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P24270

- CATA_MOUSE

UniProt

P24270 - CATA_MOUSE

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Protein

Catalase

Gene

Cat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751PROSITE-ProRule annotation
Active sitei148 – 1481PROSITE-ProRule annotation
Metal bindingi358 – 3581Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. aminoacylase activity Source: MGI
  2. catalase activity Source: MGI
  3. heme binding Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. NADP binding Source: Ensembl
  6. oxidoreductase activity, acting on peroxide as acceptor Source: MGI

GO - Biological processi

  1. aerobic respiration Source: MGI
  2. cellular response to growth factor stimulus Source: Ensembl
  3. cholesterol metabolic process Source: MGI
  4. hemoglobin metabolic process Source: MGI
  5. hydrogen peroxide catabolic process Source: MGI
  6. menopause Source: Ensembl
  7. negative regulation of apoptotic process Source: Ensembl
  8. negative regulation of NF-kappaB transcription factor activity Source: MGI
  9. osteoblast differentiation Source: Ensembl
  10. positive regulation of cell division Source: UniProtKB-KW
  11. positive regulation of NF-kappaB transcription factor activity Source: MGI
  12. positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  13. protein homotetramerization Source: Ensembl
  14. response to hyperoxia Source: Ensembl
  15. response to hypoxia Source: Ensembl
  16. response to oxidative stress Source: MGI
  17. response to vitamin E Source: Ensembl
  18. triglyceride metabolic process Source: MGI
  19. ureteric bud development Source: Ensembl
  20. UV protection Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Mitogen, Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
REACT_253802. Purine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:Cat
Synonyms:Cas-1, Cas1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:88271. Cat.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. Golgi apparatus Source: Ensembl
  5. lysosome Source: Ensembl
  6. mitochondrial intermembrane space Source: Ensembl
  7. mitochondrion Source: MGI
  8. peroxisomal membrane Source: MGI
  9. peroxisome Source: UniProtKB
  10. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111Q → H: Acatalasemia.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 527526CatalasePRO_0000084902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei13 – 131N6-succinyllysine1 Publication
Modified residuei221 – 2211N6-succinyllysine1 Publication
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei306 – 3061N6-acetyllysine; alternate1 Publication
Modified residuei306 – 3061N6-succinyllysine; alternate1 Publication
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei430 – 4301N6-acetyllysine; alternate1 Publication
Modified residuei430 – 4301N6-succinyllysine; alternate1 Publication
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei449 – 4491N6-acetyllysine; alternate2 Publications
Modified residuei449 – 4491N6-succinyllysine; alternate1 Publication
Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
Modified residuei480 – 4801N6-succinyllysine; alternate1 Publication
Modified residuei499 – 4991N6-acetyllysine1 Publication
Modified residuei522 – 5221N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP24270.
PaxDbiP24270.
PRIDEiP24270.

2D gel databases

SWISS-2DPAGEP24270.

PTM databases

PhosphoSiteiP24270.

Expressioni

Gene expression databases

BgeeiP24270.
CleanExiMM_CAT.
ExpressionAtlasiP24270. baseline and differential.
GenevestigatoriP24270.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP24270. 3 interactions.
MINTiMINT-1859622.

Structurei

3D structure databases

ProteinModelPortaliP24270.
SMRiP24270. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP24270.
KOiK03781.
OMAiEVEQMAY.
OrthoDBiEOG7V7660.
TreeFamiTF300540.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24270-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF
110 120 130 140 150
EHIGKRTPIA VRFSTVTGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT
160 170 180 190 200
PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF
210 220 230 240 250
SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ GIKNLPVGEA
260 270 280 290 300
GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT
310 320 330 340 350
KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM
360 370 380 390 400
LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG
410 420 430 440 450
APNYYPNSFS APEQQRSALE HSVQCAVDVK RFNSANEDNV TQVRTFYTKV
460 470 480 490 500
LNEEERKRLC ENIAGHLKDA QLFIQKKAVK NFTDVHPDYG ARIQALLDKY
510 520
NAEKPKNAIH TYTQAGSHMA AKGKANL
Length:527
Mass (Da):59,795
Last modified:July 27, 2011 - v4
Checksum:i4D86F3C9D1A3DF9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971A → G in AAA66054. (PubMed:8088826)Curated
Sequence conflicti117 – 1171T → A in AAA37373. (PubMed:2268310)Curated
Sequence conflicti117 – 1171T → A in CAA36342. (PubMed:2395665)Curated
Sequence conflicti117 – 1171T → A in AAA66054. (PubMed:8088826)Curated
Sequence conflicti117 – 1171T → A in AAH13447. (PubMed:16141072)Curated
Sequence conflicti316 – 3161L → V in AAA66054. (PubMed:8088826)Curated
Sequence conflicti350 – 3501M → K in AAA66054. (PubMed:8088826)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16478.1.
PIRiA36695.
RefSeqiNP_033934.2. NM_009804.2.
UniGeneiMm.4215.

Genome annotation databases

EnsembliENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
GeneIDi12359.
KEGGimmu:12359.
UCSCiuc008liw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS16478.1.
PIRi A36695.
RefSeqi NP_033934.2. NM_009804.2.
UniGenei Mm.4215.

3D structure databases

ProteinModelPortali P24270.
SMRi P24270. Positions 4-501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P24270. 3 interactions.
MINTi MINT-1859622.

PTM databases

PhosphoSitei P24270.

2D gel databases

SWISS-2DPAGE P24270.

Proteomic databases

MaxQBi P24270.
PaxDbi P24270.
PRIDEi P24270.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028610 ; ENSMUSP00000028610 ; ENSMUSG00000027187 .
GeneIDi 12359.
KEGGi mmu:12359.
UCSCi uc008liw.2. mouse.

Organism-specific databases

CTDi 847.
MGIi MGI:88271. Cat.

Phylogenomic databases

eggNOGi COG0753.
GeneTreei ENSGT00390000018100.
HOGENOMi HOG000087852.
HOVERGENi HBG003986.
InParanoidi P24270.
KOi K03781.
OMAi EVEQMAY.
OrthoDBi EOG7V7660.
TreeFami TF300540.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
REACT_253802. Purine catabolism.

Miscellaneous databases

ChiTaRSi Cat. mouse.
NextBioi 281024.
PROi P24270.
SOURCEi Search...

Gene expression databases

Bgeei P24270.
CleanExi MM_CAT.
ExpressionAtlasi P24270. baseline and differential.
Genevestigatori P24270.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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.

Entry informationi

Entry nameiCATA_MOUSE
AccessioniPrimary (citable) accession number: P24270
Secondary accession number(s): Q3TXQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3