DI3L2_CAEEL
ID DI3L2_CAEEL Reviewed; 848 AA.
AC Q09568;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000255|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_03045};
GN Name=disl-2 {ECO:0000303|PubMed:25432023, ECO:0000312|WormBase:F48E8.6};
GN ORFNames=F48E8.6 {ECO:0000312|WormBase:F48E8.6};
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 PROTEOLYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25432023; DOI=10.7554/elife.04265;
RA Weaver B.P., Zabinsky R., Weaver Y.M., Lee E.S., Xue D., Han M.;
RT "CED-3 caspase acts with miRNAs to regulate non-apoptotic gene expression
RT dynamics for robust development in C. elegans.";
RL Elife 3:E04265-E04265(2014).
CC -!- FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs
CC polyuridylated at their 3' end and mediates their degradation.
CC Component of an exosome-independent RNA degradation pathway that
CC mediates degradation of cytoplasmic mRNAs that have been deadenylated
CC and subsequently uridylated at their 3'. {ECO:0000255|HAMAP-
CC Rule:MF_03045}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03045}.
CC Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03045}.
CC -!- PTM: Cleaved by caspase ced-3 in vitro. {ECO:0000269|PubMed:25432023}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a ced-3 and ain-1
CC double mutant background reduces the percentage of animals with
CC developmental defects including production of ectopic seam cells.
CC {ECO:0000269|PubMed:25432023}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03045}.
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DR EMBL; FO081421; CCD71518.1; -; Genomic_DNA.
DR PIR; T16409; T16409.
DR RefSeq; NP_498160.2; NM_065759.3.
DR AlphaFoldDB; Q09568; -.
DR SMR; Q09568; -.
DR BioGRID; 40977; 5.
DR STRING; 6239.F48E8.6; -.
DR EPD; Q09568; -.
DR PaxDb; Q09568; -.
DR PeptideAtlas; Q09568; -.
DR EnsemblMetazoa; F48E8.6.1; F48E8.6.1; WBGene00018612.
DR GeneID; 175748; -.
DR KEGG; cel:CELE_F48E8.6; -.
DR UCSC; F48E8.6; c. elegans.
DR CTD; 175748; -.
DR WormBase; F48E8.6; CE45000; WBGene00018612; disl-2.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_2_1; -.
DR InParanoid; Q09568; -.
DR OMA; WTRMKGP; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q09568; -.
DR PRO; PR:Q09568; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00018612; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010587; P:miRNA catabolic process; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA:InterPro.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042659; P:regulation of cell fate specification; IGI:UniProtKB.
DR GO; GO:0040034; P:regulation of development, heterochronic; IGI:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_03045; DIS3L2; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR028591; DIS3L2.
DR InterPro; IPR041093; Dis3l2_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR Pfam; PF17877; Dis3l2_C_term; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..848
FT /note="DIS3-like exonuclease 2"
FT /id="PRO_0000166425"
FT REGION 153..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT SITE 353
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
SQ SEQUENCE 848 AA; 96531 MW; B09235CB66B33B28 CRC64;
MSAVESPVIV TEPGSLKPQG LTQTATGGKF GAAATVKTTP TKAKPYVKPQ NANNLQNNFN
PRKIFTEYIS KEETDAGIED GSMFKGVLRI NPKNYQECFL DHPKGTNHPD VLVLGQDRNR
AMQGDVVAVK IKPKEDWLVN YVEYVKWWAE HKKGDRNSGK TDNNSPNKTE KRCLRNEIQD
NGVTSDEVPD SCLITIGAIV HILEKKHFRV AAGKLQLMPN SANPNVLFVA TDSRVPRILI
PKSDVDKEFF SRPKDFERFL YTAKITDWRA ESVYADGRLV KLLGMSGEID TETERIVYEH
QIDHREFSDE CLESLPITTA ENWKVPDAEF EYRRDFRSDI VFTIDPKTAR DLDDALHAKH
IDDCDGKGTP GLEIGVHIAD VTFFLKEGTE LDKWASERGN STYLSQTVIP MLPRILCEQL
CSLNPGVDRL SFSTVFKMSY EAELYDVWFG RSVIRSRVKL AYEHAQDFIE NPEKDFTCDE
LPDISDGNTP FEIKEKTLML HRIAQVLRQK REDSGALRIE LPRLKFALDE DKKPQGVSIY
EIKDSNKLVE EFMLLANMEV AKKIAENFPE HALLRNHPPP KEKMIKDVAE QCARIGFPLD
GRTSGLLSTS LRKYQGKSRL DMCIRQVISS LTIKPMQQAK YFCTFEMPLS FYHHFALNVD
HYTHFTSPIR RYPDVIVHRQ LAAALGYNER SERVPEEIQE ICTRCNDTKL ASKEASDESA
MLYFGVFIHQ TGPMKCQAVV LGVMDLSFDV LIVEYGVVKR VYVDKMKRDF NKSTEKLTIY
WPADPNAESG NREEFSSSIQ MCNVVYVILV PYKSIEVSAT IVRPSLEQRN ILKSTLKDMK
ETGSTILQ
