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Protein

Deoxyribonuclease gamma

Gene

Dnase1l3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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).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
  • programmed cell death involved in cell development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Calcium

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi620669. Dnase1l3.

Subcellular locationi

  • Nucleus 1 Publication
  • Secreted By similarity

  • Note: May first pass through the ER membrane before being imported in the nucleus. Contradictory reports exist about the subcellular localization under normal physiological conditions. Under conditions of cell death, may diffuse and/or be actively transported to the nucleus (By similarity).By similarityCurated

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • nucleus Source: RGD
Complete GO annotation...

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.

Structurei

3D structure databases

ProteinModelPortaliO89107.
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.
OMAiQSPHTAV.
OrthoDBiEOG091G0I0B.
PhylomeDBiO89107.
TreeFamiTF329541.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR033125. DNASE_I_2.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR11371. PTHR11371. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFiPIRSF000988. DNase_I_euk. 1 hit.
PRINTSiPR00130. DNASEI.
SMARTiSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO89107.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiO89107.
PRIDEiO89107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012532; ENSRNOP00000012532; ENSRNOG00000009291.
GeneIDi116687.
KEGGirno:116687.

Organism-specific databases

CTDi1776.
RGDi620669. Dnase1l3.

Phylogenomic databases

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

Miscellaneous databases

PROiO89107.

Gene expression databases

BgeeiENSRNOG00000009291.
GenevisibleiO89107. RN.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR033125. DNASE_I_2.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR11371. PTHR11371. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFiPIRSF000988. DNase_I_euk. 1 hit.
PRINTSiPR00130. DNASEI.
SMARTiSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNSL3_RAT
AccessioniPrimary (citable) accession number: O89107
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 120 of the entry and version 1 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.