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P24270 (CATA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Cas-1, Cas1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 mutant phenotype PubMed 15178682. Source: MGI

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from mutant phenotype PubMed 5087482. Source: MGI

hemoglobin metabolic process

Inferred from mutant phenotype PubMed 8153151. Source: MGI

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 10617683PubMed 17275685PubMed 9600348. Source: MGI

kidney development

Inferred from electronic annotation. Source: Ensembl

menopause

Inferred from electronic annotation. Source: Ensembl

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 9600348. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 15020231. Source: MGI

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 15020231. Source: MGI

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from direct assay PubMed 17275685. Source: MGI

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from mutant phenotype PubMed 5087482. Source: MGI

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from electronic annotation. Source: Ensembl

mitochondrial intermembrane space

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

peroxisomal membrane

Inferred from direct assay PubMed 12915479. Source: MGI

peroxisome

Inferred from direct assay PubMed 17881773. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: Ensembl

aminoacylase activity

Inferred from mutant phenotype PubMed 15178682. Source: MGI

catalase activity

Inferred from direct assay PubMed 10617683PubMed 12521604PubMed 12646716PubMed 15317809PubMed 17275685PubMed 9600348. Source: MGI

heme binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on peroxide as acceptor

Inferred from direct assay PubMed 11792727. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
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.8 Ref.12
Modified residue131N6-succinyllysine Ref.12
Modified residue2211N6-succinyllysine Ref.12
Modified residue2331N6-acetyllysine Ref.13
Modified residue3061N6-acetyllysine; alternate Ref.13
Modified residue3061N6-succinyllysine; alternate Ref.12
Modified residue4171Phosphoserine Ref.11
Modified residue4301N6-acetyllysine; alternate Ref.13
Modified residue4301N6-succinyllysine; alternate Ref.12
Modified residue4341Phosphoserine Ref.11
Modified residue4491N6-acetyllysine; alternate Ref.12 Ref.13
Modified residue4491N6-succinyllysine; alternate Ref.12
Modified residue4801N6-acetyllysine; alternate Ref.13
Modified residue4801N6-succinyllysine; alternate Ref.12
Modified residue4991N6-acetyllysine Ref.13
Modified residue5221N6-succinyllysine Ref.12

Experimental info

Mutagenesis111Q → H: Acatalasemia.
Sequence conflict971A → G in AAA66054. Ref.3
Sequence conflict1171T → A in AAA37373. Ref.1
Sequence conflict1171T → A in CAA36342. Ref.2
Sequence conflict1171T → A in AAA66054. Ref.3
Sequence conflict1171T → A in AAH13447. Ref.4
Sequence conflict3161L → V in AAA66054. Ref.3
Sequence conflict3501M → K in AAA66054. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P24270 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 4D86F3C9D1A3DF9E

FASTA52759,795
        10         20         30         40         50         60 
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE 

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

       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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion and Bone marrow.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Strain: FVB/N.
Tissue: Kidney.
[8]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, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6J.
Tissue: Skeletal muscle.
[9]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 48-66, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 503-527.
[11]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-449, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-221; LYS-306; LYS-430; LYS-449; LYS-480 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[13]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233; LYS-306; LYS-430; LYS-449; LYS-480 AND LYS-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62897 mRNA. Translation: AAA37373.1.
X52108 mRNA. Translation: CAA36342.1.
L25069 mRNA. Translation: AAA66054.1.
AK150893 mRNA. Translation: BAE29939.1.
AK159152 mRNA. Translation: BAE34859.1.
AK159885 mRNA. Translation: BAE35454.1.
AK159891 mRNA. Translation: BAE35458.1.
AK169069 mRNA. Translation: BAE40856.1.
AL773505 Genomic DNA. Translation: CAM17512.1.
CH466519 Genomic DNA. Translation: EDL27697.1.
BC013447 mRNA. Translation: AAH13447.1.
M29394 mRNA. Translation: AAA37371.1.
PIRA36695.
RefSeqNP_033934.2. NM_009804.2.
UniGeneMm.4215.

3D structure databases

ProteinModelPortalP24270.
SMRP24270. Positions 4-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP24270. 3 interactions.
MINTMINT-1859622.

PTM databases

PhosphoSiteP24270.

2D gel databases

SWISS-2DPAGEP24270.

Proteomic databases

PaxDbP24270.
PRIDEP24270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
GeneID12359.
KEGGmmu:12359.
UCSCuc008liw.2. mouse.

Organism-specific databases

CTD847.
MGIMGI:88271. Cat.

Phylogenomic databases

eggNOGCOG0753.
GeneTreeENSGT00390000018100.
HOGENOMHOG000087852.
HOVERGENHBG003986.
InParanoidQ3TXQ6.
KOK03781.
OMALYTQINA.
OrthoDBEOG7V7660.
TreeFamTF300540.

Gene expression databases

ArrayExpressP24270.
BgeeP24270.
CleanExMM_CAT.
GenevestigatorP24270.

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

ChiTaRSCAT. mouse.
NextBio281024.
PROP24270.
SOURCESearch...

Entry information

Entry nameCATA_MOUSE
AccessionPrimary (citable) accession number: P24270
Secondary accession number(s): Q3TXQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 134 of the entry and version 4 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

MGD cross-references

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