ID   DNS2A_PIG               Reviewed;         364 AA.
AC   O62855;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 104.
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   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=Spleen;
RA   Wang C.C., Lu S.C., Chen H.L., Liao T.H.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=9647784; DOI=10.1006/bbrc.1998.8839;
RA   Shiokawa D., Tanuma S.;
RT   "Cloning of cDNAs encoding porcine and human DNase II.";
RL   Biochem. Biophys. Res. Commun. 247:864-869(1998).
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.
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.
CC   -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://www.worthington-biochem.com/HDAC/";
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DR   EMBL; AJ001387; CAA04717.1; -; mRNA.
DR   EMBL; AF060221; AAC39263.1; -; mRNA.
DR   PIR; JE0205; JE0205.
DR   RefSeq; NP_999361.1; NM_214196.1.
DR   AlphaFoldDB; O62855; -.
DR   SMR; O62855; -.
DR   STRING; 9823.ENSSSCP00000014601; -.
DR   BindingDB; O62855; -.
DR   ChEMBL; CHEMBL5894; -.
DR   PaxDb; O62855; -.
DR   PeptideAtlas; O62855; -.
DR   PRIDE; O62855; -.
DR   Ensembl; ENSSSCT00025087022; ENSSSCP00025037897; ENSSSCG00025063525.
DR   Ensembl; ENSSSCT00040017694; ENSSSCP00040007244; ENSSSCG00040013312.
DR   Ensembl; ENSSSCT00055047070; ENSSSCP00055037548; ENSSSCG00055023839.
DR   Ensembl; ENSSSCT00065030500; ENSSSCP00065012469; ENSSSCG00065022917.
DR   Ensembl; ENSSSCT00065030506; ENSSSCP00065012470; ENSSSCG00065022917.
DR   GeneID; 397398; -.
DR   KEGG; ssc:397398; -.
DR   CTD; 1777; -.
DR   eggNOG; KOG3825; Eukaryota.
DR   InParanoid; O62855; -.
DR   OrthoDB; 605654at2759; -.
DR   BRENDA; 3.1.22.1; 6170.
DR   PRO; PR:O62855; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004531; F:deoxyribonuclease II activity; IBA:GO_Central.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR   InterPro; IPR004947; DNase_II.
DR   PANTHER; PTHR10858; PTHR10858; 1.
DR   Pfam; PF03265; DNase_II; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Developmental protein; Direct protein sequencing;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lysosome; Nuclease;
KW   Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..364
FT                   /note="Deoxyribonuclease-2-alpha"
FT                   /id="PRO_0000007293"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..161
FT                   /evidence="ECO:0000255"
FT   DISULFID        269..349
FT                   /evidence="ECO:0000255"
FT   DISULFID        310..329
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   364 AA;  40183 MW;  2B690BBFEE33734D CRC64;
     MATLSPLLLA ALLWVPVGTL TCYGDSGQPV DWFVVYKLPA HSSPGDVAQS GLRYKYLDEE
     SGGWRDGAGS INSSTGALGR SLLPLYRNTS QLAFLLYNDQ PPKYRGSQHS SNRGHTKGVL
     LLDQEGGFWL IHSVPNFPPP SSSAAYSWPP SARTYGQTLI CVSFPLTQFL NISRQLTYTY
     PMVYDYKLEG DFARKFPYLE EVVKGHHVLQ EPWNSSVTLT SKAGASFQSF AKCGNFGDDL
     YSGWLAEALG SNLQVQFWQR SAGILPSNCS GVQHVLDVTQ IAFPGPAGPN FNATEDHSKW
     CVAPERPWTC VGDMNRNKRE EHRGGGTLCA QLPALWKAFK PLVKAWEPCE KENRAFSPRS
     PAKD