DNAS1_PIG
ID DNAS1_PIG Reviewed; 284 AA.
AC P11936; Q95KK2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Deoxyribonuclease-1;
DE EC=3.1.21.1 {ECO:0000269|PubMed:3782104};
DE AltName: Full=Deoxyribonuclease I;
DE Short=DNase I;
DE Flags: Precursor;
GN Name=DNASE1; Synonyms=DNL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=11410284; DOI=10.1016/s0167-4838(01)00196-0;
RA Mori S., Yasuda T., Takeshita H., Nakajima T., Nakazato E., Mogi K.,
RA Kaneko Y., Kishi K.;
RT "Molecular, biochemical and immunological analyses of porcine pancreatic
RT DNase I.";
RL Biochim. Biophys. Acta 1547:275-287(2001).
RN [2]
RP PROTEIN SEQUENCE OF 23-284, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT
RP ASN-40 AND ASN-128, AND DISULFIDE BONDS.
RC TISSUE=Pancreas;
RX PubMed=3782104; DOI=10.1016/s0021-9258(18)66667-0;
RA Paudel H.K., Liao T.-H.;
RT "Purification, characterization, and the complete amino acid sequence of
RT porcine pancreatic deoxyribonuclease.";
RL J. Biol. Chem. 261:16006-16011(1986).
CC -!- FUNCTION: Serum endocuclease secreted into body fluids by a wide
CC variety of exocrine and endocrine organs (PubMed:3782104). Expressed by
CC non-hematopoietic tissues and preferentially cleaves protein-free DNA
CC (By similarity). Among other functions, seems to be involved in cell
CC death by apoptosis (PubMed:3782104). Binds specifically to G-actin and
CC blocks actin polymerization (By similarity). Together with DNASE1L3,
CC plays a key role in degrading neutrophil extracellular traps (NETs) (By
CC similarity). NETs are mainly composed of DNA fibers and are released by
CC neutrophils to bind pathogens during inflammation (By similarity).
CC Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to
CC prevent formation of clots that obstruct blood vessels and cause organ
CC damage following inflammation (By similarity).
CC {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183,
CC ECO:0000269|PubMed:3782104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.21.1;
CC Evidence={ECO:0000269|PubMed:3782104};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:3782104};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3782104};
CC Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+).
CC {ECO:0000269|PubMed:3782104};
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; AB048832; BAB62268.1; -; mRNA.
DR PIR; A26324; A26324.
DR RefSeq; NP_999156.1; NM_213991.1.
DR AlphaFoldDB; P11936; -.
DR SMR; P11936; -.
DR STRING; 9823.ENSSSCP00000008492; -.
DR iPTMnet; P11936; -.
DR PaxDb; P11936; -.
DR PRIDE; P11936; -.
DR GeneID; 397051; -.
DR KEGG; ssc:397051; -.
DR CTD; 1773; -.
DR eggNOG; ENOG502QQFT; Eukaryota.
DR InParanoid; P11936; -.
DR OrthoDB; 1282784at2759; -.
DR BRENDA; 3.1.21.1; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 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; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3782104"
FT CHAIN 23..284
FT /note="Deoxyribonuclease-1"
FT /id="PRO_0000007279"
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:0000269|PubMed:3782104"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3782104"
FT DISULFID 123..126
FT /evidence="ECO:0000269|PubMed:3782104"
FT DISULFID 195..231
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT CONFLICT 109
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="S -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..230
FT /note="TH -> HT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..266
FT /note="EQ -> QE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 31626 MW; 1348C169B61EB8C9 CRC64;
MRAARLMGAL LALAGLLQLA LSLRIAAFNI RTFGETKMSN ATLSNYIVRI LSRYDIALIQ
EVRDSHLTAV GKLLNELNQD DPNNYHHVVS EPLGRSTYKE RYLFVFRPDQ VSVLDSYLYD
DGCEPCGNDT FNREPSVVKF SSPSTQVKEF AIVPLHAAPS DAAAEIDSLY DVYLNVRQKW
DLEDIMLMGD FNAGCSYVTT SHWSSIRLRE SPPFQWLIPD TADTTVSSTH CAYDRIVVAG
PLLQRAVVPD SAAPFDFQAA FGLSEQTALA ISDHYPVEVT LKRA
