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Information on EC 3.1.21.1 - deoxyribonuclease I and Organism(s) Mus musculus and UniProt Accession P49183
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3.1.21.1 deoxyribonuclease ISpecify your search results
Word Map
- 3.1.21.1
-
footprint
- polymerases
- chromatin
- strand
- milk
- neutrophil
-
single-stranded
- lysozyme
-
exonuclease
- herpes
- bacteriophage
- viruses
- phage
- histone
- triphosphate
- simplex
- transferrin
- polymerization
- infant
- transcriptase
- immunoglobulin
- actin
-
fidelity
- nucleosome
- duplex
- myeloperoxidase
- mismatch
- thymidine
- cytomegalovirus
- dntp
-
protein-dna
- fork
-
sequence-specific
- pcna
- sp1
- endonucleases
- herpesvirus
- iga
-
dna-protein
-
micrococcal
- nucleases
- ganciclovir
- whey
- beta-globin
-
supercoiled
-
exotoxin
-
dna-dependent
- ssdna
- medicine
- diagnostics
- streptokinase
- molecular biology
- analysis
- lamivudine
- pharmacology
- degradation
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lactoferrin, dna polymerase, dnase i, colicin, diphtheria toxin, dnaase, deoxyribonuclease, dnasei, deoxyribonuclease i, crm197, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deoxyribonuclease
-
-
-
-
deoxyribonuclease A
-
-
-
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deoxyribonucleic phosphatase
-
-
-
-
desoxyribonuclease
-
-
-
-
DNA endonuclease
-
-
-
-
DNase
-
-
-
-
DNase I
Dornase alfa
-
-
-
-
endodeoxyribonuclease I
-
-
-
-
Escherichia coli endonuclease I
-
-
-
-
nuclease, deoxyribo-
-
-
-
-
nuclease, Escherichia coli endo-, I
-
-
-
-
pancreatic deoxyribonuclease
-
-
-
-
pancreatic DNase
-
-
-
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streptodornase
-
-
-
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DNase I
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9003-98-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chromatin + H2O
?
recombinant DNase1 degrades chromatin effectively only in cooperation with serine proteases, such as plasmin or thrombin, which remove DNA-bound proteins. Recombinant DNase1/3 degrades chromatin without proteolytic help
-
-
?
H2AL2 nucleosome core particle + H2O
?
-
DNase I and hydroxyl radical footprinting as well as micrococcal and exonuclease III digestion show alterations in the structure of the histone variant H2AL2 nucleosome all over the nucleosomal DNA length
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I is involved in chromatin disposal in necrotic tissue
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase Y is involved in chromatin disposal in necrotic tissue
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
low activity on plasmid DNA, high activity on nuclear DNA
-
-
?
additional information
?
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
-
postnatal spermatogonia show higher sensitivity to DNase-I digestion than isolated Sertoli cells or MSC-1 Sertoli cell line
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mn2+
activity of recombinant DNase1 in the presence of Mn2+ is increased only slightly, whereas recombinant DNase1/3 displays strongly enhanced nucleolysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
actin
inhibition of enzyme by actin may serve as a self-protection mechanism against premature DNA degradtion during cell damage
NaCl
increasing concentrations of NaCl (approximately half activity in the presence of 50 mM NaCl) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (approximately half activity in the presence of 150 mM NaCl)
plasmin
directly inhibits recombinant DNase1/3, but does not inactivate recombinant DNase1
-
Tris
increasing concentrations of Tris (approximately half activity in the presence of 80 mM Tris) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (no inhibitory influence of Tris)
additional information
DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
-
additional information
-
DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
pH optimum of recombinant DNase1 is 6.5-7.5 in the presence of Mg2+, and 7.5-8.5 in the presence of Mn2+. PH optimum of recombinant DNase1/3 in the presence of Mg2+ shifts from pH 4.5-5.5 to pH 5.5-6.5 by Mn2+
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
contains two nucleases, DNase1 and DNase1/3. DNase1/3 is not N-glycosylated, whereas DNase1 is di-N-glycosylated
-
lupus-prone NZB/NZW mice have significantly lower serum concentrations of DNase 1 than normal mice, and this reduction is not related to the presence of actin
-
lupus-prone NZB/NZW mice have significantly lower urine concentrations of DNase 1 than normal mice, and this reduction is not related to the presence of actin
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
DNase I hypersensitivity analysis of the mouse brain and retina identifies region-specific regulatory elements
additional information
-
DNase I hypersensitivity analysis of the mouse brain and retina identifies region-specific regulatory elements
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DNAS1_MOUSE
284
0
32027
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
interaction of enzyme with actin and inhibition by actin. Inhibition may serve as a self-protection mechanism against premature DNA degradtion during cell damage
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A144Y
mutant with extremely reduced actin binding capacity. Induction of apoptosis or necrosis by staurosporine or oxidative stress results in faster chromatin fragmentation in mutant cells. Inclusion of actin under these conditions inhibits chromatin degradation in wild-type, but not in mutant
additional information
additional information
DNase1 knockout mice, contain residual nuclease activity. Addition of aprotinin or plasminogen activator inhibitor 1 to the sera of DNase1 KO mice completes chromatolysis to mononucleosomes and even to oligonucleotides
additional information
-
DNase1 knockout mice, contain residual nuclease activity. Addition of aprotinin or plasminogen activator inhibitor 1 to the sera of DNase1 KO mice completes chromatolysis to mononucleosomes and even to oligonucleotides
additional information
-
young DNase+/- and DNase-/- mice are healthy, but at the age of 6-8 months several animals show symptoms of disease and die. DNase+/- and DNase-/- animals reveal the presence of ANAs and signs of glomerulonephritis, suggesting a correlation between the activity of DNase1 and a systemic lupus erythematosus-like disease. The prevalence of ANAs and glomerulonephritis is higher in female mice than in males and higher in DNase-/- animals than in DNase+/- mice. Female DNase 1-deficient mice contain antibodies against dsDNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
NIH-3T3 cells with expression vectors for murine DNase1 and DNase1/3 cDNA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
DNase 1 activity is important to prevent immune stimulation and therefore its reduction or loss may result in a high risk to produce ANAs thus contributing to a potential prerequisite to develop a systemic lupus erythematosus-like disease. Survival of DNase 1-treated mice is longer that non-treated mice
molecular biology
-
DNase-I hypersensitive sites may constitute a molecular marker to identify alleles and subsequently acquire the appropriate methylation imprint. This molecular identifier may be present or absent for a specific gene according to the sex of the gamete
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takeshita, H.; Yasuda, T.; Nakajima, T.; Hosomi, O.; Nakashima, Y.; Kishi, K.
Mouse deoxyribonuclease I (DNase I): biochemical and immunological characterization, cDNA structure and tissue distribution
Biochem. Mol. Biol. Int.
42
65-75
1997
Homo sapiens, Mus musculus, Rattus sp.
Napirei, M.; Wulf, S.; Eulitz, D.; Mannherz, H.G.; Kloeckl, T.
Comparative characterization of rat deoxyribonuclease 1 (Dnase1) and murine deoxyribonuclease 1-like 3 (Dnase1l3)
Biochem. J.
389
355-364
2005
Mus musculus, Rattus norvegicus (P21704)
Napirei, M.; Gultekin, A.; Kloeckl, T.; Moroy, T.; Frostegard, J.; Mannherz, H.G.
Systemic lupus-erythematosus: deoxyribonuclease 1 in necrotic chromatin disposal
Int. J. Biochem. Cell Biol.
38
297-306
2006
Mus musculus
Eulitz, D.; Mannherz, H.G.
Inhibition of deoxyribonuclease I by actin is to protect cells from premature cell death
Apoptosis
12
1511-1521
2007
Mus musculus (P49183)
Martnez Valle, F.; Balada, E.; Ordi-Ros, J.; Vilardell-Tarres, M.
DNase 1 and systemic lupus erythematosus
Autoimmun. Rev.
7
359-363
2008
Bos taurus, Homo sapiens, Mus musculus
Napirei, M.; Ludwig, S.; Mezrhab, J.; Klckl, T.; Mannherz, H.G.
Murine serum nucleases - contrasting effects of plasmin and heparin on the activities of DNase1 and DNase1-like 3 (DNase1/3)
FEBS J.
276
1059-1073
2009
Homo sapiens, Mus musculus (O55070), Mus musculus, Mus musculus C57BL/6 (O55070)
Boyano, M.D.; Andollo, N.; Zalduendo, M.M.; Archaga, J.
Imprinting of mammalian male gametes is gene specific and does not occur at a single stage of differentiation
Int. J. Dev. Biol.
52
1105-1111
2008
Mus musculus
Syed, S.H.; Boulard, M.; Shukla, M.S.; Gautier, T.; Travers, A.; Bednar, J.; Faivre-Moskalenko, C.; Dimitrov, S.; Angelov, D.
The incorporation of the novel histone variant H2AL2 confers unusual structural and functional properties of the nucleosome
Nucleic Acids Res.
37
4684-4695
2009
Mus musculus
Wilken, M.S.; Brzezinski, J.A.; La Torre, A.; Siebenthall, K.; Thurman, R.; Sabo, P.; Sandstrom, R.S.; Vierstra, J.; Canfield, T.K.; Hansen, R.S.; Bender, M.A.; Stamatoyannopoulos, J.; Reh, T.A.
DNase I hypersensitivity analysis of the mouse brain and retina identifies region-specific regulatory elements
Epigenetics Chromatin
8
8
2015
Mus musculus (P49183), Mus musculus
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