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Protein

Deoxyribonuclease gamma

Gene

Dnase1l3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (PubMed:7957253). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA. 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. Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity (By similarity). Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). 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 (By similarity).By similarity1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by zinc.1 Publication

pH dependencei

Optimum pH is 7.2. Active from pH 6.0 to 9.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei105By similarity1
Active sitei160By similarity1

GO - Molecular functioni

  • DNA binding Source: RGD
  • endodeoxyribonuclease activity Source: RGD

GO - Biological processi

  • apoptotic DNA fragmentation Source: RGD
  • DNA catabolic process, endonucleolytic Source: UniProtKB
  • neutrophil activation involved in immune response Source: UniProtKB
  • programmed cell death involved in cell development Source: Ensembl
  • regulation of acute inflammatory response Source: UniProtKB
  • regulation of neutrophil mediated cytotoxicity Source: UniProtKB

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processApoptosis
LigandCalcium

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyribonuclease gamma (EC:3.1.21.-)
Short name:
DNase gamma
Alternative name(s):
DNaseY
Deoxyribonuclease I-like 3
Short name:
DNase I-like 3
Gene namesi
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi620669 Dnase1l3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
ChainiPRO_000000729026 – 310Deoxyribonuclease gammaAdd BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi199 ↔ 236Essential for enzymatic activityBy similarity

Post-translational modificationi

Seems to be synthesized as an inactive precursor protein and converted into an active mature enzyme by removal of the N-terminal precursor peptide during apoptosis.
Poly-ADP-ribosylated by PARP1. ADP-ribosylation negatively regulates enzymatic activity during apoptosis.By similarity

Keywords - PTMi

ADP-ribosylation, Disulfide bond

Proteomic databases

PaxDbiO89107
PRIDEiO89107

Expressioni

Tissue specificityi

Detected at high levels in spleen, lymph nodes, thymus and liver. Observed also in kidney and testis, but not in brain or heart.

Gene expression databases

BgeeiENSRNOG00000009291
GenevisibleiO89107 RN

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012532

Structurei

3D structure databases

ProteinModelPortaliO89107
SMRiO89107
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni289 – 310Not required for free DNA-nuclease activity but required for activity towards liposome-coated DNABy similarityAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi40 – 56Bipartite nuclear localization signalSequence analysisAdd BLAST17
Motifi301 – 307Nuclear localization signalSequence analysis7

Sequence similaritiesi

Belongs to the DNase I family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHHA Eukaryota
ENOG410ZR9A LUCA
GeneTreeiENSGT00390000013146
HOGENOMiHOG000059570
HOVERGENiHBG051368
InParanoidiO89107
KOiK11995
OMAiHDYQDGD
OrthoDBiEOG091G0I0B
PhylomeDBiO89107
TreeFamiTF329541

Family and domain databases

Gene3Di3.60.10.10, 1 hit
InterProiView protein in InterPro
IPR018057 Deoxyribonuclease-1_AS
IPR016202 DNase_I
IPR033125 DNASE_I_2
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
PfamiView protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PIRSFiPIRSF000988 DNase_I_euk, 1 hit
PRINTSiPR00130 DNASEI
SMARTiView protein in SMART
SM00476 DNaseIc, 1 hit
SUPFAMiSSF56219 SSF56219, 1 hit
PROSITEiView protein in PROSITE
PS00919 DNASE_I_1, 1 hit
PS00918 DNASE_I_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

O89107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLYPASPYL ASLLLFILAL HGALSLRLCS FNVRSFGESK KENHNAMDII
60 70 80 90 100
VKIIKRCDLI LLMEIKDSNN NICPMLMEKL NGNSRRSTTY NYVISSRLGR
110 120 130 140 150
NTYKEQYAFL YKEKLVSVKA KYLYHDYQDG DTDVFSREPF VVWFQAPFTA
160 170 180 190 200
AKDFVIVPLH TTPETSVKEI DELADVYTDV RRRWKAENFI FMGDFNAGCS
210 220 230 240 250
YVPKKAWKNI RLRTDPNFVW LIGDQEDTTV KKSTSCAYDR IVLRGQEIVN
260 270 280 290 300
SVVPRSSGVF DFQKAYELSE EEALDVSDHF PVEFKLQSSR AFTNSRKSVS
310
LKKKKKGSRS
Length:310
Mass (Da):35,708
Last modified:November 1, 1998 - v1
Checksum:i69C0E0874A3E9107
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039852 mRNA Translation: AAC28937.1
U75689 mRNA Translation: AAC40134.1
BC088122 mRNA Translation: AAH88122.1
RefSeqiNP_446359.1, NM_053907.1
UniGeneiRn.29996

Genome annotation databases

EnsembliENSRNOT00000012532; ENSRNOP00000012532; ENSRNOG00000009291
GeneIDi116687
KEGGirno:116687

Similar proteinsi

Entry informationi

Entry nameiDNSL3_RAT
AccessioniPrimary (citable) accession number: O89107
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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