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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

May play a role in the early stages of apoptotic DNA fragmentation. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by zinc.

pH dependencei

Optimum pH is 7.2. Active from pH 6.0 to 9.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051By similarity
Active sitei160 – 1601By similarity

GO - Molecular functioni

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

GO - Biological processi

  • apoptotic DNA fragmentation Source: RGD
  • developmental programmed cell death 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
Name:Dnase1l3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi620669. Dnase1l3.

Subcellular locationi

  • Nucleus

  • Note: May first pass through the ER membrane before being imported in the nucleus.

GO - Cellular componenti

  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 310285Deoxyribonuclease gammaPRO_0000007290Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.

Keywords - PTMi

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

GenevisibleiO89107. RN.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliO89107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi40 – 5617Bipartite nuclear localization signalSequence analysisAdd
BLAST
Motifi301 – 3077Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the DNase I family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHHA. Eukaryota.
ENOG410ZR9A. LUCA.
GeneTreeiENSGT00390000013146.
HOGENOMiHOG000059570.
HOVERGENiHBG051368.
InParanoidiO89107.
KOiK11995.
OMAiDSNNRIC.
OrthoDBiEOG73V6KW.
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.
OMAiDSNNRIC.
OrthoDBiEOG73V6KW.
PhylomeDBiO89107.
TreeFamiTF329541.

Miscellaneous databases

PROiO89107.

Gene expression databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "DNaseY: a rat DNaseI-like gene coding for a constitutively expressed chromatin-bound endonuclease."
    Liu Q.Y., Pandey S., Singh R.K., Lin W., Ribecco M., Borowy-Borowski H., Smith B., Leblanc J., Walker P.R., Sikorska M.
    Biochemistry 37:10134-10143(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Molecular cloning and expression of a cDNA encoding an apoptotic endonuclease DNase gamma."
    Shiokawa D., Tanuma S.
    Biochem. J. 332:713-720(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Spleen.
  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: Liver.
  4. "Purification, characterization, and amino acid sequencing of DNase gamma from rat spleen."
    Shiokawa D., Iwamatsu A., Tanuma S.
    Arch. Biochem. Biophys. 346:15-20(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    Tissue: Spleen.
  5. "Purification and properties of DNase gamma from apoptotic rat thymocytes."
    Shiokawa D., Ohyama H., Yamada T., Tanuma S.
    Biochem. J. 326:675-681(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
  6. "Identification of an endonuclease responsible for apoptosis in rat thymocytes."
    Shiokawa D., Ohyama H., Yamada T., Takahashi K., Tanuma S.
    Eur. J. Biochem. 226:23-30(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: Sprague-Dawley.
    Tissue: Spleen.

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: June 8, 2016
This is version 117 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.