DNSL1_MOUSE
ID DNSL1_MOUSE Reviewed; 314 AA.
AC Q9D7J6; Q3UD56;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 138.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscles. Low
CC expression in brain and thymus. Intermediated expression in other
CC tissues. {ECO:0000269|PubMed:16107205}.
CC -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ116784; AAZ94277.1; -; mRNA.
DR EMBL; AK009174; BAB26122.1; -; mRNA.
DR EMBL; AK150242; BAE29406.1; -; mRNA.
DR EMBL; BC023246; AAH23246.1; -; mRNA.
DR RefSeq; NP_001165625.1; NM_001172154.1.
DR RefSeq; NP_081385.1; NM_027109.2.
DR AlphaFoldDB; Q9D7J6; -.
DR SMR; Q9D7J6; -.
DR STRING; 10090.ENSMUSP00000019232; -.
DR GlyGen; Q9D7J6; 3 sites.
DR PhosphoSitePlus; Q9D7J6; -.
DR MaxQB; Q9D7J6; -.
DR PaxDb; Q9D7J6; -.
DR PRIDE; Q9D7J6; -.
DR ProteomicsDB; 279749; -.
DR Antibodypedia; 31202; 170 antibodies from 24 providers.
DR DNASU; 69537; -.
DR Ensembl; ENSMUST00000019232; ENSMUSP00000019232; ENSMUSG00000019088.
DR Ensembl; ENSMUST00000239445; ENSMUSP00000159293; ENSMUSG00000019088.
DR GeneID; 69537; -.
DR KEGG; mmu:69537; -.
DR UCSC; uc009tof.2; mouse.
DR CTD; 1774; -.
DR MGI; MGI:109628; Dnase1l1.
DR VEuPathDB; HostDB:ENSMUSG00000019088; -.
DR eggNOG; ENOG502QQFT; Eukaryota.
DR GeneTree; ENSGT00950000182846; -.
DR HOGENOM; CLU_043335_1_0_1; -.
DR InParanoid; Q9D7J6; -.
DR OMA; FHWAIAD; -.
DR OrthoDB; 1282784at2759; -.
DR PhylomeDB; Q9D7J6; -.
DR TreeFam; TF329541; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 69537; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Dnase1l1; mouse.
DR PRO; PR:Q9D7J6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D7J6; protein.
DR Bgee; ENSMUSG00000019088; Expressed in quadriceps femoris and 59 other tissues.
DR ExpressionAtlas; Q9D7J6; baseline and differential.
DR Genevisible; Q9D7J6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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..37
FT /evidence="ECO:0000255"
FT CHAIN 38..314
FT /note="Deoxyribonuclease-1-like 1"
FT /id="PRO_0000007285"
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 314 AA; 35604 MW; 61888D72FF13E3F9 CRC64;
MPFGQPGFLW RVPDAHIAMR GLVMAPLLIL LVGGTEAFRI CAFNAHRLTL AKLTKESVMD
TLVQILARCD IMVLQEVVDS SQNTVPFLLQ KLKSSRSYSF LNSSLLGRST YKEKYVYIYR
SDKTQVLNFY QYNDTDDIFA REPFVAHFTL PSKTLPSVVL VPLHTTPKDV EKELNALYDV
FLDVYQRWQN ENVILLGDFN ADCASLTKKR LKSLLLRTKA GFHWVIPDGE DTTVRASTNC
TYDRIVVHGQ GCQMLLKAAA TFDFPKRFQL TEEEALRISD HYPVEVELSQ ATPLSIPPHY
LAALLLSLLP SQLD
