ID   CATA_MOUSE              Reviewed;         527 AA.
AC   P24270;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 88.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=Cat; Synonyms=Cas-1, Cas1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/CS(A); TISSUE=Kidney, and Liver;
RX   MEDLINE=91097527; PubMed=2268310; DOI=10.1016/S0006-291X(05)80891-5;
RA   Shaffer J.B., Preston K.E.;
RT   "Molecular analysis of an acatalasemic mouse mutant.";
RL   Biochem. Biophys. Res. Commun. 173:1043-1050(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/CS(A), and C3H/HeJ; TISSUE=Liver;
RX   MEDLINE=90370504; PubMed=2395665; DOI=10.1093/nar/18.16.4941;
RA   Shaffer J.B., Preston K.E., Shepard B.A.;
RT   "Nucleotide and deduced amino acid sequences of mouse catalase:
RT   molecular analysis of a low activity mutant.";
RL   Nucleic Acids Res. 18:4941-4941(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=94375055; PubMed=8088826; DOI=10.1006/geno.1994.1273;
RA   Reimer D.L., Bailley J., Singh S.M.;
RT   "Complete cDNA and 5' genomic sequences and multilevel regulation of
RT   the mouse catalase gene.";
RL   Genomics 21:325-336(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA   Kanor S., Quadroni M., Bienvenut W.V.;
RL   Submitted (MAR-2006) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 503-527.
RX   MEDLINE=88007481; PubMed=3654595;
RA   Shaffer J.B., Sutton R.B., Bewley G.C.;
RT   "Isolation of a cDNA clone for murine catalase and analysis of an
RT   acatalasemic mutant.";
RL   J. Biol. Chem. 262:12908-12911(1987).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-422 AND SER-517,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide. Promotes growth of cells.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- COFACTOR: NADP.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; M62897; AAA37373.1; -; mRNA.
DR   EMBL; X52108; CAA36342.1; -; mRNA.
DR   EMBL; L25069; AAA66054.1; -; mRNA.
DR   EMBL; BC013447; AAH13447.1; -; mRNA.
DR   EMBL; M29394; AAA37371.1; -; mRNA.
DR   PIR; A36695; A36695.
DR   UniGene; Mm.4215; -.
DR   HSSP; P00432; 4BLC.
DR   SMR; P24270; 5-501.
DR   PhosphoSite; P24270; -.
DR   SWISS-2DPAGE; P24270; -.
DR   Ensembl; ENSMUSG00000027187; Mus musculus.
DR   MGI; MGI:88271; Cat.
DR   HOGENOM; P24270; -.
DR   HOVERGEN; P24270; -.
DR   ArrayExpress; P24270; -.
DR   CleanEx; MM_CAT; -.
DR   GermOnline; ENSMUSG00000027187; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
DR   GO; GO:0004046; F:aminoacylase activity; IMP:MGI.
DR   GO; GO:0004096; F:catalase activity; IDA:MGI.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
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:0032088; P:negative regulation of NF-kappaB transcript...; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcript...; IDA:MGI.
DR   GO; GO:0014068; P:positive regulation of phosphoinositide 3-k...; IDA:MGI.
DR   GO; GO:0006641; P:triacylglycerol metabolic process; IMP:MGI.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    527       Catalase.
FT                                /FTId=PRO_0000084902.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    148    148       By similarity.
FT   METAL       358    358       Iron (heme axial ligand) (By similarity).
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     231    231       Phosphotyrosine (By similarity).
FT   MOD_RES     308    308       Phosphotyrosine (By similarity).
FT   MOD_RES     422    422       Phosphoserine.
FT   MOD_RES     517    517       Phosphoserine.
FT   MUTAGEN      11     11       Q->H: Acatalasemia.
FT   CONFLICT     97     97       A -> G (in Ref. 3; AAA66054).
FT   CONFLICT    316    316       L -> V (in Ref. 3; AAA66054).
FT   CONFLICT    350    350       M -> K (in Ref. 3; AAA66054).
SQ   SEQUENCE   527 AA;  59765 MW;  2D5C4195F63FF4BF CRC64;
     MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE
     MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVAGES
     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 QLFIQKKAVK
     NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL
//