[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C3H/CS(A); TISSUE=Kidney, and Liver; DOI=10.1016/S0006-291X(05)80891-5; PubMed=2268310 [NCBI, ExPASy, EBI, Israel, Japan] Shaffer J.B., Preston K.E.; "Molecular analysis of an acatalasemic mouse mutant."; Biochem. Biophys. Res. Commun. 173:1043-1050(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C3H/CS(A), and C3H/HeJ; TISSUE=Liver; DOI=10.1093/nar/18.16.4941; PubMed=2395665 [NCBI, ExPASy, EBI, Israel, Japan] Shaffer J.B., Preston K.E., Shepard B.A.; "Nucleotide and deduced amino acid sequences of mouse catalase: molecular analysis of a low activity mutant."; Nucleic Acids Res. 18:4941-4941(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; TISSUE=Liver; DOI=10.1006/geno.1994.1273; PubMed=8088826 [NCBI, ExPASy, EBI, Israel, Japan] Reimer D.L., Bailley J., Singh S.M.; "Complete cDNA and 5' genomic sequences and multilevel regulation of the mouse catalase gene."; Genomics 21:325-336(1994).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY. STRAIN=C57BL/6J; TISSUE=Skeletal muscle; Kanor S., Quadroni M., Bienvenut W.V.; Submitted (MAR-2006) to UniProtKB.
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 503-527. PubMed=3654595 [NCBI, ExPASy, EBI, Israel, Japan] Shaffer J.B., Sutton R.B., Bewley G.C.; "Isolation of a cDNA clone for murine catalase and analysis of an acatalasemic mutant."; J. Biol. Chem. 262:12908-12911(1987).
[7]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-422 AND SER-517, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1074/mcp.M600218-MCP200; PubMed=17208939 [NCBI, ExPASy, EBI, Israel, Japan] Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."; Mol. Cell. Proteomics 6:669-676(2007).

Comments

FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
CATALYTIC ACTIVITY: 2 H₂O₂ = O₂ + 2 H₂O.
COFACTOR: Heme group.
COFACTOR: NADP.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the catalase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M62897; AAA37373.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52108; CAA36342.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L25069; AAA66054.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013447; AAH13447.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29394; AAA37371.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36695; A36695.

UniGene

Mm.4215

3D structure databases

HSSP

P00432; 4BLC. [HSSP ENTRY / PDB]

P24270; 5-501.

PTM databases

P24270; -.

2D gel databases

SWISS-2DPAGE

P24270; -.

Organism-specific databases

MGI

MGI:88271; Cat.

Gene expression databases

ArrayExpress

P24270; -.

CleanEx

MM_CAT; -.

GermOnline

ENSMUSG00000027187; Mus musculus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0005778;	Cellular component: peroxisomal membrane (inferred from direct assay from MGI).
GO:0004046;	Molecular function: aminoacylase activity (inferred from mutant phenotype from MGI).
GO:0004096;	Molecular function: catalase activity (inferred from direct assay from MGI).
GO:0009060;	Biological process: aerobic respiration (inferred from mutant phenotype from MGI).
GO:0008203;	Biological process: cholesterol metabolic process (inferred from mutant phenotype from MGI).
GO:0020027;	Biological process: hemoglobin metabolic process (inferred from mutant phenotype from MGI).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from direct assay from MGI).
GO:0032088;	Biological process: negative regulation of NF-kappaB transcription factor activity (inferred from direct assay from MGI).
GO:0051092;	Biological process: positive regulation of NF-kappaB transcription factor activity (inferred from direct assay from MGI).
GO:0014068;	Biological process: positive regulation of phosphoinositide 3-kinase cascade (inferred from direct assay from MGI).
GO:0006641;	Biological process: triacylglycerol metabolic process (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.180.10; Catalase_N; 1.

PANTHER

PTHR11465; Catalase; 1.

Pfam

PF00199; Catalase; 1.
Pfam graphical view of domain structure.

ProDom

PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.

BLOCKS

P24270.

Genome annotation databases

Ensembl

ENSMUSG00000027187; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P24270; -.

HOVERGEN

P24270; -.

Other

Cat; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; NADP; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 527`	`526`	`Catalase.`	`PRO_0000084902`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`148 148`		`By similarity.`
`METAL`	`358 358`		`Iron (heme axial ligand) (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine.`
`MOD_RES`	`21 21`		`Phosphoserine.`
`MOD_RES`	`231 231`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`308 308`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`422 422`		`Phosphoserine.`
`MOD_RES`	`517 517`		`Phosphoserine.`
`MUTAGEN`	`11 11`		`Q->H: Acatalasemia.`
`CONFLICT`	`97 97`		`A -> G (in Ref. 3; AAA66054).`
`CONFLICT`	`316 316`		`L -> V (in Ref. 3; AAA66054).`
`CONFLICT`	`350 350`		`M -> K (in Ref. 3; AAA66054).`

Sequence information

Length: 527 AA [This is the length of the unprocessed precursor]

Molecular weight: 59765 Da [This is the MW of the unprocessed precursor]

CRC64: 2D5C4195F63FF4BF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE 

        70         80         90        100        110        120 
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVAGES 

       130        140        150        160        170        180 
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD 

       190        200        210        220        230        240 
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ 

       250        260        270        280        290        300 
GIKNLPVGEA GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT 

       310        320        330        340        350        360 
KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD 

       370        380        390        400        410        420 
THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG APNYYPNSFS APEQQRSALE 

       430        440        450        460        470        480 
HSVQCAVDVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIAGHLKDA QLFIQKKAVK 

       490        500        510        520 
NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL

P24270 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools