CATA_RAT
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 03-AUG-2022, entry version 179.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
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: 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;
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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; 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 iPTMnet; P04762; -.
DR PhosphoSitePlus; P04762; -.
DR jPOST; P04762; -.
DR PaxDb; P04762; -.
DR PRIDE; P04762; -.
DR Ensembl; ENSRNOT00000011230; ENSRNOP00000011230; ENSRNOG00000008364.
DR GeneID; 24248; -.
DR KEGG; rno:24248; -.
DR UCSC; RGD:2279; rat.
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; WTCYVQV; -.
DR OrthoDB; 507937at2759; -.
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 tissues.
DR Genevisible; P04762; RN.
DR GO; GO:0062151; C:catalase complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
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:0000268; F:peroxisome targeting sequence binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0009060; P:aerobic respiration; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; 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:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; 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:0009314; P:response to radiation; 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 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; 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 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 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
