 150
    PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF 200
    SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ GIKNLPVGEA 250
    GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT 300
    KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM 350
    LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG 400
    APNYYPNSFS APEQQRSALE HSVQCAVDVK RFNSANEDNV TQVRTFYTKV 450
    LNEEERKRLC ENIAGHLKDA QLFIQKKAVK NFTDVHPDYG ARIQALLDKY 500
    NAEKPKNAIH TYTQAGSHMA AKGKANL 527
    Length:527
    Mass (Da):59,795
    Last modified:July 27, 2011 - v4
    Checksum:i4D86F3C9D1A3DF9E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971A → G in AAA66054. (PubMed:8088826)Curated
    Sequence conflicti117 – 1171T → A in AAA37373. (PubMed:2268310)Curated
    Sequence conflicti117 – 1171T → A in CAA36342. (PubMed:2395665)Curated
    Sequence conflicti117 – 1171T → A in AAA66054. (PubMed:8088826)Curated
    Sequence conflicti117 – 1171T → A in AAH13447. (PubMed:16141072)Curated
    Sequence conflicti316 – 3161L → V in AAA66054. (PubMed:8088826)Curated
    Sequence conflicti350 – 3501M → K in AAA66054. (PubMed:8088826)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62897 mRNA. Translation: AAA37373.1.
    X52108 mRNA. Translation: CAA36342.1.
    L25069 mRNA. Translation: AAA66054.1.
    AK150893 mRNA. Translation: BAE29939.1.
    AK159152 mRNA. Translation: BAE34859.1.
    AK159885 mRNA. Translation: BAE35454.1.
    AK159891 mRNA. Translation: BAE35458.1.
    AK169069 mRNA. Translation: BAE40856.1.
    AL773505 Genomic DNA. Translation: CAM17512.1.
    CH466519 Genomic DNA. Translation: EDL27697.1.
    BC013447 mRNA. Translation: AAH13447.1.
    M29394 mRNA. Translation: AAA37371.1.
    CCDSiCCDS16478.1.
    PIRiA36695.
    RefSeqiNP_033934.2. NM_009804.2.
    UniGeneiMm.4215.

    Genome annotation databases

    EnsembliENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
    GeneIDi12359.
    KEGGimmu:12359.
    UCSCiuc008liw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62897 mRNA. Translation: AAA37373.1 .
    X52108 mRNA. Translation: CAA36342.1 .
    L25069 mRNA. Translation: AAA66054.1 .
    AK150893 mRNA. Translation: BAE29939.1 .
    AK159152 mRNA. Translation: BAE34859.1 .
    AK159885 mRNA. Translation: BAE35454.1 .
    AK159891 mRNA. Translation: BAE35458.1 .
    AK169069 mRNA. Translation: BAE40856.1 .
    AL773505 Genomic DNA. Translation: CAM17512.1 .
    CH466519 Genomic DNA. Translation: EDL27697.1 .
    BC013447 mRNA. Translation: AAH13447.1 .
    M29394 mRNA. Translation: AAA37371.1 .
    CCDSi CCDS16478.1.
    PIRi A36695.
    RefSeqi NP_033934.2. NM_009804.2.
    UniGenei Mm.4215.

    3D structure databases

    ProteinModelPortali P24270.
    SMRi P24270. Positions 4-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P24270. 3 interactions.
    MINTi MINT-1859622.

    PTM databases

    PhosphoSitei P24270.

    2D gel databases

    SWISS-2DPAGE P24270.

    Proteomic databases

    MaxQBi P24270.
    PaxDbi P24270.
    PRIDEi P24270.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028610 ; ENSMUSP00000028610 ; ENSMUSG00000027187 .
    GeneIDi 12359.
    KEGGi mmu:12359.
    UCSCi uc008liw.2. mouse.

    Organism-specific databases

    CTDi 847.
    MGIi MGI:88271. Cat.

    Phylogenomic databases

    eggNOGi COG0753.
    GeneTreei ENSGT00390000018100.
    HOGENOMi HOG000087852.
    HOVERGENi HBG003986.
    InParanoidi Q3TXQ6.
    KOi K03781.
    OMAi EVEQMAY.
    OrthoDBi EOG7V7660.
    TreeFami TF300540.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi CAT. mouse.
    NextBioi 281024.
    PROi P24270.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24270.
    Bgeei P24270.
    CleanExi MM_CAT.
    Genevestigatori P24270.

    Family and domain databases

    Gene3Di 2.40.180.10. 1 hit.
    InterProi IPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024711. Catalase_clade1/3.
    IPR011614. Catalase_core.
    IPR002226. Catalase_haem_BS.
    IPR010582. Catalase_immune_responsive.
    [Graphical view ]
    PANTHERi PTHR11465. PTHR11465. 1 hit.
    Pfami PF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSi PR00067. CATALASE.
    SMARTi SM01060. Catalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56634. SSF56634. 1 hit.
    PROSITEi PS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H/CS(A).
      Tissue: Kidney and Liver.
    2. "Nucleotide and deduced amino acid sequences of mouse catalase: molecular analysis of a low activity mutant."
      Shaffer J.B., Preston K.E., Shepard B.A.
      Nucleic Acids Res. 18:4941-4941(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H/CS(A) and C3H/HeJ.
      Tissue: Liver.
    3. "Complete cDNA and 5' genomic sequences and multilevel regulation of the mouse catalase gene."
      Reimer D.L., Bailley J., Singh S.M.
      Genomics 21:325-336(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    4. "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.
      Tissue: Amnion and Bone marrow.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: FVB/N.
      Tissue: Kidney.
    8. Kanor S., Quadroni M., Bienvenut W.V.
      Submitted (MAR-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6J.
      Tissue: Skeletal muscle.
    9. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 48-66, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    10. "Isolation of a cDNA clone for murine catalase and analysis of an acatalasemic mutant."
      Shaffer J.B., Sutton R.B., Bewley G.C.
      J. Biol. Chem. 262:12908-12911(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 503-527.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-449, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-221; LYS-306; LYS-430; LYS-449; LYS-480 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    13. "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-233; LYS-306; LYS-430; LYS-449; LYS-480 AND LYS-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiCATA_MOUSE
    AccessioniPrimary (citable) accession number: P24270
    Secondary accession number(s): Q3TXQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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