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Protein

Catalase

Gene

Cat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • aerobic respiration Source: Ensembl
  • aging Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cholesterol metabolic process Source: Ensembl
  • hemoglobin metabolic process Source: Ensembl
  • hydrogen peroxide catabolic process Source: RGD
  • kidney development Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  • osteoblast differentiation Source: Ensembl
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  • protein homotetramerization Source: Ensembl
  • response to activity Source: RGD
  • response to cadmium ion Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to fatty acid Source: RGD
  • response to hyperoxia Source: RGD
  • response to hypoxia Source: RGD
  • response to inactivity Source: RGD
  • response to insulin Source: RGD
  • response to L-ascorbic acid Source: RGD
  • response to lead ion Source: RGD
  • response to light intensity Source: RGD
  • response to oxidative stress Source: RGD
  • response to ozone Source: RGD
  • response to phenylpropanoid Source: RGD
  • response to radiation Source: RGD
  • response to reactive oxygen species Source: RGD
  • response to toxic substance Source: RGD
  • response to UV Source: RGD
  • response to vitamin A Source: RGD
  • response to vitamin E Source: RGD
  • triglyceride metabolic process Source: Ensembl
  • ureteric bud development Source: RGD
  • 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

BRENDAi1.11.1.6. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.
R-RNO-74259. Purine catabolism.

Protein family/group databases

PeroxiBasei11811. RnoKat.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:Cat
Synonyms:Cas1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2279. Cat.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • endoplasmic reticulum Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • focal adhesion Source: Ensembl
  • Golgi apparatus Source: RGD
  • lysosome Source: RGD
  • mitochondrial intermembrane space Source: RGD
  • peroxisomal membrane Source: Ensembl
  • peroxisome Source: HGNC
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 527526CatalasePRO_0000084905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei221 – 2211N6-succinyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei306 – 3061N6-acetyllysine; alternateBy similarity
Modified residuei306 – 3061N6-succinyllysine; alternateBy similarity
Modified residuei417 – 4171PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineCombined sources
Modified residuei449 – 4491N6-acetyllysine; alternateBy similarity
Modified residuei449 – 4491N6-succinyllysine; alternateBy similarity
Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
Modified residuei511 – 5111PhosphothreonineBy similarity
Modified residuei517 – 5171PhosphoserineCombined sources
Modified residuei522 – 5221N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP04762.
PRIDEiP04762.

PTM databases

iPTMnetiP04762.
PhosphoSiteiP04762.

Expressioni

Gene expression databases

GenevisibleiP04762. RN.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi246433. 3 interactions.
IntActiP04762. 2 interactions.
STRINGi10116.ENSRNOP00000011230.

Structurei

3D structure databases

ProteinModelPortaliP04762.
SMRiP04762. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP04762.
KOiK03781.
OMAiWDYRADD.
OrthoDBiEOG7V7660.
PhylomeDBiP04762.
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.

P04762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADSRDPASD QMKQWKEQRA PQKPDVLTTG GGNPIGDKLN IMTAGPRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF
110 120 130 140 150
EHIGKRTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT
160 170 180 190 200
PIFFIRDAML FPSFIHSQKR NPQTHLKDPD MVWDFWSLCP ESLHQVTFLF
210 220 230 240 250
SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLPVEEA
260 270 280 290 300
GRLAQEDPDY GLRDLFNAIA SGNYPSWTFY IQVMTFKEAE TFPFNPFDLT
310 320 330 340 350
KVWPHKDYPL IPVGKLVLNR NPANYFAEVE QMAFDPSNMP PGIEPSPDKM
360 370 380 390 400
LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG
410 420 430 440 450
APNYYPNSFS APEQQGSALE HHSQCSADVK RFNSANEDNV TQVRTFYTKV
460 470 480 490 500
LNEEERKRLC ENIANHLKDA QLFIQRKAVK NFTDVHPDYG ARVQALLDQY
510 520
NSQKPKNAIH TYVQAGSHIA AKGKANL
Length:527
Mass (Da):59,757
Last modified:January 23, 2007 - v3
Checksum:iCA28530A0FC6EFA6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti434 – 4341S → N in AAA40885 (PubMed:6547842).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11670 mRNA. Translation: AAA40884.1.
M25680
, 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.
PIRiJU0065. CSRT.
RefSeqiNP_036652.1. NM_012520.2.
UniGeneiRn.3001.

Genome annotation databases

EnsembliENSRNOT00000011230; ENSRNOP00000011230; ENSRNOG00000008364.
GeneIDi24248.
KEGGirno:24248.
UCSCiRGD:2279. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11670 mRNA. Translation: AAA40884.1.
M25680
, 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.
PIRiJU0065. CSRT.
RefSeqiNP_036652.1. NM_012520.2.
UniGeneiRn.3001.

3D structure databases

ProteinModelPortaliP04762.
SMRiP04762. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246433. 3 interactions.
IntActiP04762. 2 interactions.
STRINGi10116.ENSRNOP00000011230.

Chemistry

ChEMBLiCHEMBL1075216.

Protein family/group databases

PeroxiBasei11811. RnoKat.

PTM databases

iPTMnetiP04762.
PhosphoSiteiP04762.

Proteomic databases

PaxDbiP04762.
PRIDEiP04762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011230; ENSRNOP00000011230; ENSRNOG00000008364.
GeneIDi24248.
KEGGirno:24248.
UCSCiRGD:2279. rat.

Organism-specific databases

CTDi847.
RGDi2279. Cat.

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP04762.
KOiK03781.
OMAiWDYRADD.
OrthoDBiEOG7V7660.
PhylomeDBiP04762.
TreeFamiTF300540.

Enzyme and pathway databases

BRENDAi1.11.1.6. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.
R-RNO-74259. Purine catabolism.

Miscellaneous databases

NextBioi602753.
PROiP04762.

Gene expression databases

GenevisibleiP04762. RN.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCATA_RAT
AccessioniPrimary (citable) accession number: P04762
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 144 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.