ID   CATA_CANFA              Reviewed;         527 AA.
AC   O97492; Q9GKY3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=CAT;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=10524763;
RA   Nakamura K., Watanabe M., Ikeda T.;
RT   "cDNA and deduced amino acid sequences of dog catalase.";
RL   DNA Seq. 9:347-352(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ACATALASEMIA THR-327.
RC   STRAIN=Beagle;
RX   MEDLINE=20579473; PubMed=11137458; DOI=10.1016/S1357-2725(00)00057-1;
RA   Nakamura K., Watanabe M., Takanaka K., Sasaki Y., Ikeda T.;
RT   "cDNA cloning of mutant catalase in acatalasemic beagle dog: single
RT   nucleotide substitution leading to thermal-instability and enhanced
RT   proteolysis of mutant enzyme.";
RL   Int. J. Biochem. Cell Biol. 32:1183-1193(2000).
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 (By similarity).
CC   -!- COFACTOR: NADP (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- DISEASE: Defects in CAT are the cause of acatalasia; also known as
CC       acatalasemia. This disease is characterized by absence of catalase
CC       activity.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AB012918; BAA36420.1; -; mRNA.
DR   EMBL; AB038231; BAB20764.1; -; mRNA.
DR   RefSeq; NP_001002984.1; -.
DR   UniGene; Cfa.188; -.
DR   HSSP; P00432; 4BLC.
DR   SMR; O97492; 5-501.
DR   PeroxiBase; 5319; CfaKat01.
DR   Ensembl; ENSCAFG00000006941; Canis familiaris.
DR   GeneID; 403474; -.
DR   KEGG; cfa:403474; -.
DR   HOVERGEN; O97492; -.
DR   BRENDA; 1.11.1.6; 463.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008283; P:cell proliferation; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
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   Disease mutation; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    527       Catalase.
FT                                /FTId=PRO_0000084899.
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     231    231       Phosphotyrosine (By similarity).
FT   MOD_RES     308    308       Phosphotyrosine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   VARIANT     327    327       A -> T (in acatalasemia; heat-labile).
SQ   SEQUENCE   527 AA;  59797 MW;  CC0BC7F88FE2C2AC CRC64;
     MADSRDPASD QMKLWKEQRA AQKPDVLTTG GGNPIGDKLN VMTAGPRGPL LVQDVVFTDE
     MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKRTPIA VRFSTVAGES
     GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD
     MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNAAGEAV YCKFHYKTDQ
     GIKNLSVEDA ARLSHEDPDY GLRDLFNAIA TGNYPSWTFY IQVMTFSQAE TFPFNPFDLT
     KIWPHQDYPL IPVGKLVLNR NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD
     THRHRLGPNY LQIPVNCPFR ARVANYQRDG PMCMLDNQGG APNYYPNSFS APEQQRCVLE
     HSSQCSPDVQ RFNSANEDNV TQVRTFYLKV LGEEERKRLC ENIAGHLKDA QLFIQKKAVK
     NFSDVHPDYG ARIQALLDKY NAEKPKNAIH TFMQHGSHLA AREKANL
//