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CAT catalase [ Bos taurus (domestic cattle) ]

Gene ID: 531682, updated on 5-Sep-2025
Official Symbol
CATprovided by VGNC
Official Full Name
catalaseprovided by VGNC
Primary source
VGNC:VGNC:26792
See related
EnsemblRapid:ENSBTAG00070025560
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Orthologs
human mouse all
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See CAT in Genome Data Viewer
Location:
chromosome: 15
Exon count:
13
Annotation release Status Assembly Chr Location
RS_2024_12 current ARS-UCD2.0 (GCF_002263795.3) 15 NC_037342.1 (64975290..65011234)

Chromosome 15 - NC_037342.1Genomic Context describing neighboring genes Neighboring gene ankyrin repeat and BTB domain containing 2 Neighboring gene uncharacterized LOC132342356 Neighboring gene uncharacterized LOC104974297 Neighboring gene E74 like ETS transcription factor 5 Neighboring gene uncharacterized LOC132342357 Neighboring gene ETS homologous factor

Genomic Sequence:
NC_037342.1 Chromosome 15 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

  • Project title: Dominette sequence data
  • BioProject: PRJNA294306
  • Analysis date: Tue Dec 17 08:57:05 2024

Related articles in PubMed

  1. Sixty years from discovery to solution: crystal structure of bovine liver catalase form III. Foroughi LM, et al. Acta Crystallogr D Biol Crystallogr, 2011 Sep. PMID 21904028
  2. Comparison of beef liver and Penicillium vitale catalases. Melik-Adamyan WR, et al. J Mol Biol, 1986 Mar 5. PMID 3712444
  3. Structure and heme environment of beef liver catalase at 2.5 A resolution. Reid TJ 3rd, et al. Proc Natl Acad Sci U S A, 1981 Aug. PMID 6946424, Free PMC Article
  4. The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase. Schroeder WA, et al. Arch Biochem Biophys, 1982 Mar. PMID 7082009
  5. Structure of beef liver catalase. Murthy MR, et al. J Mol Biol, 1981 Oct 25. PMID 7328661

See all (33) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Interaction of artemisinin protects the activity of antioxidant enzyme catalase: A biophysical study.
    Title: Interaction of artemisinin protects the activity of antioxidant enzyme catalase: A biophysical study.
  2. The interactions between cationic surfactants dodecyltrimethylammonium bromide (DTAB) and tetradecyltrimethylammonium bromide (TTAB) with varying alkyl chain lengths and bovine liver catalase (BLC) were examined by various biophysical approaches.
    Title: Cationic surfactant mediated fibrillogenesis in bovine liver catalase: a biophysical approach.
  3. Enzyme activity assay and molecular docking revealed that the activity of CAT was slightly inhibited in the presence of Sudan dyes. In comparison, the binding of Sudan II with CAT was slightly stronger than Sudan IV. Also, Sudan II and Sudan IV showed a different impact on the microenvironment of aromatic amino acid residues.
    Title: Comparison of the toxicity of the dyes Sudan II and Sudan IV to catalase.
  4. the decrease in accessible surface area and increase in pKa of important lysine residues were considered as predominant factors in decreased glycation of bovine liver catalase by curcumin.
    Title: Destructive effect of non-enzymatic glycation on catalase and remediation via curcumin.
  5. ITC confirms the stability of bovine liver catalase (BLC)upon gemini combination. Docking provides support to fluorescence results by presenting the localization site of m-E2-m surfactants near to aromatic residues (mainly Tyr, Trp and Phe)
    Title: Biophysical perspective of the binding of ester-functionalized gemini surfactants with catalase.
  6. Data show that liver catalase is able to tolerate very high levels of the modifying alpha-oxoaldehyde methylglyoxal so that its essential enzymatic function is not impaired.
    Title: Arg354 in the catalytic centre of bovine liver catalase is protected from methylglyoxal-mediated glycation.
  7. The structure of bovine liver catalase determined from a single crystal at 3.2 A resolution by MicroED, is reported.
    Title: Structure of catalase determined by MicroED.
  8. These maps demonstrate that it is indeed possible to build atomic models from such crystals and even to determine the charged states of amino acid residues in the Ca(2+)-binding sites of Ca(2+)-ATPase and that of the iron atom in the heme in catalase.
    Title: Electron crystallography of ultrathin 3D protein crystals: atomic model with charges.
  9. Data indicate compatible osmolytes, proline, xylitol, and valine destabilize the denatured form of the catalase enzyme and, therefore, increase its disaggregation and thermal stability.
    Title: Effect of compatible and noncompatible osmolytes on the enzymatic activity and thermal stability of bovine liver catalase.
  10. Flavonoid inhibition of catalase activity is, at least partially, due to the formation of hydrogen bonds between catalase and the flavonoid.
    Title: Catalase is inhibited by flavonoids.
Submit: New GeneRIF Correction See all GeneRIFs (19)
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Clone Names

  • MGC128112

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables catalase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables heme binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in hydrogen peroxide catabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in response to hydrogen peroxide IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in peroxisome IEA
Inferred from Electronic Annotation
more info
 PubMed 
Preferred Names
catalase
NP_001030463.1

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001035386.2 → NP_001030463.1  catalase

    See identical proteins and their annotated locations for NP_001030463.1

    Status: PROVISIONAL

    Source sequence(s)
    BC103066
    UniProtKB/Swiss-Prot
    P00432, Q3SZ80
    UniProtKB/TrEMBL
    A0A3Q1LKF1
    Related
    ENSBTAP00070034475.1, ENSBTAT00070057959.1
    Conserved Domains (1) summary
    cd08156
    Location:68 → 497
    catalase_clade_3; Clade 3 of the heme-binding enzyme catalase

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2024_12

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037342.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    64975290..65011234
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00432.3 GenPept UniProtKB/Swiss-Prot:P00432

Gene LinkOut

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