ID Q3UZE7_MOUSE Unreviewed; 527 AA. AC Q3UZE7; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 27-MAY-2015, entry version 74. DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498}; DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498}; GN Name=Cat {ECO:0000313|MGI:MGI:88271}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE21910.1}; RN [1] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., RA Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., RA Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N., RA Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D., RA Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A., RA Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE21910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21910.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE21910.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and CC serves to protect cells from the toxic effects of hydrogen CC peroxide. {ECO:0000256|RuleBase:RU004142}. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC {ECO:0000256|RuleBase:RU000498}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038928-2}; CC -!- SIMILARITY: Belongs to the catalase family. CC {ECO:0000256|RuleBase:RU000498}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK133881; BAE21910.1; -; mRNA. DR UniGene; Mm.4215; -. DR ProteinModelPortal; Q3UZE7; -. DR SMR; Q3UZE7; 4-501. DR PeroxiBase; 5275; MmKat01. DR PRIDE; Q3UZE7; -. DR MGI; MGI:88271; Cat. DR HOVERGEN; HBG003986; -. DR ChiTaRS; Cat; mouse. DR Genevestigator; Q3UZE7; -. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005925; C:focal adhesion; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005778; C:peroxisomal membrane; IDA:MGI. DR GO; GO:0005777; C:peroxisome; IDA:MGI. DR GO; GO:0004046; F:aminoacylase activity; IMP:MGI. DR GO; GO:0016209; F:antioxidant activity; ISO:MGI. DR GO; GO:0004096; F:catalase activity; IDA:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0020037; F:heme binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; ISO:MGI. DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0005102; F:receptor binding; ISO:MGI. DR GO; GO:0009060; P:aerobic respiration; IMP:MGI. DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI. DR GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI. DR GO; GO:0001649; P:osteoblast differentiation; ISO:MGI. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI. DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI. DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI. DR GO; GO:0051262; P:protein tetramerization; ISO:MGI. DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI. DR GO; GO:0000302; P:response to reactive oxygen species; ISO:MGI. DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI. DR GO; GO:0009650; P:UV protection; ISO:MGI. DR Gene3D; 2.40.180.10; -; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR020835; Catalase-like_dom. DR InterPro; IPR024708; Catalase_AS. DR InterPro; IPR024711; Catalase_clade1/3. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR002226; Catalase_haem_BS. DR InterPro; IPR010582; Catalase_immune_responsive. DR PANTHER; PTHR11465; PTHR11465; 1. DR Pfam; PF00199; Catalase; 1. DR Pfam; PF06628; Catalase-rel; 1. DR PIRSF; PIRSF038928; Catalase_clade1-3; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF56634; SSF56634; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 2: Evidence at transcript level; KW Heme {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU000498}; KW Iron {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2, KW ECO:0000256|RuleBase:RU000498}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000498}; KW Peroxidase {ECO:0000256|RuleBase:RU000498}. FT ACT_SITE 75 75 {ECO:0000256|PIRSR:PIRSR038928-1}. FT ACT_SITE 148 148 {ECO:0000256|PIRSR:PIRSR038928-1}. FT METAL 358 358 Iron (heme axial ligand). FT {ECO:0000256|PIRSR:PIRSR038928-2}. SQ SEQUENCE 527 AA; 59795 MW; 1786F3C9C07504E2 CRC64; MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVTGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ GIKNLPVGEA GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG APNYYPNSFS APEQQRSALE HSVQCAVDVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIAGHLKDA QLFIKKKAVK NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL //