ID   DNS2A_BOVIN             Reviewed;         365 AA.
AC   P56541; O46614; Q17QD1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 98.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal lung;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 90-365.
RC   TISSUE=Spleen;
RA   Krieser R.J., Eastman A.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; BC118429; AAI18430.1; -; mRNA.
DR   EMBL; AF047017; AAC77367.1; -; mRNA.
DR   RefSeq; NP_001068595.1; NM_001075127.2.
DR   AlphaFoldDB; P56541; -.
DR   SMR; P56541; -.
DR   STRING; 9913.ENSBTAP00000007993; -.
DR   PaxDb; P56541; -.
DR   PRIDE; P56541; -.
DR   GeneID; 282218; -.
DR   KEGG; bta:282218; -.
DR   CTD; 1777; -.
DR   eggNOG; KOG3825; Eukaryota.
DR   InParanoid; P56541; -.
DR   OrthoDB; 605654at2759; -.
DR   BRENDA; 3.1.22.1; 908.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004531; F:deoxyribonuclease II activity; IEA:UniProtKB-EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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..365
FT                   /note="Deoxyribonuclease-2-alpha"
FT                   /id="PRO_0000145100"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..162
FT                   /evidence="ECO:0000255"
FT   DISULFID        270..348
FT                   /evidence="ECO:0000255"
FT   DISULFID        311..330
FT                   /evidence="ECO:0000255"
FT   CONFLICT        146
FT                   /note="V -> A (in Ref. 2; AAC77367)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="A -> G (in Ref. 2; AAC77367)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="S -> A (in Ref. 2; AAC77367)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   365 AA;  40282 MW;  B9B6219E51448622 CRC64;
     MATLSSLLLT ALLWVPVGTL TCYGDSGQPV DWFVVYKLPA HTGSGDATQN GLRYKYFDEH
     SEDWSDGVGF INSTTGAVGR SLLPLYRNNN SQLAFVLYND QPPKSSESKD SSSRGHTKGV
     LLLDQEGGFW LIHSVPNFPP RASSAVYSWP PGAQKYGQTL ICVSFPLTQF LDISKQLTYT
     YPLVYDHRLE GDFAQKFPYL EEVVKGHHVR QGPWNSSVTL TSKKGATFQS FAKFGNFGDD
     LYSGWLSEAL GSTLQVQFWQ RSSGILPSNC SGAQHVFDVT QTAFPGPAGP AFNATEDHSK
     WCVTPKGPWA CVGDMNRNQR EEHRGGGTLC AQMLWKAFKP LVKAWEPCEK KSRAYSLGSP
     AGLWT