NUC1_CAEEL
ID NUC1_CAEEL Reviewed; 375 AA.
AC Q17778;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Deoxyribonuclease-2;
DE EC=3.1.22.1;
DE AltName: Full=Deoxyribonuclease II;
DE Short=DNase II;
DE Flags: Precursor;
GN Name=nuc-1; ORFNames=C07B5.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=10903446; DOI=10.1016/s0378-1119(00)00213-4;
RA Lyon C.J., Evans C.J., Bill B.R., Otsuka A.J., Aguilera R.J.;
RT "The C. elegans apoptotic nuclease NUC-1 is related in sequence and
RT activity to mammalian DNase II.";
RL Gene 252:147-154(2000).
CC -!- FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for
CC double-stranded DNA. Implicated in apoptosis.
CC {ECO:0000269|PubMed:10903446}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC phosphooligonucleotide end-products.; EC=3.1.22.1;
CC -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
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DR EMBL; Z46266; CAA86412.1; -; Genomic_DNA.
DR PIR; T19038; T19038.
DR RefSeq; NP_509604.1; NM_077203.5.
DR AlphaFoldDB; Q17778; -.
DR SMR; Q17778; -.
DR BioGRID; 46090; 6.
DR STRING; 6239.C07B5.5; -.
DR EPD; Q17778; -.
DR PaxDb; Q17778; -.
DR PeptideAtlas; Q17778; -.
DR EnsemblMetazoa; C07B5.5.1; C07B5.5.1; WBGene00003828.
DR GeneID; 181174; -.
DR KEGG; cel:CELE_C07B5.5; -.
DR UCSC; C07B5.5; c. elegans.
DR CTD; 181174; -.
DR WormBase; C07B5.5; CE00895; WBGene00003828; nuc-1.
DR eggNOG; KOG3825; Eukaryota.
DR GeneTree; ENSGT00390000002634; -.
DR HOGENOM; CLU_053867_0_0_1; -.
DR InParanoid; Q17778; -.
DR OMA; MLYSDQP; -.
DR OrthoDB; 605654at2759; -.
DR PhylomeDB; Q17778; -.
DR BRENDA; 3.1.22.1; 1045.
DR PRO; PR:Q17778; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003828; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0005764; C:lysosome; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; TAS:WormBase.
DR GO; GO:0004531; F:deoxyribonuclease II activity; IMP:WormBase.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IMP:WormBase.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IMP:WormBase.
DR GO; GO:0002785; P:negative regulation of antimicrobial peptide production; IMP:WormBase.
DR InterPro; IPR004947; DNase_II.
DR PANTHER; PTHR10858; PTHR10858; 1.
DR Pfam; PF03265; DNase_II; 1.
PE 3: Inferred from homology;
KW Apoptosis; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..375
FT /note="Deoxyribonuclease-2"
FT /id="PRO_0000007299"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 375 AA; 41541 MW; E051189832919D3F CRC64;
MGLSPAAVLI FLLLGVSQTY AAFSCKDQSG NDVDWFAVYK MPIEKDDGSV TGLAGGVAWY
YVDVNKKGTL TPSAKTLDDN DQAIAYTLQQ YYDKQNDKTI FHVMYNDEPW GSKSTSGIKL
EEILSNRVYS NYTHEDDSTS TAFGHTKGTI FFDGTSGVWL VHSVPLFPNP TKYEYPVSGH
DYGQTMLCMT FKYAQLKSIG TQLFFNRPNI YSSNLPTNMA ADNADLAKAI AGQYQKGQPF
QSVIELETMA GYSFTNFAKS KEFNADLYDT LVAPTLKTDL VVETWRRGSE IPLDCKLTYH
ANDALSIHVG STTAFSYTKD HSKMAHSADM TKPWVCIGDI NRMTSQYVRG GGTTCISSSF
LWKAYSVIAT QNNCA
