Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O97492 (CATA_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase

EC=1.11.1.6
Gene names
Name:CAT
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

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 processHydrogen peroxide
   Cellular componentPeroxisome
   DiseaseDisease mutation
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMitogen
Oxidoreductase
Peroxidase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatalase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 527526Catalase
PRO_0000084899

Sites

Active site751 By similarity
Active site1481 By similarity
Metal binding3581Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue131N6-succinyllysine By similarity
Modified residue2211N6-succinyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue4341Phosphoserine By similarity
Modified residue4491N6-acetyllysine; alternate By similarity
Modified residue4491N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine; alternate By similarity
Modified residue4801N6-succinyllysine; alternate By similarity
Modified residue4991N6-acetyllysine By similarity

Natural variations

Natural variant3271A → T in acatalasemia; heat-labile. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O97492 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CC0BC7F88FE2C2AC

FASTA52759,797
        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 

« Hide

References

[1]"cDNA and deduced amino acid sequences of dog catalase."
Nakamura K., Watanabe M., Ikeda T.
DNA Seq. 9:347-352(1998) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ACATALASEMIA THR-327.
Strain: Beagle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012918 mRNA. Translation: BAA36420.1.
AB038231 mRNA. Translation: BAB20764.1.
RefSeqNP_001002984.1. NM_001002984.1.
UniGeneCfa.188.

3D structure databases

ProteinModelPortalO97492.
SMRO97492. Positions 4-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000010324.

Protein family/group databases

PeroxiBase5319. CfaKat01.

Proteomic databases

PaxDbO97492.
PRIDEO97492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000011146; ENSCAFP00000010324; ENSCAFG00000006941.
GeneID403474.
KEGGcfa:403474.

Organism-specific databases

CTD847.

Phylogenomic databases

eggNOGCOG0753.
GeneTreeENSGT00390000018100.
HOGENOMHOG000087852.
HOVERGENHBG003986.
InParanoidO97492.
KOK03781.
OMANASQFIQ.
OrthoDBEOG7V7660.
TreeFamTF300540.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. 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]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816990.

Entry information

Entry nameCATA_CANFA
AccessionPrimary (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: May 14, 2014
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families