ID   CATA_CANLF              Reviewed;         527 AA.
AC   O97492; Q9GKY3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=CAT;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=10524763; DOI=10.3109/10425179809008475;
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   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 peroxide.
CC       Promotes growth of cells.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in CAT are the cause of acatalasia; also known as
CC       acatalasemia. This disease is characterized by absence of catalase
CC       activity. {ECO:0000269|PubMed:11137458}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AB012918; BAA36420.1; -; mRNA.
DR   EMBL; AB038231; BAB20764.1; -; mRNA.
DR   RefSeq; NP_001002984.1; NM_001002984.1.
DR   AlphaFoldDB; O97492; -.
DR   SMR; O97492; -.
DR   STRING; 9615.ENSCAFP00000010324; -.
DR   PeroxiBase; 5319; CfaKat01.
DR   PaxDb; O97492; -.
DR   PRIDE; O97492; -.
DR   Ensembl; ENSCAFT00030042809; ENSCAFP00030037354; ENSCAFG00030023279.
DR   Ensembl; ENSCAFT00845042560; ENSCAFP00845033366; ENSCAFG00845024098.
DR   GeneID; 403474; -.
DR   KEGG; cfa:403474; -.
DR   CTD; 847; -.
DR   VEuPathDB; HostDB:ENSCAFG00845024098; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   GeneTree; ENSGT00390000018100; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   InParanoid; O97492; -.
DR   OMA; WTCYVQV; -.
DR   OrthoDB; 507937at2759; -.
DR   TreeFam; TF300540; -.
DR   Reactome; R-CFA-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-CFA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000002254; Chromosome 18.
DR   GO; GO:0062151; C:catalase complex; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0004046; F:aminoacylase activity; IEA:Ensembl.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:Ensembl.
DR   GO; GO:0000268; F:peroxisome targeting sequence binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0009060; P:aerobic respiration; IEA:Ensembl.
DR   GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR   GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR   GO; GO:0009650; P:UV protection; IEA:Ensembl.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
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   InterPro; IPR020835; Catalase_sf.
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   1: Evidence at protein level;
KW   Acetylation; Disease variant; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   CHAIN           2..527
FT                   /note="Catalase"
FT                   /id="PRO_0000084899"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         358
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   MOD_RES         13
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         221
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         233
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         449
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         449
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         480
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         480
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         499
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         511
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   VARIANT         327
FT                   /note="A -> T (in acatalasemia; heat-labile)"
FT                   /evidence="ECO:0000269|PubMed:11137458"
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