DNAS1_HORSE
ID DNAS1_HORSE Reviewed; 282 AA.
AC Q4AEE3;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Deoxyribonuclease-1;
DE EC=3.1.21.1 {ECO:0000250|UniProtKB:P24855};
DE AltName: Full=Deoxyribonuclease I;
DE Short=DNase I;
DE Flags: Precursor;
GN Name=DNASE1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Parotid gland;
RA Yasuda T.;
RT "Cloning of cDNA encoding horse parotid deoxyribonuclease I.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serum endocuclease secreted into body fluids by a wide
CC variety of exocrine and endocrine organs (By similarity). Expressed by
CC non-hematopoietic tissues and preferentially cleaves protein-free DNA.
CC Among other functions, seems to be involved in cell death by apoptosis.
CC Binds specifically to G-actin and blocks actin polymerization (By
CC similarity). Together with DNASE1L3, plays a key role in degrading
CC neutrophil extracellular traps (NETs). NETs are mainly composed of DNA
CC fibers and are released by neutrophils to bind pathogens during
CC inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3
CC is required to prevent formation of clots that obstruct blood vessels
CC and cause organ damage following inflammation (By similarity).
CC {ECO:0000250|UniProtKB:P00639, ECO:0000250|UniProtKB:P21704,
CC ECO:0000250|UniProtKB:P24855, ECO:0000250|UniProtKB:P49183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.21.1;
CC Evidence={ECO:0000250|UniProtKB:P24855};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P24855};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P24855};
CC Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+).
CC {ECO:0000250|UniProtKB:P24855};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen
CC granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in
CC zymogen granules and found in the nuclear envelope.
CC {ECO:0000250|UniProtKB:P24855}.
CC -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
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DR EMBL; AB162819; BAE19916.1; -; mRNA.
DR RefSeq; NP_001075983.1; NM_001082514.2.
DR AlphaFoldDB; Q4AEE3; -.
DR SMR; Q4AEE3; -.
DR STRING; 9796.ENSECAP00000006438; -.
DR PaxDb; Q4AEE3; -.
DR PeptideAtlas; Q4AEE3; -.
DR GeneID; 100034219; -.
DR KEGG; ecb:100034219; -.
DR CTD; 1773; -.
DR InParanoid; Q4AEE3; -.
DR OrthoDB; 1282784at2759; -.
DR BRENDA; 3.1.21.1; 2120.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042588; C:zymogen granule; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006308; P:DNA catabolic process; IBA:GO_Central.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; ISS:UniProtKB.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0002673; P:regulation of acute inflammatory response; ISS:UniProtKB.
DR GO; GO:0070948; P:regulation of neutrophil mediated cytotoxicity; ISS:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR018057; Deoxyribonuclease-1_AS.
DR InterPro; IPR016202; DNase_I.
DR InterPro; IPR033125; DNASE_I_2.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR PIRSF; PIRSF000988; DNase_I_euk; 1.
DR PRINTS; PR00130; DNASEI.
DR SMART; SM00476; DNaseIc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS00919; DNASE_I_1; 1.
DR PROSITE; PS00918; DNASE_I_2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Apoptosis; Calcium; Cytoplasmic vesicle; Disulfide bond;
KW Endonuclease; Glycoprotein; Hydrolase; Nuclease; Nucleus;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT CHAIN 23..282
FT /note="Deoxyribonuclease-1"
FT /id="PRO_0000042587"
FT ACT_SITE 100
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT ACT_SITE 156
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT SITE 35
FT /note="Involved in actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT SITE 89
FT /note="Involved in actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..126
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT DISULFID 195..231
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000250|UniProtKB:P00639"
SQ SEQUENCE 282 AA; 31708 MW; 154508EA2F77D6CE CRC64;
MRGARLTGAL LALAGLLQVA LSLRIAAFNI RTFGETKMSN DTLSNYIVQI LNRYDIALIQ
EVRDSHLTAV GKLLDRLNQD DPNTYHFVVS EPLGRNNYKE RYLFVFRPDQ VSLLDSYQYN
DGCEPCGNDT FSREPAIVKF SSPFTQVKEF AIVPLHAAPS DALAEIDSLY DVYLDVQQKW
DMEDIMLMGD FNAGCSYVTS SQWPSIRLRR NPAFWWLIPD TADTTVKSTH CAYDRIVVAG
TLLQEAVVPD SAVPFDFQAA YGLNDQTAEA ISDHYPVEVT LM
