ID G7NTJ7_MACFA Unreviewed; 361 AA.
AC G7NTJ7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Deoxyribonuclease-2-beta {ECO:0000256|RuleBase:RU369111};
DE EC=3.1.22.1 {ECO:0000256|RuleBase:RU369111};
DE AltName: Full=DNase II-like acid DNase {ECO:0000256|RuleBase:RU369111};
DE AltName: Full=DNase2-like acid DNase {ECO:0000256|RuleBase:RU369111};
DE AltName: Full=Deoxyribonuclease II beta {ECO:0000256|RuleBase:RU369111};
DE AltName: Full=Endonuclease DLAD {ECO:0000256|RuleBase:RU369111};
GN ORFNames=EGM_00795 {ECO:0000313|EMBL:EHH50034.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH50034.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH50034.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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:0000256|RuleBase:RU369111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC phosphooligonucleotide end-products.; EC=3.1.22.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000447,
CC ECO:0000256|RuleBase:RU369111};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|RuleBase:RU369111}.
CC -!- SIMILARITY: Belongs to the DNase II family.
CC {ECO:0000256|ARBA:ARBA00007527, ECO:0000256|RuleBase:RU369111}.
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DR EMBL; CM001276; EHH50034.1; -; Genomic_DNA.
DR AlphaFoldDB; G7NTJ7; -.
DR eggNOG; KOG3825; Eukaryota.
DR OrthoDB; 4662at2759; -.
DR Proteomes; UP000009130; Chromosome 1.
DR GO; GO:0004531; F:deoxyribonuclease II activity; IEA:UniProtKB-EC.
DR CDD; cd09190; PLDc_DNaseII_beta_1; 1.
DR CDD; cd09192; PLDc_DNaseII_beta_2; 1.
DR InterPro; IPR004947; DNase_II.
DR PANTHER; PTHR10858; DEOXYRIBONUCLEASE II; 1.
DR PANTHER; PTHR10858:SF2; DEOXYRIBONUCLEASE-2-BETA; 1.
DR Pfam; PF03265; DNase_II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|RuleBase:RU369111};
KW Glycoprotein {ECO:0000256|RuleBase:RU369111};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU369111};
KW Lysosome {ECO:0000256|RuleBase:RU369111};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU369111};
KW Signal {ECO:0000256|RuleBase:RU369111}.
SQ SEQUENCE 361 AA; 41695 MW; 48E4E5D5896F0A40 CRC64;
MKQKMMARLL RTSFALVFLG LFGVLGTATI SCRNEEGKAV DWFTFYKLPK RQNKESGETG
LEYLYLDSTT RSWRKSEQLM NTTKSVLGRT LQQLYEAYAS KSNNTAYLIY NDGVPKSVNY
SRKYGHTKGL LLWNRVQGFW LIHSIPQFPP IPEEGYDYPP TGRRNGQSGI CITFKYNQYE
AIDSQLLVCN PNIYSCSIPA TFHQELIHMP QLCTRASSSE IPGRLLTTLQ SAQGQKFLHF
AKSDSFLDDI FAAWMAQRLK THLLTETWQR KRQELPSNCS LPYHVYNIKA IKLSRHSYFS
SYQDHAKWCI SQKGTKNHWT CIGDLNRSPH QAFRSGGFIC TQNWHIYQAF QGLVLYYESC
N
//
