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P04762 (CATA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. 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
Synonyms:Cas1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

NADP.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMitogen
Oxidoreductase
Peroxidase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processUV protection

Inferred from electronic annotation. Source: Ensembl

aerobic respiration

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from expression pattern PubMed 21276205. Source: RGD

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

hemoglobin metabolic process

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 17576767. Source: RGD

kidney development

Inferred from mutant phenotype PubMed 22733796. Source: RGD

menopause

Inferred from expression pattern PubMed 21226757. Source: RGD

negative regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 10569634. Source: RGD

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

response to hyperoxia

Inferred from expression pattern PubMed 19895324. Source: RGD

response to hypoxia

Inferred from mutant phenotype PubMed 18270324. Source: RGD

response to vitamin E

Inferred from expression pattern PubMed 19641679. Source: RGD

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

ureteric bud development

Inferred from mutant phenotype PubMed 22733796. Source: RGD

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 17576767. Source: RGD

cytosol

Inferred from direct assay PubMed 17576767. Source: RGD

endoplasmic reticulum

Inferred from direct assay PubMed 17576767. Source: RGD

lysosome

Inferred from direct assay PubMed 17576767. Source: RGD

mitochondrial intermembrane space

Inferred from direct assay PubMed 17576767. Source: RGD

peroxisomal membrane

Inferred from electronic annotation. Source: Ensembl

peroxisome

Inferred from direct assay PubMed 14561759. Source: HGNC

plasma membrane

Inferred from direct assay PubMed 17576767. Source: RGD

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: Ensembl

aminoacylase activity

Inferred from electronic annotation. Source: Ensembl

catalase activity

Inferred from direct assay PubMed 15773229PubMed 15777843PubMed 15869839PubMed 17576767Ref.1. Source: RGD

heme binding

Inferred from electronic annotation. Source: Ensembl

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_0000084905

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 residue3061N6-acetyllysine; alternate By similarity
Modified residue3061N6-succinyllysine; alternate By similarity
Modified residue4171Phosphoserine 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 residue5221N6-succinyllysine By similarity

Experimental info

Sequence conflict4341S → N in AAA40885. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P04762 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CA28530A0FC6EFA6

FASTA52759,757
        10         20         30         40         50         60 
MADSRDPASD QMKQWKEQRA PQKPDVLTTG GGNPIGDKLN IMTAGPRGPL LVQDVVFTDE 

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

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

       190        200        210        220        230        240 
MVWDFWSLCP ESLHQVTFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ 

       250        260        270        280        290        300 
GIKNLPVEEA GRLAQEDPDY GLRDLFNAIA SGNYPSWTFY IQVMTFKEAE TFPFNPFDLT 

       310        320        330        340        350        360 
KVWPHKDYPL IPVGKLVLNR NPANYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD 

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

       430        440        450        460        470        480 
HHSQCSADVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIANHLKDA QLFIQRKAVK 

       490        500        510        520 
NFTDVHPDYG ARVQALLDQY NSQKPKNAIH TYVQAGSHIA AKGKANL 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase."
Furuta S., Hayashi H., Hijikata M., Miyazawa S., Osumi T., Hashimoto T.
Proc. Natl. Acad. Sci. U.S.A. 83:313-317(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Isolation and characterization of the rat catalase-encoding gene."
Nakashima H., Yamamoto M., Goto K., Osumi T., Hashimoto T., Endo H.
Gene 79:279-288(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Molecular cloning of cDNA for rat liver catalase."
Osumi T., Ozasa H., Miyazawa S., Hashimoto T.
Biochem. Biophys. Res. Commun. 122:831-837(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 399-527.
[5]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 481-492, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11670 mRNA. Translation: AAA40884.1.
M25680 expand/collapse EMBL AC list , M25669, M25670, M25671, M25672, M25673, M25674, M25675, M25676, M25677, M25678, M25679 Genomic DNA. Translation: AAB42378.1.
BC081853 mRNA. Translation: AAH81853.1.
K01929 mRNA. Translation: AAA40885.1.
PIRCSRT. JU0065.
RefSeqNP_036652.1. NM_012520.2.
UniGeneRn.3001.

3D structure databases

ProteinModelPortalP04762.
SMRP04762. Positions 4-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246433. 2 interactions.
IntActP04762. 2 interactions.
STRING10116.ENSRNOP00000011230.

Chemistry

ChEMBLCHEMBL1075216.

Protein family/group databases

PeroxiBase11811. RnoKat.

PTM databases

PhosphoSiteP04762.

Proteomic databases

PaxDbP04762.
PRIDEP04762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000011230; ENSRNOP00000011230; ENSRNOG00000008364.
GeneID24248.
KEGGrno:24248.
UCSCRGD:2279. rat.

Organism-specific databases

CTD847.
RGD2279. Cat.

Phylogenomic databases

eggNOGCOG0753.
GeneTreeENSGT00390000018100.
HOGENOMHOG000087852.
HOVERGENHBG003986.
InParanoidP04762.
KOK03781.
OMALYTQINA.
OrthoDBEOG7V7660.
TreeFamTF300540.

Gene expression databases

GenevestigatorP04762.

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

NextBio602753.
PROP04762.

Entry information

Entry nameCATA_RAT
AccessionPrimary (citable) accession number: P04762
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 125 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