NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle;
TISSUE=Liver;
Nakamura K.;
"cDNA sequence and deduced amino acid sequence of dog catalase.";
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ACATALASEMIA THR-327.
STRAIN=Beagle;
DOI=10.1016/S1357-2725(00)00057-1; PubMed=11137458 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura K., Watanabe M., Takanaka K., Sasaki Y., Ikeda T.;
"cDNA cloning of mutant catalase in acatalasemic beagle dog: single nucleotide substitution leading to thermal-instability and enhanced proteolysis of mutant enzyme.";
Int. J. Biochem. Cell Biol. 32:1183-1193(2000).

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 (By similarity).
COFACTOR: NADP (By similarity).
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Peroxisome (By similarity).
DISEASE: Defects in CAT are the cause of acatalasia; also known as acatalasemia. This disease is characterized by absence of catalase activity.
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

AB012918; BAA36420.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB038231; BAB20764.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001002984.1; -.

UniGene

Cfa.188

3D structure databases

HSSP

P00432; 4BLC. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

O97492; 5-501.

ModBase

O97492.

Protein family/group databases

PeroxiBase

5319; CfaKat01.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

PRINTS

PR00067; CATALASE.

ProDom

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

PROSITE

PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.
PS51402; CATALASE_3; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSCAFG00000006941; Canis familiaris. [Contig view]

GeneID

403474; -.

KEGG

cfa:403474; -.

Phylogenomic databases

HOVERGEN

O97492; -.

Other

UniRef

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

Keywords

Disease mutation; 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 (By similarity).`
`CHAIN`	`2 527`	`526`	`Catalase.`	`PRO_0000084899`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`148 148`		`By similarity.`
`METAL`	`358 358`		`Iron (heme axial ligand) (By similarity).`
`MOD_RES`	`231 231`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`308 308`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`422 422`		`Phosphoserine (By similarity).`
`MOD_RES`	`517 517`		`Phosphoserine (By similarity).`
`VARIANT`	`327 327`	`1`	`A -> T (in acatalasemia; heat-labile).`

Sequence information

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

Molecular weight: 59797 Da [This is the MW of the unprocessed precursor]

CRC64: CC0BC7F88FE2C2AC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADSRDPASD QMKLWKEQRA AQKPDVLTTG GGNPIGDKLN VMTAGPRGPL LVQDVVFTDE 

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

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

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

       250        260        270        280        290        300 
GIKNLSVEDA ARLSHEDPDY GLRDLFNAIA TGNYPSWTFY IQVMTFSQAE TFPFNPFDLT 

       310        320        330        340        350        360 
KIWPHQDYPL IPVGKLVLNR NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD 

       370        380        390        400        410        420 
THRHRLGPNY LQIPVNCPFR ARVANYQRDG PMCMLDNQGG APNYYPNSFS APEQQRCVLE 

       430        440        450        460        470        480 
HSSQCSPDVQ RFNSANEDNV TQVRTFYLKV LGEEERKRLC ENIAGHLKDA QLFIQKKAVK 

       490        500        510        520 
NFSDVHPDYG ARIQALLDKY NAEKPKNAIH TFMQHGSHLA AREKANL

O97492 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