DNSL2_MOUSE
ID DNSL2_MOUSE Reviewed; 278 AA.
AC Q9D1G0; Q3KQI2; Q9D645;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Deoxyribonuclease-1-like 2;
DE EC=3.1.21.-;
DE AltName: Full=Deoxyribonuclease I-like 2;
DE Short=DNase I-like 2;
DE Flags: Precursor;
GN Name=Dnase1l2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 -!- FUNCTION: Divalent cation-dependent acid DNA endonuclease involved in
CC the breakdown of the nucleus during corneocyte formation of epidermal
CC keratinocytes. May play an immune role by eliminating harmful DNA
CC released into the extracellular environment by damaged epidermal cells
CC (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
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DR EMBL; AK003619; BAB22893.1; -; mRNA.
DR EMBL; AK014633; BAB29476.1; -; mRNA.
DR EMBL; BC106188; AAI06189.1; -; mRNA.
DR CCDS; CCDS37489.1; -.
DR RefSeq; NP_079994.2; NM_025718.3.
DR AlphaFoldDB; Q9D1G0; -.
DR SMR; Q9D1G0; -.
DR BioGRID; 211658; 1.
DR IntAct; Q9D1G0; 1.
DR STRING; 10090.ENSMUSP00000085862; -.
DR iPTMnet; Q9D1G0; -.
DR PhosphoSitePlus; Q9D1G0; -.
DR PaxDb; Q9D1G0; -.
DR PRIDE; Q9D1G0; -.
DR ProteomicsDB; 279554; -.
DR Antibodypedia; 51835; 61 antibodies from 13 providers.
DR DNASU; 66705; -.
DR Ensembl; ENSMUST00000088506; ENSMUSP00000085862; ENSMUSG00000024136.
DR Ensembl; ENSMUST00000119932; ENSMUSP00000113508; ENSMUSG00000024136.
DR GeneID; 66705; -.
DR KEGG; mmu:66705; -.
DR UCSC; uc008avw.1; mouse.
DR CTD; 1775; -.
DR MGI; MGI:1913955; Dnase1l2.
DR VEuPathDB; HostDB:ENSMUSG00000024136; -.
DR eggNOG; ENOG502SGB6; Eukaryota.
DR GeneTree; ENSGT00950000182846; -.
DR HOGENOM; CLU_043335_2_1_1; -.
DR InParanoid; Q9D1G0; -.
DR OMA; CNYVRAQ; -.
DR OrthoDB; 1282784at2759; -.
DR PhylomeDB; Q9D1G0; -.
DR TreeFam; TF329541; -.
DR BioGRID-ORCS; 66705; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Dnase1l2; mouse.
DR PRO; PR:Q9D1G0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D1G0; protein.
DR Bgee; ENSMUSG00000024136; Expressed in lip and 92 other tissues.
DR ExpressionAtlas; Q9D1G0; baseline and differential.
DR Genevisible; Q9D1G0; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004536; F:deoxyribonuclease activity; IC:MGI.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003335; P:corneocyte development; IMP:MGI.
DR GO; GO:0006308; P:DNA catabolic process; IMP:MGI.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IBA:GO_Central.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
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 Calcium; Cytoplasm; Disulfide bond; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..278
FT /note="Deoxyribonuclease-1-like 2"
FT /id="PRO_0000007287"
FT ACT_SITE 99
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /evidence="ECO:0000250"
FT DISULFID 189..225
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000250"
FT CONFLICT 183
FT /note="G -> C (in Ref. 1; BAB29476)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> H (in Ref. 1; BAB29476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 31138 MW; 71FEA07A1BF940E8 CRC64;
MGWPWAPLTA VWALGVMGAT ALRIGAFNVQ SFGDNKVSDP DCGSVIAQIL AGYDIALVQE
VRDPDLSAVS LLMEQINRVS KHEYGFVSSK PLGRDQYKEM YLFVYRKDVA SVVSTYQYPD
PEDAFSREPF VVKFSVPSCA TKELVLIPLH AAPHQAVAEI DALYDVYLDV IDKWNTDDML
FLGDFNADCK YVKAHDWPSI RLRSSEVFKW LIPDSADTTV GNSDCAYDRI VVSGAHLRRS
LKPHSASVHN FQEEFDLDQT QALAISDHFP VEVTFKTH
