Dnase1l3
entrez
13421
canonical
uniprot
O55070
canonical
ensembl
ENSMUSG00000025279
resolver
ensp
ENSMUSP00000026315
resolver
enst
ENSMUST00000026315
resolver
genesymbol
Dnase1l3
resolver
uniprot
Q91X38
resolver
uniprot_entry
DNSL3_MOUSE
resolver
uniprot_sec
Q91X38
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by zinc. Inhibited by heparin and proteolysis by plasmin. {ECO:0000250|UniProtKB:O89107, ECO:0000269|PubMed:19154352}.
uniprot
proteins
amino_acid_sequence
MSLHPASPRLASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSRRSTTYNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVKKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQSSRAFTNNRKSVSLKKRKKGNRS
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 (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA (PubMed:12095301, PubMed:15796714, PubMed:19154352). 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}.
uniprot
proteins
mass_dalton
35760
uniprot
proteins
post_translational_modification
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
10807908
uniprot
proteins
pubmed
12050166
uniprot
proteins
pubmed
12095301
uniprot
proteins
pubmed
12974753
uniprot
proteins
pubmed
15167901
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15796714
uniprot
proteins
pubmed
17218958
uniprot
proteins
pubmed
19154352
uniprot
proteins
pubmed
24312463
uniprot
proteins
pubmed
27293190
uniprot
proteins
pubmed
29191910
uniprot
proteins
pubmed
9714828
uniprot
proteins
sequence_length
310
uniprot
proteins
subcellular_location
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}.
uniprot
proteins