CATA_HUMAN
ID CATA_HUMAN Reviewed; 527 AA.
AC P04040; A8K6C0; B2RCZ9; D3DR07; Q2M1U4; Q4VXX5; Q9BWT9; Q9UC85;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=CAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3755525; DOI=10.1093/nar/14.13.5321;
RA Quan F., Korneluk R.G., Tropak M.B., Gravel R.A.;
RT "Isolation and characterization of the human catalase gene.";
RL Nucleic Acids Res. 14:5321-5335(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=3755526;
RA Bell G.I., Najarian R.C., Mullenbach G.T., Hallewell R.A.;
RT "cDNA sequence coding for human kidney catalase.";
RL Nucleic Acids Res. 14:5561-5562(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=11728823; DOI=10.1016/s0891-5849(01)00734-1;
RA Jin L.H., Bahn J.H., Eum W.S., Kwon H.Y., Jang S.H., Han K.H., Kang T.-C.,
RA Won M.H., Kang J.H., Cho S.-W., Park J., Choi S.Y.;
RT "Transduction of human catalase mediated by an HIV-1 TAT protein basic
RT domain and arginine-rich peptides into mammalian cells.";
RL Free Radic. Biol. Med. 31:1509-1519(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=8282800; DOI=10.1172/jci116959;
RA Yoo J.-H., Erzurum S.C., Hay J.G., Lemarchand P., Crystal R.G.;
RT "Vulnerability of the human airway epithelium to hyperoxia. Constitutive
RT expression of the catalase gene in human bronchial epithelial cells despite
RT oxidant stress.";
RL J. Clin. Invest. 93:297-302(1994).
RN [10]
RP PROTEIN SEQUENCE OF 2-19.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP PROTEIN SEQUENCE OF 24-38; 99-105; 307-315 AND 469-476, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Erythrocyte;
RX PubMed=7882369;
RA Takeuchi A., Miyamoto T., Yamaji K., Masuho Y., Hayashi M., Hayashi H.,
RA Onozaki K.;
RT "A human erythrocyte-derived growth-promoting factor with a wide target
RT cell spectrum: identification as catalase.";
RL Cancer Res. 55:1586-1589(1995).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-527.
RC TISSUE=Fibroblast;
RX PubMed=6548744; DOI=10.1016/s0021-9258(18)89819-2;
RA Korneluk R.G., Quan F., Lewis W.H., Guise K.S., Willard H.F., Holmes M.T.,
RA Gravel R.A.;
RT "Isolation of human fibroblast catalase cDNA clones. Sequence of clones
RT derived from spliced and unspliced mRNA.";
RL J. Biol. Chem. 259:13819-13823(1984).
RN [13]
RP PROTEIN SEQUENCE OF 445-456, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [14]
RP INVOLVEMENT IN ACATLAS.
RX PubMed=2308162; DOI=10.1016/0022-2836(90)90359-t;
RA Wen J.K., Osumi T., Hashimoto T., Ogata M.;
RT "Molecular analysis of human acatalasemia. Identification of a splicing
RT mutation.";
RL J. Mol. Biol. 211:383-393(1990).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-422; THR-511; SER-515
RP AND SER-517, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RX PubMed=10666617; DOI=10.1107/s0907444999015930;
RA Ko T.P., Safo M.K., Musayev F.N., Di Salvo M.L., Wang C., Wu S.H.,
RA Abraham D.J.;
RT "Structure of human erythrocyte catalase.";
RL Acta Crystallogr. D 56:241-245(2000).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=10656833; DOI=10.1006/jmbi.1999.3458;
RA Putnam C.D., Arvai A.S., Bourne Y., Tainer J.A.;
RT "Active and inhibited human catalase structures: ligand and NADPH binding
RT and catalytic mechanism.";
RL J. Mol. Biol. 296:295-309(2000).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=11134921; DOI=10.1107/s0907444900013767;
RA Safo M.K., Musayev F.N., Wu S.H., Abraham D.J., Ko T.P.;
RT "Structure of tetragonal crystals of human erythrocyte catalase.";
RL Acta Crystallogr. D 57:1-7(2001).
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 including T-cells, B-cells, myeloid leukemia
CC cells, melanoma cells, mastocytoma cells and normal and transformed
CC fibroblast cells. {ECO:0000269|PubMed:7882369}.
