ID   DNSL1_CHLAE             Reviewed;         302 AA.
AC   Q2QDF1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Deoxyribonuclease-1-like 1;
DE            EC=3.1.21.-;
DE   AltName: Full=DNase X;
DE   AltName: Full=Deoxyribonuclease I-like 1;
DE            Short=DNase I-like 1;
DE   Flags: Precursor;
GN   Name=DNASE1L1;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16107205; DOI=10.1042/bj20051114;
RA   Shiokawa D., Shika Y., Saito K., Yamazaki K., Tanuma S.;
RT   "Physical and biochemical properties of mammalian DNase X proteins: non-AUG
RT   translation initiation of porcine and bovine mRNAs for DNase X.";
RL   Biochem. J. 392:511-517(2005).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
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DR   EMBL; DQ116781; AAZ94274.1; -; mRNA.
DR   AlphaFoldDB; Q2QDF1; -.
DR   SMR; Q2QDF1; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004536; F:deoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
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   Disulfide bond; Endonuclease; Endoplasmic reticulum; Glycoprotein;
KW   Hydrolase; Nuclease; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..302
FT                   /note="Deoxyribonuclease-1-like 1"
FT                   /id="PRO_0000231031"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        187..224
FT                   /note="Essential for enzymatic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  33946 MW;  54A5F946DB492C46 CRC64;
     MHYPTALLFL ILVNGAQAFR ICAFNAQRLT LAKVAREQVM DTLVRILARC DIMVLQEVVD
     SSGSAIPLLL RELNRFDASG PYSTLSSPQL GRTTYVETYV YFYRSHKTQV LSSYVYNDED
     DVFAREPFVA QFSLPSDVLP SLVLVPLHTT PKAVEKELNA LYDVFLEVSQ HWQSKDVILL
     GDFNADCASL TKKRLDKLEL RTEPGFHWVI ADGEDTTVRA STHCAYDRIV LHGERCRSLL
     HTAAAFDFPT TFQLTEEEAL NISDHYPVEV ELKLSQAHSV QPLSLTVLLL LSLLSPQLCP
     AT