ID   DNAS1_CHICK             Reviewed;         282 AA.
AC   Q9YGI5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Deoxyribonuclease-1;
DE            EC=3.1.21.1 {ECO:0000269|PubMed:12739897};
DE   AltName: Full=Deoxyribonuclease I;
DE            Short=DNase I;
DE   Flags: Precursor;
GN   Name=DNASE1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC   TISSUE=Pancreas;
RX   PubMed=12739897; DOI=10.1023/a:1023015810840;
RA   Hu C.C., Lu S.C., Cheng C.C., Chen L.H., Liao T.H.;
RT   "Chicken deoxyribonuclease: purification, characterization, gene cloning
RT   and gene expression.";
RL   J. Protein Chem. 22:41-49(2003).
CC   -!- FUNCTION: Serum endocuclease secreted into body fluids by a wide
CC       variety of exocrine and endocrine organs (PubMed:12739897). Expressed
CC       by non-hematopoietic tissues and preferentially cleaves protein-free
CC       DNA (By similarity). Among other functions, seems to be involved in
CC       cell death by apoptosis (By similarity). Binds specifically to G-actin
CC       and blocks actin polymerization (By similarity).
CC       {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P24855,
CC       ECO:0000269|PubMed:12739897}.
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:12739897};
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   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12739897}.
CC   -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
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DR   EMBL; AJ131751; CAA10503.1; -; mRNA.
DR   RefSeq; NP_996840.1; NM_206957.1.
DR   AlphaFoldDB; Q9YGI5; -.
DR   SMR; Q9YGI5; -.
DR   STRING; 9031.ENSGALP00000029321; -.
DR   PaxDb; Q9YGI5; -.
DR   GeneID; 395725; -.
DR   KEGG; gga:395725; -.
DR   CTD; 1773; -.
DR   VEuPathDB; HostDB:geneid_395725; -.
DR   eggNOG; ENOG502QQFT; Eukaryota.
DR   InParanoid; Q9YGI5; -.
DR   OrthoDB; 1282784at2759; -.
DR   BRENDA; 3.1.21.1; 1306.
DR   PRO; PR:Q9YGI5; -.
DR   Proteomes; UP000000539; 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; Disulfide bond;
KW   Endonuclease; Glycoprotein; Hydrolase; Nuclease; Nucleus;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250|UniProtKB:P00639"
FT   CHAIN           21..282
FT                   /note="Deoxyribonuclease-1"
FT                   /id="PRO_0000007282"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000250|UniProtKB:P00639"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000250|UniProtKB:P00639"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        121..124
FT                   /evidence="ECO:0000250|UniProtKB:P00639"
FT   DISULFID        193..229
FT                   /note="Essential for enzymatic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00639"
SQ   SEQUENCE   282 AA;  31400 MW;  2226267860842EA7 CRC64;
     MARLVLELLA AALLLRVAAT LRISAFNIRT FGDSKMSNQT VAGFIVSILV QYDITLVQEV
     RDADLSSVKK LVSQLNSASS YPYSFLSSIP LGRNSYKEQY VFIYRSDIVS VLESYYYDDG
     CESCGTDIFS REPFIVKFSS PTTQLDEFVI VPLHAEPSSA PAEINALTDV YTDVINKWET
     NNIFFMGDFN ADCSYVTAEQ WPSIRLRSLS SCEWLIPDSA DTTVTSTDCA YDRIVACGSA
     LRQAVEYGSA TVNNFQETLR IQNKDALAIS DHFPVEVTLK AR