DNS2B_MOUSE
ID DNS2B_MOUSE Reviewed; 354 AA.
AC Q9QY48; Q8C589;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Deoxyribonuclease-2-beta;
DE EC=3.1.22.1;
DE AltName: Full=DNase II-like acid DNase;
DE AltName: Full=DNase2-like acid DNase;
DE AltName: Full=Deoxyribonuclease II beta;
DE Short=DNase II beta;
DE AltName: Full=Endonuclease DLAD;
DE Flags: Precursor;
GN Name=Dnase2b; Synonyms=Dlad;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=10497274; DOI=10.1093/nar/27.20.4083;
RA Shiokawa D., Tanuma S.;
RT "DLAD, a novel mammalian divalent cation-independent endonuclease with
RT homology to DNase II.";
RL Nucleic Acids Res. 27:4083-4089(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=11700027; DOI=10.1006/bbrc.2001.5894;
RA Shiokawa D., Tanuma S.;
RT "Isolation and characterization of the DLAD/Dlad genes, which lie head-to-
RT head with the genes for urate oxidase.";
RL Biochem. Biophys. Res. Commun. 288:1119-1128(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12944971; DOI=10.1038/nature01895;
RA Nishimoto S., Kawane K., Watanabe-Fukunaga R., Fukuyama H., Ohsawa Y.,
RA Uchiyama Y., Hashida N., Ohguro N., Tano Y., Morimoto T., Fukuda Y.,
RA Nagata S.;
RT "Nuclear cataract caused by a lack of DNA degradation in the mouse eye
RT lens.";
RL Nature 424:1071-1074(2003).
CC -!- FUNCTION: Hydrolyzes DNA under acidic conditions. Does not require
CC divalent cations for activity. Participates in the degradation of
CC nuclear DNA during lens cell differentiation.
CC {ECO:0000269|PubMed:10497274, ECO:0000269|PubMed:12944971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC phosphooligonucleotide end-products.; EC=3.1.22.1;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the eye lens. Detected in
CC liver, but not in the other tissues tested.
CC {ECO:0000269|PubMed:10497274, ECO:0000269|PubMed:12944971}.
CC -!- MISCELLANEOUS: Inhibited by aurintricarboxylic acid and Zn(2+).
CC -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
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DR EMBL; AF128888; AAF05082.1; -; mRNA.
DR EMBL; AF334608; AAL34450.1; -; Genomic_DNA.
DR EMBL; AF334603; AAL34450.1; JOINED; Genomic_DNA.
DR EMBL; AF334604; AAL34450.1; JOINED; Genomic_DNA.
DR EMBL; AF334605; AAL34450.1; JOINED; Genomic_DNA.
DR EMBL; AF334606; AAL34450.1; JOINED; Genomic_DNA.
DR EMBL; AF334607; AAL34450.1; JOINED; Genomic_DNA.
DR EMBL; AK079224; BAC37579.1; -; mRNA.
DR EMBL; BC075661; AAH75661.1; -; mRNA.
DR CCDS; CCDS17904.1; -.
DR RefSeq; NP_064341.3; NM_019957.4.
DR RefSeq; XP_006501826.1; XM_006501763.3.
DR RefSeq; XP_006501827.1; XM_006501764.2.
DR RefSeq; XP_011238473.1; XM_011240171.1.
DR RefSeq; XP_011238474.1; XM_011240172.1.
DR AlphaFoldDB; Q9QY48; -.
DR SMR; Q9QY48; -.
DR STRING; 10090.ENSMUSP00000029836; -.
DR GlyGen; Q9QY48; 9 sites.
DR PhosphoSitePlus; Q9QY48; -.
DR PaxDb; Q9QY48; -.
DR PRIDE; Q9QY48; -.
DR ProteomicsDB; 279553; -.
DR Antibodypedia; 19765; 101 antibodies from 21 providers.
DR DNASU; 56629; -.
DR Ensembl; ENSMUST00000029836; ENSMUSP00000029836; ENSMUSG00000028185.
DR Ensembl; ENSMUST00000200633; ENSMUSP00000142872; ENSMUSG00000028185.
DR GeneID; 56629; -.
DR KEGG; mmu:56629; -.
DR UCSC; uc008rrn.2; mouse.
DR CTD; 58511; -.
DR MGI; MGI:1913283; Dnase2b.
DR VEuPathDB; HostDB:ENSMUSG00000028185; -.
DR eggNOG; KOG3825; Eukaryota.
DR GeneTree; ENSGT00390000002634; -.
DR HOGENOM; CLU_053867_0_0_1; -.
DR InParanoid; Q9QY48; -.
DR OMA; HMPQLCA; -.
DR OrthoDB; 605654at2759; -.
DR PhylomeDB; Q9QY48; -.
DR TreeFam; TF314536; -.
DR BRENDA; 3.1.22.1; 3474.
DR BioGRID-ORCS; 56629; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Dnase2b; mouse.
DR PRO; PR:Q9QY48; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9QY48; protein.
DR Bgee; ENSMUSG00000028185; Expressed in seminal vesicle and 15 other tissues.
DR Genevisible; Q9QY48; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004531; F:deoxyribonuclease II activity; ISO:MGI.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:MGI.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR InterPro; IPR004947; DNase_II.
DR PANTHER; PTHR10858; PTHR10858; 1.
DR Pfam; PF03265; DNase_II; 1.
PE 2: Evidence at transcript level;
KW Endonuclease; Glycoprotein; Hydrolase; Lysosome; Nuclease;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..354
FT /note="Deoxyribonuclease-2-beta"
FT /id="PRO_0000007296"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 85
FT /note="R -> K (in Ref. 3; BAC37579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40794 MW; 40A5DD6E9AD278A1 CRC64;
MTAKPLRTVL SLLFFALSGV LGTPEISCRN EYGEAVDWFI FYKLPKRTSK ASEEAGLQYL
YLDSTRQTWN KSLYLINSTR SALGRTLQHL YDTHNSTNDT AYLIYNDGVP GSVNYSRQYG
HAKGLLVWNR TQGFWLIHSV PKFPPVHGYE YPTSGRRYGQ TGICITFGYS QFEEIDFQLL
VLQPNIYSCF IPSTFHWKLI YMPRMCANSS SLKIPVRYLA ELHSAQGLNF VHFAKSSFYT
DDIFTGWIAQ KLKTHLLAQT WQKKKQELPS NCSLPYHVYN IKSIGVTSKS YFSSRQDHSK
WCVSIKGSAN RWTCIGDLNR SLHQALRGGG FICTKNHYIY QAFHKLYLRY GFCK
