DNAS1_CANLF
ID DNAS1_CANLF Reviewed; 284 AA.
AC Q767J3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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;
DE Flags: Precursor;
GN Name=DNASE1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ACTIN, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=14688237; DOI=10.1093/jb/mvg196;
RA Kaneko Y., Takeshita H., Mogi K., Nakajima T., Yasuda T., Itoi M.,
RA Kuwano H., Kishi K.;
RT "Molecular, biochemical and immunological analyses of canine pancreatic
RT DNase I.";
RL J. Biochem. 134:711-718(2003).
CC -!- FUNCTION: Serum endocuclease secreted into body fluids by a wide
CC variety of exocrine and endocrine organs (PubMed:14688237). 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 (PubMed:14688237). Binds specifically to G-
CC actin and blocks actin polymerization (PubMed:14688237). Together with
CC DNASE1L3, plays a key role in degrading neutrophil extracellular traps
CC (NETs) (By similarity). NETs are mainly composed of DNA fibers and are
CC released by neutrophils to bind pathogens during inflammation (By
CC similarity). 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:P21704, ECO:0000250|UniProtKB:P49183,
CC ECO:0000269|PubMed:14688237}.
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 -!- TISSUE SPECIFICITY: Highest expression in pancreas.
CC {ECO:0000269|PubMed:14688237}.
CC -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
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DR EMBL; AB113380; BAD06000.1; -; mRNA.
DR RefSeq; NP_001002946.1; NM_001002946.1.
DR AlphaFoldDB; Q767J3; -.
DR SMR; Q767J3; -.
DR STRING; 9615.ENSCAFP00000054576; -.
DR PaxDb; Q767J3; -.
DR Ensembl; ENSCAFT00000093753; ENSCAFP00000054576; ENSCAFG00000019267.
DR Ensembl; ENSCAFT00030005956; ENSCAFP00030005264; ENSCAFG00030003196.
DR Ensembl; ENSCAFT00845003514; ENSCAFP00845002788; ENSCAFG00845002013.
DR GeneID; 403413; -.
DR KEGG; cfa:403413; -.
DR CTD; 1773; -.
DR VEuPathDB; HostDB:ENSCAFG00845002013; -.
DR VGNC; VGNC:40023; DNASE1.
DR eggNOG; ENOG502QQFT; Eukaryota.
DR GeneTree; ENSGT00950000182846; -.
DR HOGENOM; CLU_043335_2_1_1; -.
DR InParanoid; Q767J3; -.
DR OMA; SCPFTEV; -.
DR OrthoDB; 1282784at2759; -.
DR TreeFam; TF329541; -.
DR BRENDA; 3.1.21.1; 1153.
DR Proteomes; UP000002254; Chromosome 6.
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; 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..284
FT /note="Deoxyribonuclease-1"
FT /id="PRO_0000007276"
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 87
FT /note="Nitration by tetranitromethane destroys a Ca(2+)
FT binding site and inactivates enzyme"
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 284 AA; 31485 MW; 0EE5FEE145CA10AF CRC64;
MRGARLMGAL LALAGLLQGA LALRMAAFNI RTFGETKMSN ATLSKYIVQI LSRYDVAVVQ
EVRDSHLTAV GKLLDTLNQD DPNAYHYVVS EPLGRSSYKE RYLFLFRPDR VSVLDSYQYD
DGCEPCGNDT FSREPAIVRF HSPLTEVKEF AVVPLHAAPL DAVAEIDALY DVYLDVQHKW
DLEDIVLMGD FNAGCSYVAA SQWSSIRLRT NPAFQWLIPD TADTTSTSTH CAYDRIVVAG
SQLQHAVVPE SAAPFNFQVA YGLSSQLAQA ISDHYPVEVT LKRA