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 ECO:0000269|PubMed:7882369};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P04040; P04040: CAT; NbExp=5; IntAct=EBI-2432181, EBI-2432181;
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISEASE: Acatalasemia (ACATLAS) [MIM:614097]: A metabolic disorder
CC characterized by a total or near total loss of catalase activity in red
CC cells. It is often associated with ulcerating oral lesions.
CC Acatalasemia is inherited as an autosomal recessive trait.
CC {ECO:0000269|PubMed:2308162}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Catalase entry;
CC URL="https://en.wikipedia.org/wiki/Catalase";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/cat/";
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DR EMBL; X04085; CAA27721.1; -; Genomic_DNA.
DR EMBL; X04086; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04087; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04088; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04089; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04090; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04091; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04092; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04093; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04094; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04095; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04096; CAA27721.1; JOINED; Genomic_DNA.
DR EMBL; X04076; CAA27717.1; -; mRNA.
DR EMBL; AY028632; AAK29181.1; -; mRNA.
DR EMBL; AK291585; BAF84274.1; -; mRNA.
DR EMBL; AK315350; BAG37746.1; -; mRNA.
DR EMBL; AY545477; AAS37679.1; -; Genomic_DNA.
DR EMBL; AL035079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68170.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68171.1; -; Genomic_DNA.
DR EMBL; BC110398; AAI10399.1; -; mRNA.
DR EMBL; BC112217; AAI12218.1; -; mRNA.
DR EMBL; BC112219; AAI12220.1; -; mRNA.
DR EMBL; L13609; AAA16651.1; -; Genomic_DNA.
DR EMBL; K02400; AAB59522.1; -; Genomic_DNA.
DR CCDS; CCDS7891.1; -.
DR PIR; A23646; CSHU.
DR RefSeq; NP_001743.1; NM_001752.3.
DR PDB; 1DGB; X-ray; 2.20 A; A/B/C/D=4-501.
DR PDB; 1DGF; X-ray; 1.50 A; A/B/C/D=5-501.
DR PDB; 1DGG; X-ray; 1.80 A; A/B/C/D=5-501.
DR PDB; 1DGH; X-ray; 2.00 A; A/B/C/D=4-501.
DR PDB; 1F4J; X-ray; 2.40 A; A/B/C/D=1-527.
DR PDB; 1QQW; X-ray; 2.75 A; A/B/C/D=1-527.
DR PDB; 7P8W; EM; 2.20 A; A/B/C/D=1-527.
DR PDB; 7VD9; EM; 2.29 A; A/B/C/D=1-527.
DR PDBsum; 1DGB; -.
DR PDBsum; 1DGF; -.
DR PDBsum; 1DGG; -.
DR PDBsum; 1DGH; -.
DR PDBsum; 1F4J; -.
DR PDBsum; 1QQW; -.
DR PDBsum; 7P8W; -.
DR PDBsum; 7VD9; -.
DR AlphaFoldDB; P04040; -.
DR PCDDB; P04040; -.
DR SMR; P04040; -.
DR BioGRID; 107297; 136.
DR ComplexPortal; CPX-4742; Catalase complex.
DR ELM; P04040; -.
DR IntAct; P04040; 91.
DR MINT; P04040; -.
DR STRING; 9606.ENSP00000241052; -.
DR BindingDB; P04040; -.
DR ChEMBL; CHEMBL3627594; -.
DR DrugBank; DB09096; Benzoyl peroxide.
DR DrugBank; DB09116; Calcium carbimide.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB01213; Fomepizole.
DR DrugBank; DB11091; Hydrogen peroxide.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR PeroxiBase; 5282; HsKat01.
DR GlyConnect; 1925; 16 N-Linked glycans (3 sites), 1 O-Linked glycan (2 sites).
DR GlyGen; P04040; 5 sites, 16 N-linked glycans (3 sites), 1 O-linked glycan (2 sites).
DR iPTMnet; P04040; -.
DR PhosphoSitePlus; P04040; -.
DR SwissPalm; P04040; -.
DR BioMuta; CAT; -.
DR DMDM; 115702; -.
DR OGP; P04040; -.
DR REPRODUCTION-2DPAGE; IPI00465436; -.
DR REPRODUCTION-2DPAGE; P04040; -.
DR SWISS-2DPAGE; P04040; -.
DR CPTAC; CPTAC-472; -.
DR CPTAC; CPTAC-473; -.
DR EPD; P04040; -.
DR jPOST; P04040; -.
DR MassIVE; P04040; -.
