ID A0A1S2ZUL7_ERIEU Unreviewed; 335 AA.
AC A0A1S2ZUL7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=DNASE2B {ECO:0000313|RefSeq:XP_007524792.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007524792.1};
RN [1] {ECO:0000313|RefSeq:XP_007524792.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_007524792.1; XM_007524730.2.
DR AlphaFoldDB; A0A1S2ZUL7; -.
DR CTD; 58511; -.
DR eggNOG; KOG3825; Eukaryota.
DR OrthoDB; 4662at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Signal {ECO:0000256|RuleBase:RU369111, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..335
FT /note="Deoxyribonuclease-2-beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010160818"
SQ SEQUENCE 335 AA; 38504 MW; 8167F2D214997889 CRC64;
MSARFLRATL ALLALNCFGT PVATAISCRN EEGEAVDWFT FYKLPKRQDK EKRDIGLEYL
YLDSTTRRWK RSKQLMNSTQ SVLGKTLEQL YEAYASKGNN TAYVIYNDGV PGAVNYSRKY
GHTKTPEEGY GYPPTGTRNG QTGICVTFKY NQYEAIDSQL LICNPNIYSC FIPTTFNREL
IYIRQLCTGS TSREIPGQHL TTLQSAQGQK FLHFAKSDSY LEDIFAAWMA QRLKTHLLTE
TWQRKRQELP SNCSLPYHVY NVKAIKLSGR SYFSSYQDHA KWCVSRKGTK NHWTCIGDLN
RSPHQAFRSG GFICTQNQHI YQAFQGLVLY YENCD
//
