ID   DNSL1_PIG               Reviewed;         315 AA.
AC   Q2QDF0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 60.
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   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].
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; DQ116782; AAZ94275.1; -; mRNA.
DR   RefSeq; NP_001033721.1; NM_001038632.1.
DR   AlphaFoldDB; Q2QDF0; -.
DR   SMR; Q2QDF0; -.
DR   PeptideAtlas; Q2QDF0; -.
DR   PRIDE; Q2QDF0; -.
DR   GeneID; 654408; -.
DR   KEGG; ssc:654408; -.
DR   CTD; 1774; -.
DR   InParanoid; Q2QDF0; -.
DR   OrthoDB; 1282784at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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; 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; 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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..315
FT                   /note="Deoxyribonuclease-1-like 1"
FT                   /id="PRO_0000231033"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        198..235
FT                   /note="Essential for enzymatic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  34986 MW;  7AC9019600AD163A CRC64;
     MDSSGGFQKH TCGHALLLLL LLLAGGAEAF RICAFNAQRL TLAKVAREYV MDTLVRILAR
     CDITVLQEVV DSTGSAIPLL LRELNRFDGS GPYSSLSSPL LGRGAYKEKY AYIYRSHRTQ
     VLNFYLYPDE DDLFAREPFV GQFSLPSKVL PSLVLVPLHT TPKAVEPELK ALYEVFLDVS
     QRWQSEDVIL LGDFNADCAS LTKKRLDELV LRTQAGFHWA VADGVDTTVR ASTHCTYDRI
     VLHGERLQSL LRNAGAFDFP QSFGLTEEEA LNISDHYPVE VELSRAVHRI QPLSLATLLL
     SLLLLLLSPQ LGLAA