ID   DNS2A_RAT               Reviewed;         350 AA.
AC   Q9QZK8; Q5BKC7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Deoxyribonuclease-2-alpha;
DE            EC=3.1.22.1;
DE   AltName: Full=Acid DNase;
DE   AltName: Full=Deoxyribonuclease II alpha;
DE            Short=DNase II alpha;
DE   AltName: Full=Lysosomal DNase II;
DE   Flags: Precursor;
GN   Name=Dnase2; Synonyms=Dnase2a, Dnl2;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=10558878; DOI=10.1006/bbrc.1999.1699;
RA   Tanuma S., Shiokawa D.;
RT   "Cloning of a cDNA encoding a rat DNase II-like acid DNase.";
RL   Biochem. Biophys. Res. Commun. 265:395-399(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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).
CC   -!- FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for
CC       double-stranded DNA. Plays a major role in the degradation of nuclear
CC       DNA in cellular apoptosis during development. Necessary for proper
CC       fetal development and for definitive erythropoiesis in fetal liver,
CC       where it degrades nuclear DNA expelled from erythroid precursor cells
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC         phosphooligonucleotide end-products.; EC=3.1.22.1;
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10558878}.
CC   -!- MISCELLANEOUS: Not required for the generation of the characteristic
CC       DNA fragmentation observed in apoptotic cells, but for the degradation
CC       of DNA from dying cells. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
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DR   EMBL; AF178975; AAF13597.1; -; mRNA.
DR   EMBL; BC091124; AAH91124.1; -; mRNA.
DR   RefSeq; NP_612548.1; NM_138539.2.
DR   AlphaFoldDB; Q9QZK8; -.
DR   SMR; Q9QZK8; -.
DR   STRING; 10116.ENSRNOP00000014887; -.
DR   GlyGen; Q9QZK8; 4 sites.
DR   PaxDb; Q9QZK8; -.
DR   Ensembl; ENSRNOT00000014887; ENSRNOP00000014887; ENSRNOG00000023830.
DR   GeneID; 171575; -.
DR   KEGG; rno:171575; -.
DR   CTD; 1777; -.
DR   RGD; 621457; Dnase2.
DR   eggNOG; KOG3825; Eukaryota.
DR   GeneTree; ENSGT00390000002634; -.
DR   HOGENOM; CLU_053867_0_0_1; -.
DR   InParanoid; Q9QZK8; -.
DR   OMA; ILYNDQK; -.
DR   OrthoDB; 605654at2759; -.
DR   PhylomeDB; Q9QZK8; -.
DR   TreeFam; TF314536; -.
DR   BRENDA; 3.1.22.1; 5301.
DR   Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR   PRO; PR:Q9QZK8; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000023830; Expressed in pancreas and 19 other tissues.
DR   Genevisible; Q9QZK8; RN.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004531; F:deoxyribonuclease II activity; IBA:GO_Central.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:RGD.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR   GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
DR   InterPro; IPR004947; DNase_II.
DR   PANTHER; PTHR10858; PTHR10858; 1.
DR   Pfam; PF03265; DNase_II; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Developmental protein; Disulfide bond; Endonuclease;
KW   Glycoprotein; Hydrolase; Lysosome; Nuclease; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..350
FT                   /note="Deoxyribonuclease-2-alpha"
FT                   /id="PRO_0000007294"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..162
FT                   /evidence="ECO:0000255"
FT   DISULFID        270..350
FT                   /evidence="ECO:0000255"
FT   DISULFID        311..330
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   350 AA;  38175 MW;  6483AF5AC13C5111 CRC64;
     MAAPSSLLLA ALLWVPAEAL SCYGDSGRPV DWFVVYKLPA NSGSGDKPWK GLMYKYMDQN
     SEGWQDGVGH IDSKDGAVGL TLQPLYQKNS SQLAFLLYND QPPKSSSAQD SSSRGHTKGV
     LLLDQEGGFW LVHSVPRFPS PASSGAYSWP PNARTYGQTL LCVSLPFSQF PGIGKQLTYT
     YPLVYDHKLE GIFAQKLPDL EEVTKGHHVL REPWNSSVIL TSRAGTTFQS FAKFGKFGDD
     LYSGWLAAAL GTNLQVQFWP NSPGILPSNC SGTHKILDVT ETGFPGPSGP TFNATEDHSK
     WCVAPEGPWV CVGDMNRNKR ETHRGGGTLC TQVPALWKAF RSLVKACKPC