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Catalase (EC 1.11.1.6)

 CATA_RAT                Reviewed;         527 AA.
P04762;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 156.
RecName: Full=Catalase;
EC=1.11.1.6;
Name=Cat; Synonyms=Cas1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3455767; DOI=10.1073/pnas.83.2.313;
Furuta S., Hayashi H., Hijikata M., Miyazawa S., Osumi T.,
Hashimoto T.;
"Complete nucleotide sequence of cDNA and deduced amino acid sequence
of rat liver catalase.";
Proc. Natl. Acad. Sci. U.S.A. 83:313-317(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=2792765; DOI=10.1016/0378-1119(89)90210-2;
Nakashima H., Yamamoto M., Goto K., Osumi T., Hashimoto T., Endo H.;
"Isolation and characterization of the rat catalase-encoding gene.";
Gene 79:279-288(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 399-527.
PubMed=6547842; DOI=10.1016/S0006-291X(84)80109-6;
Osumi T., Ozasa H., Miyazawa S., Hashimoto T.;
"Molecular cloning of cDNA for rat liver catalase.";
Biochem. Biophys. Res. Commun. 122:831-837(1984).
[5]
PROTEIN SEQUENCE OF 481-492, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND SER-517, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Occurs in almost all aerobically respiring organisms and
serves to protect cells from the toxic effects of hydrogen
peroxide. Promotes growth of cells.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349;
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M11670; AAA40884.1; -; mRNA.
EMBL; M25680; AAB42378.1; -; Genomic_DNA.
EMBL; M25669; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25670; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25671; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25672; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25673; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25674; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25675; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25676; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25677; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25678; AAB42378.1; JOINED; Genomic_DNA.
EMBL; M25679; AAB42378.1; JOINED; Genomic_DNA.
EMBL; BC081853; AAH81853.1; -; mRNA.
EMBL; K01929; AAA40885.1; -; mRNA.
PIR; JU0065; CSRT.
RefSeq; NP_036652.1; NM_012520.2.
UniGene; Rn.3001; -.
ProteinModelPortal; P04762; -.
SMR; P04762; -.
BioGrid; 246433; 3.
IntAct; P04762; 2.
STRING; 10116.ENSRNOP00000011230; -.
ChEMBL; CHEMBL1075216; -.
PeroxiBase; 11811; RnoKat.
iPTMnet; P04762; -.
PhosphoSitePlus; P04762; -.
PaxDb; P04762; -.
PRIDE; P04762; -.
Ensembl; ENSRNOT00000011230; ENSRNOP00000011230; ENSRNOG00000008364.
GeneID; 24248; -.
KEGG; rno:24248; -.
UCSC; RGD:2279; rat.
CTD; 847; -.
RGD; 2279; Cat.
eggNOG; KOG0047; Eukaryota.
eggNOG; COG0753; LUCA.
GeneTree; ENSGT00390000018100; -.
HOGENOM; HOG000087852; -.
HOVERGEN; HBG003986; -.
InParanoid; P04762; -.
KO; K03781; -.
OMA; HADFGRM; -.
OrthoDB; EOG091G04V5; -.
PhylomeDB; P04762; -.
TreeFam; TF300540; -.
BRENDA; 1.11.1.6; 5301.
Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P04762; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000008364; -.
Genevisible; P04762; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
GO; GO:0005777; C:peroxisome; IDA:HGNC.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0004046; F:aminoacylase activity; IEA:Ensembl.
GO; GO:0004096; F:catalase activity; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050661; F:NADP binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0009060; P:aerobic respiration; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:RGD.
GO; GO:0001822; P:kidney development; IMP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IMP:RGD.
GO; GO:0014854; P:response to inactivity; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0009642; P:response to light intensity; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
GO; GO:0010193; P:response to ozone; IEP:RGD.
GO; GO:0080184; P:response to phenylpropanoid; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0000302; P:response to reactive oxygen species; IMP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0009411; P:response to UV; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0033197; P:response to vitamin E; IEP:RGD.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; IMP:RGD.
GO; GO:0009650; P:UV protection; IEA:Ensembl.
Gene3D; 2.40.180.10; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024711; Catalase_clade1/3.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
PANTHER; PTHR11465; PTHR11465; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
PIRSF; PIRSF038928; Catalase_clade1-3; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; Heme;
Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase;
Peroxidase; Peroxisome; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04040}.
CHAIN 2 527 Catalase.
/FTId=PRO_0000084905.
ACT_SITE 75 75 {ECO:0000255|PROSITE-ProRule:PRU10013}.
ACT_SITE 148 148 {ECO:0000255|PROSITE-ProRule:PRU10013}.
METAL 358 358 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 13 13 N6-succinyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 221 221 N6-succinyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 306 306 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 306 306 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 449 449 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 449 449 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 480 480 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 480 480 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 511 511 Phosphothreonine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 522 522 N6-succinyllysine.
{ECO:0000250|UniProtKB:P24270}.
CONFLICT 434 434 S -> N (in Ref. 4; AAA40885).
{ECO:0000305}.
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


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