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Reviewed, UniProtKB/Swiss-Prot P24270 (CATA_MOUSE)

Last modified October 13, 2009. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Catalase
    EC=1.11.1.6
Gene names
Name: Cat
Synonyms: Cas-1, Cas1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

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

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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.

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Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMitogen
Oxidoreductase
Peroxidase
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processaerobic respiration

Inferred from mutant phenotype. Source: MGI

cholesterol metabolic process

Inferred from mutant phenotype. Source: MGI

hemoglobin metabolic process

Inferred from mutant phenotype. Source: MGI

hydrogen peroxide catabolic process

Inferred from direct assay. Source: MGI

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay. Source: MGI

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay. Source: MGI

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of phosphoinositide 3-kinase cascade

Inferred from direct assay. Source: MGI

triglyceride metabolic process

Inferred from mutant phenotype. Source: MGI

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

peroxisomal membrane

Inferred from direct assay. Source: MGI

   Molecular functionaminoacylase activity

Inferred from mutant phenotype. Source: MGI

catalase activity

Inferred from direct assay. Source: MGI

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 527526Catalase
PRO_0000084902

Sites

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

Amino acid modifications

Modified residue21N-acetylserine Ref.5
Modified residue211Phosphoserine Ref.8
Modified residue2311Phosphotyrosine By similarity
Modified residue3081Phosphotyrosine By similarity
Modified residue4221Phosphoserine Ref.8
Modified residue5171Phosphoserine Ref.8

Experimental info

Mutagenesis111Q → H: Acatalasemia.
Sequence conflict971A → G in AAA66054. Ref.3
Sequence conflict3161L → V in AAA66054. Ref.3
Sequence conflict3501M → K in AAA66054. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P24270-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2D5C4195F63FF4BF

FASTA52759,765
        10         20         30         40         50         60 
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE 

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

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

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

       250        260        270        280        290        300 
GIKNLPVGEA GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT 

       310        320        330        340        350        360 
KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD 

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

       430        440        450        460        470        480 
HSVQCAVDVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIAGHLKDA QLFIQKKAVK 

       490        500        510        520 
NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL

« Hide

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References

« Hide 'large scale' references
[1]"Molecular analysis of an acatalasemic mouse mutant."
Shaffer J.B., Preston K.E.
Biochem. Biophys. Res. Commun. 173:1043-1050(1990) [PubMed: 2268310] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/CS(A).
Tissue: Kidney and Liver.
[2]"Nucleotide and deduced amino acid sequences of mouse catalase: molecular analysis of a low activity mutant."
Shaffer J.B., Preston K.E., Shepard B.A.
Nucleic Acids Res. 18:4941-4941(1990) [PubMed: 2395665] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/CS(A) and C3H/HeJ.
Tissue: Liver.
[3]"Complete cDNA and 5' genomic sequences and multilevel regulation of the mouse catalase gene."
Reimer D.L., Bailley J., Singh S.M.
Genomics 21:325-336(1994) [PubMed: 8088826] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[5]Kanor S., Quadroni M., Bienvenut W.V.
Submitted (MAR-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
Strain: C57BL/6J.
Tissue: Skeletal muscle.
[6]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 48-66, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[7]"Isolation of a cDNA clone for murine catalase and analysis of an acatalasemic mutant."
Shaffer J.B., Sutton R.B., Bewley G.C.
J. Biol. Chem. 262:12908-12911(1987) [PubMed: 3654595] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 503-527.
[8]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-422 AND SER-517, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M62897 mRNA. Translation: AAA37373.1.
X52108 mRNA. Translation: CAA36342.1.
L25069 mRNA. Translation: AAA66054.1.
BC013447 mRNA. Translation: AAH13447.1.
M29394 mRNA. Translation: AAA37371.1.
IPIIPI00312058.
PIRA36695.
UniGeneMm.4215

3D structure databases

HSSPHSSP built from PDB template 4BLC based on UniProtKB P00432.
SMRP24270. Positions 5-501.
ModBaseSearch...

Protein-protein interaction databases

STRINGP24270.

PTM databases

PhosphoSiteP24270.

2-D gel databases

SWISS-2DPAGEP24270.

Proteomic databases

PRIDEP24270.

Genome annotation databases

EnsemblENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187; Mus musculus. [Genome view]
UCSCF41G4.2b.1. c. elegans.

Organism-specific databases

MGIMGI:88271. Cat.

Phylogenomic databases

HOGENOMP24270.
HOVERGENP24270.

Enzyme and pathway databases

BRENDA1.11.1.6. 244.

Gene expression databases

ArrayExpressP24270.
BgeeP24270.
CleanExMM_CAT.
GenevestigatorP24270.
GermOnlineENSMUSG00000027187. Mus musculus.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
ProDomPD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameCATA_MOUSE
AccessionPrimary (citable) accession number: P24270
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents