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Deoxyribonuclease gamma (DNase gamma) (EC 3.1.21.-) (DNase I homolog protein DHP2) (Deoxyribonuclease I-like 3) (DNase I-like 3) (Liver and spleen DNase) (LS-DNase) (LSD)

 DNSL3_MOUSE             Reviewed;         310 AA.
O55070; Q91X38;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
10-OCT-2018, entry version 140.
RecName: Full=Deoxyribonuclease gamma;
Short=DNase gamma;
EC=3.1.21.-;
AltName: Full=DNase I homolog protein DHP2;
AltName: Full=Deoxyribonuclease I-like 3;
Short=DNase I-like 3;
AltName: Full=Liver and spleen DNase;
Short=LS-DNase;
Short=LSD;
Flags: Precursor;
Name=Dnase1l3 {ECO:0000312|MGI:MGI:1314633};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9714828; DOI=10.1016/S0378-1119(98)00281-9;
Baron W.F., Pan C.Q., Spencer S.A., Ryan A.M., Lazarus R.A.,
Baker K.P.;
"Cloning and characterization of an actin-resistant DNase I-like
endonuclease secreted by macrophages.";
Gene 215:291-301(1998).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6J;
Shiokawa D., Tanuma S.;
"Characterization of the murine DNase gamma gene.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10807908; DOI=10.1074/jbc.M001087200;
Yakovlev A.G., Wang G., Stoica B.A., Boulares H.A., Spoonde A.Y.,
Yoshihara K., Smulson M.E.;
"A role of the Ca2+/Mg2+-dependent endonuclease in apoptosis and its
inhibition by poly(ADP-ribose) polymerase.";
J. Biol. Chem. 275:21302-21308(2000).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12050166; DOI=10.1074/jbc.M204038200;
Shiokawa D., Kobayashi T., Tanuma S.;
"Involvement of DNase gamma in apoptosis associated with myogenic
differentiation of C2C12 cells.";
J. Biol. Chem. 277:31031-31037(2002).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12095301; DOI=10.1006/mthe.2002.0625;
Wilber A., Lu M., Schneider M.C.;
"Deoxyribonuclease I-like III is an inducible macrophage barrier to
liposomal transfection.";
Mol. Ther. 6:35-42(2002).
[7]
FUNCTION.
PubMed=15167901; DOI=10.1038/sj.cdd.4401454;
Shiokawa D., Tanuma S.;
"Differential DNases are selectively used in neuronal apoptosis
depending on the differentiation state.";
Cell Death Differ. 11:1112-1120(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, COFACTOR, AND ACTIVITY REGULATION.
PubMed=15796714; DOI=10.1042/BJ20042124;
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).
[9]
FUNCTION.
PubMed=17218958; DOI=10.1038/sj.cdd.4402086;
Shiokawa D., Shika Y., Araki S., Sunaga S., Mizuta R., Kitamura D.,
Tanuma S.;
"Stage-specific expression of DNasegamma during B-cell development and
its role in B-cell receptor-mediated apoptosis in WEHI-231 cells.";
Cell Death Differ. 14:992-1000(2007).
[10]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=19154352; DOI=10.1111/j.1742-4658.2008.06849.x;
Napirei M., Ludwig S., Mezrhab J., Kloeckl T., Mannherz H.G.;
"Murine serum nucleases--contrasting effects of plasmin and heparin on
the activities of DNase1 and DNase1-like 3 (DNase1l3).";
FEBS J. 276:1059-1073(2009).
[11]
FUNCTION.
PubMed=24312463; DOI=10.1371/journal.pone.0080223;
Mizuta R., Araki S., Furukawa M., Furukawa Y., Ebara S., Shiokawa D.,
Hayashi K., Tanuma S., Kitamura D.;
"DNase gamma is the effector endonuclease for internucleosomal DNA
fragmentation in necrosis.";
PLoS ONE 8:E80223-E80223(2013).
[12]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=27293190; DOI=10.1016/j.cell.2016.05.034;
Sisirak V., Sally B., D'Agati V., Martinez-Ortiz W., Oezcakar Z.B.,
David J., Rashidfarrokhi A., Yeste A., Panea C., Chida A.S.,
Bogunovic M., Ivanov I.I., Quintana F.J., Sanz I., Elkon K.B.,
Tekin M., Yalcinkaya F., Cardozo T.J., Clancy R.M., Buyon J.P.,
Reizis B.;
"Digestion of chromatin in apoptotic cell microparticles prevents
autoimmunity.";
Cell 166:88-101(2016).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=29191910; DOI=10.1126/science.aam8897;
Jimenez-Alcazar M., Rangaswamy C., Panda R., Bitterling J.,
Simsek Y.J., Long A.T., Bilyy R., Krenn V., Renne C., Renne T.,
Kluge S., Panzer U., Mizuta R., Mannherz H.G., Kitamura D.,
Herrmann M., Napirei M., Fuchs T.A.;
"Host DNases prevent vascular occlusion by neutrophil extracellular
traps.";
Science 358:1202-1206(2017).
[14]
VARIANT ILE-89, CHARACTERIZATION OF ILE-89, AND POSSIBLE INVOLVEMENT
IN SLE.
PubMed=12974753; DOI=10.1046/j.1365-2249.2003.02267.x;
Wilber A., O'Connor T.P., Lu M.L., Karimi A., Schneider M.C.;
"Dnase1l3 deficiency in lupus-prone MRL and NZB/W F1 mice.";
Clin. Exp. Immunol. 134:46-52(2003).
-!- FUNCTION: Has DNA hydrolytic activity. Is capable of both
single- and double-stranded DNA cleavage, producing DNA fragments
with 3'-OH ends (By similarity). Can cleave chromatin to
nucleosomal units and cleaves nucleosomal and liposome-coated DNA
(PubMed:15796714, PubMed:19154352, PubMed:12095301). Acts in
internucleosomal DNA fragmentation (INDF) during apoptosis and
necrosis. The role in apoptosis includes myogenic and neuronal
differentiation, and BCR-mediated clonal deletion of self-reactive
B cells (PubMed:12050166, PubMed:15167901, PubMed:17218958,
PubMed:24312463). Is active on chromatin in apoptotic cell-derived
membrane-coated microparticles and thus suppresses anti-DNA
autoimmunity (PubMed:15796714, PubMed:27293190). Together with
DNASE1, plays a key role in degrading neutrophil extracellular
traps (NETs) (PubMed:29191910). NETs are mainly composed of DNA
fibers and are released by neutrophils to bind pathogens during
inflammation (PubMed:29191910). Degradation of intravascular NETs
by DNASE1 and DNASE1L3 is required to prevent formation of clots
that obstruct blood vessels and cause organ damage following
inflammation (PubMed:29191910). {ECO:0000250|UniProtKB:O89107,
ECO:0000269|PubMed:12050166, ECO:0000269|PubMed:15167901,
ECO:0000269|PubMed:17218958, ECO:0000269|PubMed:24312463,
ECO:0000269|PubMed:27293190, ECO:0000269|PubMed:29191910,
ECO:0000305|PubMed:15796714}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:Q13609};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q13609};
-!- ACTIVITY REGULATION: Inhibited by zinc. Inhibited by heparin and
proteolysis by plasmin. {ECO:0000250|UniProtKB:O89107,
ECO:0000269|PubMed:19154352}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13609,
ECO:0000269|PubMed:12050166}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q13609}. Secreted
{ECO:0000269|PubMed:12095301, ECO:0000269|PubMed:15796714,
ECO:0000269|PubMed:27293190}. Note=Contradictory reports exist
about the subcellular localization under normal physiological
conditions. Shown to translocate to rough endoplasmic reticulum
and to be transported through the entire secretory pathway for
secretion. However, under conditions of cell death, may diffuse
and/or be actively transported to the nucleus.
{ECO:0000305|PubMed:15796714, ECO:0000305|PubMed:27293190}.
-!- TISSUE SPECIFICITY: Expressed at high levels in liver, spleen and
testes. Expressed at lower levels in heart, lungs, skeletal muscle
and kidney. Not expressed in brain. Predominantly expressed in
macrophages; at protein level. Secreted by mononuclear phagocytes.
{ECO:0000269|PubMed:10807908, ECO:0000269|PubMed:12050166,
ECO:0000269|PubMed:12095301, ECO:0000269|PubMed:27293190}.
-!- DEVELOPMENTAL STAGE: Expression is first detected at embryonic day
11, and higher amounts were detected at days 15 and 17.
{ECO:0000269|PubMed:10807908}.
-!- PTM: Poly-ADP-ribosylated by PARP1. ADP-ribosylation negatively
regulates enzymatic activity during apoptosis.
{ECO:0000250|UniProtKB:Q13609}.
-!- DISRUPTION PHENOTYPE: Mice develop symptoms of the autoimmune
disease systemic lupus erythematosus, characterized by high titers
of anti-nuclear autoantibodies (ANA) directed against nucleosomes
and double-stranded DNA, the deposition of immune complexes in
glomeruli and full-blown glomerulonephritis (PubMed:27293190).
Mice lacking both Dnase1 and Dnase1l3 show vascular occlusions
following bacterial infection: defects are caused by the formation
of intravascular neutrophil extracellular traps (NETs) clots that
obstruct blood vessels and cause organ damage (PubMed:29191910).
{ECO:0000269|PubMed:27293190, ECO:0000269|PubMed:29191910}.
-!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF047355; AAC35753.1; -; mRNA.
EMBL; U76110; AAD09222.1; -; mRNA.
EMBL; AY024355; AAK07733.1; -; Genomic_DNA.
EMBL; BC012671; AAH12671.1; -; mRNA.
CCDS; CCDS26807.1; -.
RefSeq; NP_031896.3; NM_007870.3.
RefSeq; XP_006517984.1; XM_006517921.3.
UniGene; Mm.272258; -.
UniGene; Mm.490513; -.
ProteinModelPortal; O55070; -.
SMR; O55070; -.
iPTMnet; O55070; -.
PhosphoSitePlus; O55070; -.
MaxQB; O55070; -.
PaxDb; O55070; -.
PRIDE; O55070; -.
Ensembl; ENSMUST00000026315; ENSMUSP00000026315; ENSMUSG00000025279.
GeneID; 13421; -.
KEGG; mmu:13421; -.
UCSC; uc007sem.1; mouse.
CTD; 1776; -.
MGI; MGI:1314633; Dnase1l3.
eggNOG; ENOG410IHHA; Eukaryota.
eggNOG; ENOG410ZR9A; LUCA.
GeneTree; ENSGT00390000013146; -.
HOGENOM; HOG000059570; -.
HOVERGEN; HBG051368; -.
InParanoid; O55070; -.
KO; K11995; -.
OMA; HDYQDGD; -.
OrthoDB; EOG091G0I0B; -.
PhylomeDB; O55070; -.
TreeFam; TF329541; -.
BRENDA; 3.1.21.1; 3474.
PRO; PR:O55070; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000025279; Expressed in 43 organ(s), highest expression level in mesenteric lymph node.
CleanEx; MM_DNASE1L3; -.
Genevisible; O55070; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0004520; F:endodeoxyribonuclease activity; ISO:MGI.
GO; GO:0004519; F:endonuclease activity; IDA:MGI.
GO; GO:0006309; P:apoptotic DNA fragmentation; IDA:MGI.
GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:UniProtKB.
GO; GO:0002283; P:neutrophil activation involved in immune response; IDA:UniProtKB.
GO; GO:0010623; P:programmed cell death involved in cell development; IDA:MGI.
GO; GO:0002673; P:regulation of acute inflammatory response; IDA:UniProtKB.
GO; GO:0070948; P:regulation of neutrophil mediated cytotoxicity; IDA:UniProtKB.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR018057; Deoxyribonuclease-1_AS.
InterPro; IPR016202; DNase_I.
InterPro; IPR033125; DNASE_I_2.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
Pfam; PF03372; Exo_endo_phos; 1.
PIRSF; PIRSF000988; DNase_I_euk; 1.
PRINTS; PR00130; DNASEI.
SMART; SM00476; DNaseIc; 1.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS00919; DNASE_I_1; 1.
PROSITE; PS00918; DNASE_I_2; 1.
1: Evidence at protein level;
ADP-ribosylation; Apoptosis; Calcium; Complete proteome;
Disulfide bond; Endonuclease; Endoplasmic reticulum; Hydrolase;
Necrosis; Nuclease; Nucleus; Reference proteome; Secreted; Signal.
SIGNAL 1 25 {ECO:0000250}.
CHAIN 26 310 Deoxyribonuclease gamma.
/FTId=PRO_0000007289.
REGION 289 310 Not required for free DNA-nuclease
activity but required for activity
towards liposome-coated DNA.
{ECO:0000269|PubMed:12095301}.
MOTIF 40 56 Bipartite nuclear localization signal.
{ECO:0000255}.
MOTIF 301 307 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 105 105 {ECO:0000250|UniProtKB:P00639}.
ACT_SITE 160 160 {ECO:0000250|UniProtKB:P00639}.
DISULFID 199 236 Essential for enzymatic activity.
{ECO:0000269|PubMed:15796714}.
VARIANT 89 89 T -> I (in strain: DBA/2, NZB and NZW, in
vitro decreases nuclease activity against
free DNA by approximately twofold and
decreases activity to establish a barrier
to liposomal gene transfection by
eightfold).
{ECO:0000269|PubMed:12974753}.
SEQUENCE 310 AA; 35760 MW; BE483821E045E374 CRC64;
MSLHPASPRL ASLLLFILAL HDTLALRLCS FNVRSFGASK KENHEAMDII VKIIKRCDLI
LLMEIKDSSN NICPMLMEKL NGNSRRSTTY NYVISSRLGR NTYKEQYAFV YKEKLVSVKT
KYHYHDYQDG DTDVFSREPF VVWFHSPFTA VKDFVIVPLH TTPETSVKEI DELVDVYTDV
RSQWKTENFI FMGDFNAGCS YVPKKAWQNI RLRTDPKFVW LIGDQEDTTV KKSTSCAYDR
IVLCGQEIVN SVVPRSSGVF DFQKAYDLSE EEALDVSDHF PVEFKLQSSR AFTNNRKSVS
LKKRKKGNRS


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