DNAS1_RAT
ID DNAS1_RAT Reviewed; 284 AA.
AC P21704; Q5FVU6;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 154.
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; Synonyms=Dnl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Parotid gland;
RX PubMed=2263485; DOI=10.1093/nar/18.23.7151;
RA Polzar B., Mannherz H.G.;
RT "Nucleotide sequence of a full length cDNA clone encoding the
RT deoxyribonuclease I from the rat parotid gland.";
RL Nucleic Acids Res. 18:7151-7151(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9303433; DOI=10.1089/dna.1997.16.911;
RA Liu Q.Y., Ribecco M., Hou Y., Walker P.R., Sikorska M.;
RT "DNase I primary transcript is alternatively spliced in both normal and
RT apoptotic cells: no evidence of up-regulation in apoptosis.";
RL DNA Cell Biol. 16:911-918(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=12036587; DOI=10.1016/s0378-1119(02)00479-1;
RA Basnakian A.G., Singh A.B., Shah S.V.;
RT "Identification and expression of deoxyribonuclease (DNase) I alternative
RT transcripts in the rat.";
RL Gene 289:87-96(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=8428592; DOI=10.1002/j.1460-2075.1993.tb05666.x;
RA Peitsch M.C., Polzar B., Stephan H., Crompton T., McDonald H.R.,
RA Mannherz H.G., Tschopp J.;
RT "Characterization of the endogenous deoxyribonuclease involved in nuclear
RT DNA degradation during apoptosis (programmed cell death).";
RL EMBO J. 12:371-377(1993).
RN [6]
RP FUNCTION.
RX PubMed=15796714; DOI=10.1042/bj20042124;
RA Napirei M., Wulf S., Eulitz D., Mannherz H.G., Kloeckl T.;
RT "Comparative characterization of rat deoxyribonuclease 1 (Dnase1) and
RT murine deoxyribonuclease 1-like 3 (Dnase1l3).";
RL Biochem. J. 389:355-364(2005).
CC -!- FUNCTION: Serum endocuclease secreted into body fluids by a wide
CC variety of exocrine and endocrine organs (PubMed:8428592,
CC PubMed:15796714). Expressed by non-hematopoietic tissues and
CC preferentially cleaves protein-free DNA (PubMed:15796714). Among other
CC functions, seems to be involved in cell death by apoptosis
CC (PubMed:8428592, PubMed:15796714). 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:P00639, ECO:0000250|UniProtKB:P49183,
CC ECO:0000269|PubMed:15796714, ECO:0000269|PubMed:8428592}.
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; X56060; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U76635; AAB71495.1; -; Genomic_DNA.
DR EMBL; AF397150; AAK97471.1; -; mRNA.
DR EMBL; AF397151; AAK97472.1; -; mRNA.
DR EMBL; BC089764; AAH89764.1; -; mRNA.
DR PIR; S13676; S13676.
DR RefSeq; NP_037229.1; NM_013097.2.
DR RefSeq; XP_006245891.1; XM_006245829.3.
DR AlphaFoldDB; P21704; -.
DR SMR; P21704; -.
DR STRING; 10116.ENSRNOP00000009283; -.
DR GlyGen; P21704; 2 sites.
DR PaxDb; P21704; -.
DR Ensembl; ENSRNOT00000009283; ENSRNOP00000009283; ENSRNOG00000006873.
DR GeneID; 25633; -.
DR KEGG; rno:25633; -.
DR UCSC; RGD:2510; rat.
DR CTD; 1773; -.
DR RGD; 2510; Dnase1.
DR eggNOG; ENOG502QQFT; Eukaryota.
DR GeneTree; ENSGT00950000182846; -.
DR HOGENOM; CLU_043335_2_1_1; -.
DR InParanoid; P21704; -.
DR OMA; SCPFTEV; -.
DR OrthoDB; 1282784at2759; -.
DR PhylomeDB; P21704; -.
DR TreeFam; TF329541; -.
DR BRENDA; 3.1.21.1; 5301.
DR PRO; PR:P21704; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000006873; Expressed in kidney and 16 other tissues.
DR Genevisible; P21704; RN.
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:0004536; F:deoxyribonuclease activity; IDA:CACAO.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IDA:RGD.
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..284
FT /note="Deoxyribonuclease-1"
FT /id="PRO_0000007281"
FT ACT_SITE 100
FT /evidence="ECO:0000250|UniProtKB:P00639"
FT ACT_SITE 156
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 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; 32064 MW; 45075AFF133781FA CRC64;
MRYTGLMGIL LTLVNLLQLA ATLRIAAFNI RTFGDTKMSN ATLSSYIVKI LSRYDIAVVQ
EVRDTHLVAV GKLLDELNRD IPDNYRYIIS EPLGRKSYKE QYLFVYRPSQ VSVLDSYHYD
DGCEPCGNDT FSREPAIVKF FSPYTEVREF AIVPLHSAPT EAVSEIDALY DVYLDVRQKW
GLEDIMFMGD FNAGCSYVTS SQWSSIRLRT SPIFQWLIPD SADTTATSTH CAYDRIVVAG
ALLQAAVVPS SAVPFDFQAE YRLTNQMAEA ISDHYPVEVT LRKT
