ID   CATA_RAT                Reviewed;         527 AA.
AC   P04762;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013};
GN   Name=Cat; Synonyms=Cas1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=3455767; DOI=10.1073/pnas.83.2.313;
RA   Furuta S., Hayashi H., Hijikata M., Miyazawa S., Osumi T., Hashimoto T.;
RT   "Complete nucleotide sequence of cDNA and deduced amino acid sequence of
RT   rat liver catalase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:313-317(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=2792765; DOI=10.1016/0378-1119(89)90210-2;
RA   Nakashima H., Yamamoto M., Goto K., Osumi T., Hashimoto T., Endo H.;
RT   "Isolation and characterization of the rat catalase-encoding gene.";
RL   Gene 79:279-288(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 399-527.
RX   PubMed=6547842; DOI=10.1016/s0006-291x(84)80109-6;
RA   Osumi T., Ozasa H., Miyazawa S., Hashimoto T.;
RT   "Molecular cloning of cDNA for rat liver catalase.";
RL   Biochem. Biophys. Res. Commun. 122:831-837(1984).
RN   [5]
RP   PROTEIN SEQUENCE OF 481-492, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND SER-517, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2))
CC       generated by peroxisomal oxidases to water and oxygen, thereby
CC       protecting cells from the toxic effects of hydrogen peroxide. Promotes
CC       growth of cells including T-cells, B-cells, myeloid leukemia cells,
CC       melanoma cells, mastocytoma cells and normal and transformed fibroblast
CC       cells. {ECO:0000250|UniProtKB:P04040}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P04040};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P04040};
CC   -!- SUBUNIT: Homotetramer. Interacts (via microbody targeting signal) with
CC       PEX5, monomeric form interacts with PEX5, leading to its translocation
CC       into peroxisomes. {ECO:0000250|UniProtKB:P04040}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P04040}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; M11670; AAA40884.1; -; mRNA.
DR   EMBL; M25680; AAB42378.1; -; Genomic_DNA.
DR   EMBL; M25669; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25670; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25671; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25672; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25673; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25674; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25675; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25676; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25677; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25678; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; M25679; AAB42378.1; JOINED; Genomic_DNA.
DR   EMBL; BC081853; AAH81853.1; -; mRNA.
DR   EMBL; K01929; AAA40885.1; -; mRNA.
DR   PIR; JU0065; CSRT.
DR   RefSeq; NP_036652.1; NM_012520.2.
DR   AlphaFoldDB; P04762; -.
DR   SMR; P04762; -.
DR   BioGRID; 246433; 5.
DR   IntAct; P04762; 3.
DR   STRING; 10116.ENSRNOP00000011230; -.
DR   BindingDB; P04762; -.
DR   ChEMBL; CHEMBL1075216; -.
DR   PeroxiBase; 11811; RnoKat.
DR   CarbonylDB; P04762; -.
DR   GlyGen; P04762; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P04762; -.
DR   PhosphoSitePlus; P04762; -.
DR   SwissPalm; P04762; -.
DR   jPOST; P04762; -.
DR   PaxDb; 10116-ENSRNOP00000011230; -.
DR   Ensembl; ENSRNOT00000011230.6; ENSRNOP00000011230.4; ENSRNOG00000008364.7.
DR   Ensembl; ENSRNOT00055000340; ENSRNOP00055000232; ENSRNOG00055000198.
DR   Ensembl; ENSRNOT00060002762; ENSRNOP00060001804; ENSRNOG00060001791.
DR   Ensembl; ENSRNOT00065028977; ENSRNOP00065022943; ENSRNOG00065017370.
DR   GeneID; 24248; -.
DR   KEGG; rno:24248; -.
DR   UCSC; RGD:2279; rat.
DR   AGR; RGD:2279; -.
DR   CTD; 847; -.
DR   RGD; 2279; Cat.
DR   eggNOG; KOG0047; Eukaryota.
DR   GeneTree; ENSGT00390000018100; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   InParanoid; P04762; -.
DR   OMA; KFRWNVF; -.
DR   OrthoDB; 3198922at2759; -.
DR   PhylomeDB; P04762; -.
DR   TreeFam; TF300540; -.
DR   BRENDA; 1.11.1.6; 5301.
DR   Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-9033241; Peroxisomal protein import.
DR   PRO; PR:P04762; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000008364; Expressed in liver and 19 other cell types or tissues.
DR   GO; GO:0062151; C:catalase complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:Ensembl.
DR   GO; GO:0005778; C:peroxisomal membrane; ISO:RGD.
DR   GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0004046; F:aminoacylase activity; ISO:RGD.
DR   GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR   GO; GO:0004096; F:catalase activity; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0020037; F:heme binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; ISO:RGD.
DR   GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0009060; P:aerobic respiration; ISO:RGD.
DR   GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; ISO:RGD.
DR   GO; GO:0098869; P:cellular oxidant detoxification; ISO:RGD.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR   GO; GO:0020027; P:hemoglobin metabolic process; ISO:RGD.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:RGD.
DR   GO; GO:0001822; P:kidney development; IMP:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD.
DR   GO; GO:0014823; P:response to activity; IEP:RGD.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IMP:RGD.
DR   GO; GO:0014854; P:response to inactivity; IEP:RGD.
DR   GO; GO:0032868; P:response to insulin; IEP:RGD.
DR   GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR   GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR   GO; GO:0009642; P:response to light intensity; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR   GO; GO:0010193; P:response to ozone; IEP:RGD.
DR   GO; GO:0080184; P:response to phenylpropanoid; IEP:RGD.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   GO; GO:0009411; P:response to UV; IEP:RGD.
DR   GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR   GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR   GO; GO:0001657; P:ureteric bud development; IMP:RGD.
DR   GO; GO:0009650; P:UV protection; ISO:RGD.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 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; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
DR   Genevisible; P04762; RN.
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; 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_0000084905"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           524..527
FT                   /note="Microbody targeting signal; atypical"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
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         194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   BINDING         201
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   BINDING         203
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   BINDING         213
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   BINDING         237
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   BINDING         303
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   BINDING         305
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   BINDING         306
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
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|UniProtKB:P04040"
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         306
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         306
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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         511
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04040"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         522
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24270"
FT   CONFLICT        434
FT                   /note="S -> N (in Ref. 4; AAA40885)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   527 AA;  59757 MW;  CA28530A0FC6EFA6 CRC64;
     MADSRDPASD QMKQWKEQRA PQKPDVLTTG GGNPIGDKLN IMTAGPRGPL LVQDVVFTDE
     MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVAGES
     GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAML FPSFIHSQKR NPQTHLKDPD
     MVWDFWSLCP ESLHQVTFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ
     GIKNLPVEEA GRLAQEDPDY GLRDLFNAIA SGNYPSWTFY IQVMTFKEAE TFPFNPFDLT
     KVWPHKDYPL IPVGKLVLNR NPANYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD
     THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG APNYYPNSFS APEQQGSALE
     HHSQCSADVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIANHLKDA QLFIQRKAVK
     NFTDVHPDYG ARVQALLDQY NSQKPKNAIH TYVQAGSHIA AKGKANL
//