DR MaxQB; P04040; -.
DR PaxDb; P04040; -.
DR PeptideAtlas; P04040; -.
DR PRIDE; P04040; -.
DR ProteomicsDB; 51636; -.
DR ABCD; P04040; 4 sequenced antibodies.
DR Antibodypedia; 3595; 968 antibodies from 47 providers.
DR DNASU; 847; -.
DR Ensembl; ENST00000241052.5; ENSP00000241052.4; ENSG00000121691.7.
DR GeneID; 847; -.
DR KEGG; hsa:847; -.
DR MANE-Select; ENST00000241052.5; ENSP00000241052.4; NM_001752.4; NP_001743.1.
DR UCSC; uc001mvm.4; human.
DR CTD; 847; -.
DR DisGeNET; 847; -.
DR GeneCards; CAT; -.
DR HGNC; HGNC:1516; CAT.
DR HPA; ENSG00000121691; Tissue enhanced (liver).
DR MalaCards; CAT; -.
DR MIM; 115500; gene.
DR MIM; 614097; phenotype.
DR neXtProt; NX_P04040; -.
DR OpenTargets; ENSG00000121691; -.
DR Orphanet; 926; Acatalasemia.
DR PharmGKB; PA26099; -.
DR VEuPathDB; HostDB:ENSG00000121691; -.
DR eggNOG; KOG0047; Eukaryota.
DR GeneTree; ENSGT00390000018100; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; P04040; -.
DR OMA; WTCYVQV; -.
DR OrthoDB; 507937at2759; -.
DR PhylomeDB; P04040; -.
DR TreeFam; TF300540; -.
DR BioCyc; MetaCyc:MON66-341; -.
DR BRENDA; 1.11.1.6; 2681.
DR PathwayCommons; P04040; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR SABIO-RK; P04040; -.
DR SignaLink; P04040; -.
DR SIGNOR; P04040; -.
DR BioGRID-ORCS; 847; 11 hits in 1086 CRISPR screens.
DR ChiTaRS; CAT; human.
DR EvolutionaryTrace; P04040; -.
DR GeneWiki; Catalase; -.
DR GenomeRNAi; 847; -.
DR Pharos; P04040; Tbio.
DR PRO; PR:P04040; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P04040; protein.
DR Bgee; ENSG00000121691; Expressed in trabecular bone tissue and 209 other tissues.
DR ExpressionAtlas; P04040; baseline and differential.
DR Genevisible; P04040; HS.
DR GO; GO:0062151; C:catalase complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0004046; F:aminoacylase activity; IEA:Ensembl.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0004096; F:catalase activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; ISS:UniProtKB.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; IDA:ComplexPortal.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; 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; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
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:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0014854; P:response to inactivity; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
DR GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
DR GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
DR GO; GO:0010193; P:response to ozone; IEA:Ensembl.
DR GO; GO:0080184; P:response to phenylpropanoid; IEA:Ensembl.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0009650; P:UV protection; IMP:UniProtKB.
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 3D-structure; Acetylation; Direct protein sequencing; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase;
KW Peroxidase; Peroxisome; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..527
FT /note="Catalase"
FT /id="PRO_0000084901"
FT ACT_SITE 75
FT ACT_SITE 148
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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:0007744|PubMed:24275569"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT 54
FT /note="D -> N (in Ref. 3; AAK29181)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="F -> L (in Ref. 4; BAG37746)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="D -> G (in Ref. 3; AAK29181)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="Y -> D (in Ref. 3; AAK29181)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="K -> R (in Ref. 3; AAK29181)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="L -> P (in Ref. 4; BAG37746)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="N -> D (in Ref. 4; BAG37746)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="Q -> R (in Ref. 3; AAK29181)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="A -> V (in Ref. 3; AAK29181)"
FT /evidence="ECO:0000305"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:1DGF"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1QQW"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1F4J"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:1DGF"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:1DGF"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:1DGF"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:1DGF"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 349..365
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1DGF"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:7VD9"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:1DGF"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7VD9"
FT HELIX 441..449
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 453..467
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 472..485
FT /evidence="ECO:0007829|PDB:1DGF"
FT HELIX 487..500
FT /evidence="ECO:0007829|PDB:1DGF"
SQ SEQUENCE 527 AA; 59756 MW; 7BAA2394D124ED20 CRC64;
MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ
GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT
KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD
THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE
HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK
NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL
