ID G5C929_HETGA Unreviewed; 357 AA.
AC G5C929;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=GW7_02235 {ECO:0000313|EMBL:EHB18040.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB18040.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB18040.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(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; JH173940; EHB18040.1; -; Genomic_DNA.
DR AlphaFoldDB; G5C929; -.
DR STRING; 10181.G5C929; -.
DR eggNOG; KOG3825; Eukaryota.
DR InParanoid; G5C929; -.
DR OMA; HMPQLCA; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0004531; F:deoxyribonuclease II activity; IEA:UniProtKB-EC.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Signal {ECO:0000256|RuleBase:RU369111, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..357
FT /note="Deoxyribonuclease-2-beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003475336"
SQ SEQUENCE 357 AA; 41051 MW; DFC2EE141CA92A7A CRC64;
MTARLQRTTI GLVFFGLFGV LEAATIACRN EDGDAVDWFI FYKLPKRQDK ESRETGLEYL
YLDSTIGSWR RSEQLINATK SALGRTLQQL YEAYASKSNN TAYLLYNDGA PKSVGYNRNF
GHTKGLLLWN KIQGFWLIHS IPQFPPIPEE GYDYPSTGRR NGQSGICITF KYNQYEIIDS
QLLVCNPNIY SCSIPITFHQ ELIHMPQLCA SFSSSKIPVR HLTTLQSAQG QSFLHFAKSD
SFPNDILAGW MAQQLKTHLL SETWQRKRQE LPSNCSLPYH VYNIKAIKIS RQSYFSSYQD
HAKWCISQKG TKDRWTCIGD LNRSPHQAFR SGGFICTQNR NTYQAFQKLV LYYQDCD
//
