DNAS1_SHEEP
ID DNAS1_SHEEP Reviewed; 260 AA.
AC P11937;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Deoxyribonuclease-1;
DE EC=3.1.21.1 {ECO:0000250|UniProtKB:P24855};
DE AltName: Full=Deoxyribonuclease I;
DE Short=DNase I;
GN Name=DNASE1; Synonyms=DNL1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-18.
RC TISSUE=Pancreas;
RX PubMed=3782105; DOI=10.1016/s0021-9258(18)66668-2;
RA Paudel H.K., Liao T.-H.;
RT "Comparison of the three primary structures of deoxyribonuclease isolated
RT from bovine, ovine, and porcine pancreas. Derivation of the amino acid
RT sequence of ovine DNase and revision of the previously published amino acid
RT sequence of bovine DNase.";
RL J. Biol. Chem. 261:16012-16017(1986).
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 PIR; B26325; B26325.
DR AlphaFoldDB; P11937; -.
DR SMR; P11937; -.
DR STRING; 9940.ENSOARP00000002296; -.
DR iPTMnet; P11937; -.
DR PRIDE; P11937; -.
DR eggNOG; ENOG502QQFT; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Actin-binding; Apoptosis; Calcium; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Nuclease; Nucleus; Reference proteome; Secreted.
FT CHAIN 1..260
FT /note="Deoxyribonuclease-1"
FT /id="PRO_0000145099"
FT ACT_SITE 78
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT ACT_SITE 134
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT SITE 13
FT /note="Involved in actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT SITE 65
FT /note="Nitration by tetranitromethane destroys a Ca(2+)
FT binding site and inactivates enzyme"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT SITE 67
FT /note="Involved in actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3782105"
FT DISULFID 101..104
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT DISULFID 173..209
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT VARIANT 163
FT /note="I -> V (in minor variant)"
SQ SEQUENCE 260 AA; 28939 MW; B1B4D2C50DA3BF20 CRC64;
LKIAAFNIRT FGETKMSNAT LSSYIVRILR RYDIALIEQV RDSHLVAVGK LLDDLNQDDP
NSYHYVVSEP LGRNSYKERY LFVFRPNKVS VLDTYQYDDG CESCGNDSFS REPAVVKFSS
PSTKVKAFAI VPLHSAPSDA VAEINSLYDV YLDVQQKWDL NDIMLMGDFN ADCSYVTSSQ
WSSIRLRTSS TFQWLIPDSA DTTATSTNCA YDRIVVAGSL LQSSVVGPSA VPFDFQAAYG
LSNEMALAIS DHYPVEVTLT
