CATA_MOUSE
ID CATA_MOUSE Reviewed; 527 AA.
AC P24270; Q3TXQ6;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=Cat; Synonyms=Cas-1, Cas1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/CS(A); TISSUE=Kidney, and Liver;
RX PubMed=2268310; DOI=10.1016/s0006-291x(05)80891-5;
RA Shaffer J.B., Preston K.E.;
RT "Molecular analysis of an acatalasemic mouse mutant.";
RL Biochem. Biophys. Res. Commun. 173:1043-1050(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/CS(A), and C3H/HeJ; TISSUE=Liver;
RX PubMed=2395665; DOI=10.1093/nar/18.16.4941;
RA Shaffer J.B., Preston K.E., Shepard B.A.;
RT "Nucleotide and deduced amino acid sequences of mouse catalase: molecular
RT analysis of a low activity mutant.";
RL Nucleic Acids Res. 18:4941-4941(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8088826; DOI=10.1006/geno.1994.1273;
RA Reimer D.L., Bailley J., Singh S.M.;
RT "Complete cDNA and 5' genomic sequences and multilevel regulation of the
RT mouse catalase gene.";
RL Genomics 21:325-336(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [8]
RP PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA Kanor S., Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 48-66, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 503-527.
RX PubMed=3654595; DOI=10.1016/s0021-9258(18)45143-5;
RA Shaffer J.B., Sutton R.B., Bewley G.C.;
RT "Isolation of a cDNA clone for murine catalase and analysis of an
RT acatalasemic mutant.";
RL J. Biol. Chem. 262:12908-12911(1987).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-422 AND SER-517, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-434 AND SER-517, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-449, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-13; LYS-221; LYS-306; LYS-430; LYS-449;
RP LYS-480 AND LYS-522, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233; LYS-306; LYS-430; LYS-449;
RP LYS-480 AND LYS-499, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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}.
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DR EMBL; M62897; AAA37373.1; -; mRNA.
DR EMBL; X52108; CAA36342.1; -; mRNA.
DR EMBL; L25069; AAA66054.1; -; mRNA.
DR EMBL; AK150893; BAE29939.1; -; mRNA.
DR EMBL; AK159152; BAE34859.1; -; mRNA.
DR EMBL; AK159885; BAE35454.1; -; mRNA.
DR EMBL; AK159891; BAE35458.1; -; mRNA.
DR EMBL; AK169069; BAE40856.1; -; mRNA.
DR EMBL; AL773505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27697.1; -; Genomic_DNA.
DR EMBL; BC013447; AAH13447.1; -; mRNA.
DR EMBL; M29394; AAA37371.1; -; mRNA.
DR CCDS; CCDS16478.1; -.
DR PIR; A36695; A36695.
DR RefSeq; NP_033934.2; NM_009804.2.
DR AlphaFoldDB; P24270; -.
DR SMR; P24270; -.
DR BioGRID; 198490; 28.
DR ComplexPortal; CPX-4767; Catalase complex.
DR IntAct; P24270; 9.
DR MINT; P24270; -.
DR STRING; 10090.ENSMUSP00000028610; -.
DR iPTMnet; P24270; -.
DR PhosphoSitePlus; P24270; -.
DR SwissPalm; P24270; -.
DR SWISS-2DPAGE; P24270; -.
DR CPTAC; non-CPTAC-3639; -.
DR EPD; P24270; -.
DR jPOST; P24270; -.
DR MaxQB; P24270; -.
DR PaxDb; P24270; -.
DR PeptideAtlas; P24270; -.
DR PRIDE; P24270; -.
DR ProteomicsDB; 265446; -.
DR Antibodypedia; 3595; 968 antibodies from 47 providers.
DR DNASU; 12359; -.
DR Ensembl; ENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
DR GeneID; 12359; -.
DR KEGG; mmu:12359; -.
DR UCSC; uc008liw.2; mouse.
DR CTD; 847; -.
DR MGI; MGI:88271; Cat.
DR VEuPathDB; HostDB:ENSMUSG00000027187; -.
DR eggNOG; KOG0047; Eukaryota.
DR GeneTree; ENSGT00390000018100; -.
DR HOGENOM; CLU_010645_4_1_1; -.
DR InParanoid; P24270; -.
DR OMA; WTCYVQV; -.
DR OrthoDB; 507937at2759; -.
DR PhylomeDB; P24270; -.
DR TreeFam; TF300540; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 12359; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cat; mouse.
DR PRO; PR:P24270; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P24270; protein.
DR Bgee; ENSMUSG00000027187; Expressed in left lobe of liver and 259 other tissues.
DR ExpressionAtlas; P24270; baseline and differential.
DR Genevisible; P24270; MM.
DR GO; GO:0062151; C:catalase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004046; F:aminoacylase activity; IMP:MGI.
DR GO; GO:0016209; F:antioxidant activity; ISO:MGI.
DR GO; GO:0004096; F:catalase activity; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:MGI.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0009060; P:aerobic respiration; IMP:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
DR GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI.
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; ISO:MGI.
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:0006979; P:response to oxidative stress; IDA:MGI.
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; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0001657; P:ureteric bud development; ISO:MGI.
DR GO; GO:0009650; P:UV protection; ISO:MGI.
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:0000269|Ref.8, ECO:0007744|PubMed:23806337"
FT CHAIN 2..527
FT /note="Catalase"
FT /id="PRO_0000084902"
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-acetylserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:23806337"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 221
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 306
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 306
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 430
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 430
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 449
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 449
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 480
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
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:17208939,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 11
FT /note="Q->H: Acatalasemia."
FT CONFLICT 97
FT /note="A -> G (in Ref. 3; AAA66054)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="T -> A (in Ref. 1; AAA37373, 2; CAA36342, 3;
FT AAA66054 and 4; AAH13447)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="L -> V (in Ref. 3; AAA66054)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="M -> K (in Ref. 3; AAA66054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59795 MW; 4D86F3C9D1A3DF9E CRC64;
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVTGES
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ
GIKNLPVGEA GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT
KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD
THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG APNYYPNSFS APEQQRSALE
HSVQCAVDVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIAGHLKDA QLFIQKKAVK
NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL
