Dnase1l3
entrez
116687
canonical
uniprot
O89107
canonical
ensembl
ENSRNOG00000009291
resolver
ensembl
ENSRNOG00055013867
resolver
ensembl
ENSRNOG00060020997
resolver
ensembl
ENSRNOG00065008865
resolver
ensp
ENSRNOP00000012532
resolver
ensp
ENSRNOP00055019452
resolver
ensp
ENSRNOP00060029991
resolver
ensp
ENSRNOP00065010590
resolver
enst
ENSRNOT00000012532
resolver
enst
ENSRNOT00055023854
resolver
enst
ENSRNOT00060036436
resolver
enst
ENSRNOT00065014155
resolver
genesymbol
Dnase1l3
resolver
uniprot_entry
DNSL3_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by zinc. {ECO:0000269|PubMed:9665719}.
uniprot
proteins
amino_acid_sequence
MSLYPASPYLASLLLFILALHGALSLRLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSRRSTTYNYVISSRLGRNTYKEQYAFLYKEKLVSVKAKYLYHDYQDGDTDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVKEIDELADVYTDVRRRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTVKKSTSCAYDRIVLRGQEIVNSVVPRSSGVFDFQKAYELSEEEALDVSDHFPVEFKLQSSRAFTNSRKSVSLKKKKKGSRS
uniprot
proteins
ec_number
3.1.21.-
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:O55070, ECO:0000250|UniProtKB:Q13609, ECO:0000269|PubMed:7957253}.
uniprot
proteins
mass_dalton
35708
uniprot
proteins
post_translational_modification
PTM: 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.; PTM: Poly-ADP-ribosylated by PARP1. ADP-ribosylation negatively regulates enzymatic activity during apoptosis. {ECO:0000250|UniProtKB:Q13609}.
uniprot
proteins
protein_family
DNase I family
uniprot
proteins
pubmed
15167901
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
7957253
uniprot
proteins
pubmed
9307016
uniprot
proteins
pubmed
9328279
uniprot
proteins
pubmed
9620874
uniprot
proteins
pubmed
9665719
uniprot
proteins
sequence_length
310
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9665719}. Secreted {ECO:0000250|UniProtKB:O55070, ECO:0000250|UniProtKB:Q13609}. 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). {ECO:0000250|UniProtKB:O55070, ECO:0000305}.
uniprot
proteins