O97492 (CATA_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase
EC=1.11.1.6

Gene names

Name:

CAT

Organism

Canis familiaris (Dog) (Canis lupus familiaris)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 H2O2 = O2 + 2 H2O.
Cofactor	Heme group By similarity. NADP By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Peroxisome By similarity.
Involvement in disease	Note=Defects in CAT are the cause of acatalasia; also known as acatalasemia. This disease is characterized by absence of catalase activity.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Disease	Disease mutation
Ligand	Heme Iron Metal-binding NADP
Molecular function	Mitogen Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	catalase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 527	526	Catalase		PRO_0000084899
Sites
	Active site	75	1	By similarity
	Active site	148	1	By similarity
	Metal binding	358	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Modified residue	231	1	Phosphotyrosine By similarity
	Modified residue	308	1	Phosphotyrosine By similarity
	Modified residue	422	1	Phosphoserine By similarity
	Modified residue	517	1	Phosphoserine By similarity
Natural variations
	Natural variant	327	1	A → T in acatalasemia; heat-labile. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O97492 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CC0BC7F88FE2C2AC	FASTA	527	59,797
	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

References

[1]	"cDNA and deduced amino acid sequences of dog catalase." Nakamura K., Watanabe M., Ikeda T. DNA Seq. 9:347-352(1998) [PubMed: 10524763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Beagle. Tissue: Liver.
[2]	"cDNA cloning of mutant catalase in acatalasemic beagle dog: single nucleotide substitution leading to thermal-instability and enhanced proteolysis of mutant enzyme." Nakamura K., Watanabe M., Takanaka K., Sasaki Y., Ikeda T. Int. J. Biochem. Cell Biol. 32:1183-1193(2000) [PubMed: 11137458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ACATALASEMIA THR-327. Strain: Beagle.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB012918 mRNA. Translation: BAA36420.1. AB038231 mRNA. Translation: BAB20764.1.
RefSeq	NP_001002984.1. NM_001002984.1.
UniGene	Cfa.188.
3D structure databases
ProteinModelPortal	O97492.
SMR	O97492. Positions 4-501.
ModBase	Search...
Protein-protein interaction databases
STRING	O97492.
Protein family/group databases
PeroxiBase	5319. CfaKat01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	403474.
KEGG	cfa:403474.
Organism-specific databases
CTD	847.
Phylogenomic databases
eggNOG	maNOG07901.
GeneTree	ENSGT00390000018100.
HOVERGEN	HBG003986.
InParanoid	O97492.
OrthoDB	EOG45TCMV.
PhylomeDB	O97492.
Family and domain databases
InterPro	IPR018028. Catalase. IPR020835. Catalase-like_dom. IPR024708. Catalase_AS. IPR024711. Catalase_clade1/3. IPR011614. Catalase_core. IPR002226. Catalase_haem_BS. IPR010582. Catalase_immune_responsive. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
KO	K03781.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PIRSF	PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTS	PR00067. CATALASE.
SMART	SM01060. Catalase. 1 hit. [Graphical view]
SUPFAM	SSF56634. Catalase_N. 1 hit.
PROSITE	PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA_CANFA

Accession

Primary (citable) accession number: O97492
Secondary accession number(s): Q9GKY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program