ID   DNSL1_RAT               Reviewed;         312 AA.
AC   Q2QDE7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
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   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=Sprague-Dawley;
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; DQ116785; AAZ94278.1; -; mRNA.
DR   RefSeq; NP_001014245.2; NM_001014223.2.
DR   AlphaFoldDB; Q2QDE7; -.
DR   SMR; Q2QDE7; -.
DR   STRING; 10116.ENSRNOP00000053125; -.
DR   GlyGen; Q2QDE7; 3 sites.
DR   PaxDb; Q2QDE7; -.
DR   Ensembl; ENSRNOT00000083203; ENSRNOP00000073157; ENSRNOG00000055641.
DR   GeneID; 363522; -.
DR   KEGG; rno:363522; -.
DR   CTD; 1774; -.
DR   RGD; 1359588; Dnase1l1.
DR   eggNOG; ENOG502QQFT; Eukaryota.
DR   GeneTree; ENSGT00950000182846; -.
DR   HOGENOM; CLU_043335_1_0_1; -.
DR   InParanoid; Q2QDE7; -.
DR   OMA; FHWAIAD; -.
DR   OrthoDB; 1282784at2759; -.
DR   PhylomeDB; Q2QDE7; -.
DR   TreeFam; TF329541; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q2QDE7; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000055641; Expressed in skeletal muscle tissue and 19 other tissues.
DR   ExpressionAtlas; Q2QDE7; baseline and differential.
DR   Genevisible; Q2QDE7; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0006308; P:DNA catabolic process; IBA:GO_Central.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IBA:GO_Central.
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; Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..312
FT                   /note="Deoxyribonuclease-1-like 1"
FT                   /id="PRO_0000231034"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        203..240
FT                   /note="Essential for enzymatic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  35182 MW;  73049972C0A8F9BD CRC64;
     MPSGQPVFPR RVPDAYIAMR GLVVASLLIL LVGGTDAFRI CAFNAHRLTL TKVIKESVMD
     TLVQILARCD IMVLQEVVDS SQNTVLFLLQ KLQSSKSYSF LNSSLLGRST YKEKYVYIYR
     SDKTQVLNFY QYNDTEDIFA REPFVAQFTL PSKILPSVVL VPLHTTPKDV EKELNALYDV
     FLDVSQRWQN ENVILLGDFN ADCASLAKKR LNSLLLRTKA GFHWVIPDGE DTTVRASTNC
     TYDRIVMHGQ GCQKLLKAAA TFDFPRRFQL TEEEALRVSD HYPVEVELNK AAQGIPPHCL
     STLLLLSLSQ LG