P24270 (CATA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase
EC=1.11.1.6

Gene names

Name:	Cat
Synonyms:	Cas-1, Cas1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding NADP
Molecular function	Mitogen Oxidoreductase Peroxidase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	UV protection Inferred from electronic annotation. Source: Compara aerobic respiration Inferred from mutant phenotype PubMed 15178682. Source: MGI cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara 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 menopause Inferred from electronic annotation. Source: Compara 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: Compara 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 cascade Inferred from direct assay PubMed 15020231. Source: MGI protein homotetramerization Inferred from electronic annotation. Source: Compara response to hyperoxia Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to vitamin E Inferred from electronic annotation. Source: Compara triglyceride metabolic process Inferred from mutant phenotype PubMed 5087482. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: Compara mitochondrial intermembrane space Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI peroxisomal membrane Inferred from direct assay PubMed 12915479. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	NADP binding Inferred from electronic annotation. Source: Compara 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: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 527	526	Catalase		PRO_0000084902
Sites
	Active site	75	1	By similarity
	Active site	148	1	By similarity
	Metal binding	358	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.8
	Modified residue	21	1	Phosphoserine Ref.11
	Modified residue	422	1	Phosphoserine Ref.11
	Modified residue	517	1	Phosphoserine Ref.11
Experimental info
	Mutagenesis	11	1	Q → H: Acatalasemia.
	Sequence conflict	97	1	A → G in AAA66054. Ref.3
	Sequence conflict	117	1	T → A in AAA37373. Ref.1
	Sequence conflict	117	1	T → A in CAA36342. Ref.2
	Sequence conflict	117	1	T → A in AAA66054. Ref.3
	Sequence conflict	117	1	T → A in AAH13447. Ref.4
	Sequence conflict	316	1	L → V in AAA66054. Ref.3
	Sequence conflict	350	1	M → K in AAA66054. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P24270 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 4D86F3C9D1A3DF9E	FASTA	527	59,795
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-422 AND SER-517, MASS SPECTROMETRY. 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.
IPI	IPI00312058.
PIR	A36695.
RefSeq	NP_033934.2. NM_009804.2.
UniGene	Mm.4215.
3D structure databases
ProteinModelPortal	P24270.
SMR	P24270. Positions 4-501.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24270. 1 interaction.
PTM databases
PhosphoSite	P24270.
2D gel databases
SWISS-2DPAGE	P24270.
Proteomic databases
PaxDb	P24270.
PRIDE	P24270.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
GeneID	12359.
KEGG	mmu:12359.
Organism-specific databases
CTD	847.
MGI	MGI:88271. Cat.
Phylogenomic databases
eggNOG	COG0753.
GeneTree	ENSGT00390000018100.
HOGENOM	HOG000087852.
HOVERGEN	HBG003986.
InParanoid	Q3TXQ6.
KO	K03781.
OMA	HDITRYS.
OrthoDB	EOG45TCMV.
Gene expression databases
ArrayExpress	P24270.
Bgee	P24270.
CleanEx	MM_CAT.
Genevestigator	P24270.
GermOnline	ENSMUSG00000027187. Mus musculus.
Family and domain databases
Gene3D	2.40.180.10. 1 hit.
InterPro	IPR018028. 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]
PANTHER	PTHR11465. PTHR11465. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PIRSF	PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTS	PR00067. CATALASE.
SMART	SM01060. Catalase. 1 hit. [Graphical view]
SUPFAM	SSF56634. Catalase_N. 1 hit.
PROSITE	PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CAT. mouse.
NextBio	281024.
SOURCE	Search...

Entry information

Entry name

CATA_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program