ERI1_CAEEL
ID ERI1_CAEEL Reviewed; 582 AA.
AC O44406; O44407; U4PC85; U4PCK7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=3'-5' exonuclease eri-1;
DE EC=3.1.-.-;
DE AltName: Full=Enhanced RNAi protein;
GN Name=eri-1 {ECO:0000312|WormBase:T07A9.5b};
GN ORFNames=T07A9.5 {ECO:0000312|WormBase:T07A9.5b};
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, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14961122; DOI=10.1038/nature02302;
RA Kennedy S., Wang D., Ruvkun G.;
RT "A conserved siRNA-degrading RNase negatively regulates RNA interference in
RT C. elegans.";
RL Nature 427:645-649(2004).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE ERI/DICER COMPLEX, AND INTERACTION WITH
RP PIR-1.
RX PubMed=33378643; DOI=10.1016/j.molcel.2020.12.004;
RA Chaves D.A., Dai H., Li L., Moresco J.J., Oh M.E., Conte D. Jr.,
RA Yates J.R. III, Mello C.C., Gu W.;
RT "The RNA phosphatase PIR-1 regulates endogenous small RNA pathways in C.
RT elegans.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: RNA exonuclease that acts as a negative regulator of RNA
CC interference (RNAi) (PubMed:14961122). Probably acts by degrading the
CC 3'-overhangs of short interfering RNAs (siRNAs) (PubMed:14961122).
CC Component of the ERI/DICER complex which is involved in processing
CC amplified double-stranded RNA (dsRNA) intermediates during small-RNA-
CC mediated gene-silencing or RNA interference (RNAi) (Probable).
CC {ECO:0000269|PubMed:14961122, ECO:0000305|PubMed:33378643}.
CC -!- SUBUNIT: Component of the ERI/DICER complex at least composed of dcr-1,
CC rrf-3 and eri-1. {ECO:0000305|PubMed:33378643}.
CC -!- SUBUNIT: [Isoform b]: Interacts with pir-1.
CC {ECO:0000269|PubMed:33378643}.
CC -!- INTERACTION:
CC O44406; P34529: dcr-1; NbExp=4; IntAct=EBI-863689, EBI-326716;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14961122}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:T07A9.5b}; Synonyms=eri-1b
CC {ECO:0000303|PubMed:14961122};
CC IsoId=O44406-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:T07A9.5a}; Synonyms=eri-1a
CC {ECO:0000303|PubMed:14961122};
CC IsoId=O44406-2; Sequence=VSP_009699, VSP_009700;
CC Name=c {ECO:0000312|WormBase:T07A9.5c};
CC IsoId=O44406-3; Sequence=VSP_061023, VSP_009699, VSP_009700;
CC Name=d {ECO:0000312|WormBase:T07A9.5d};
CC IsoId=O44406-4; Sequence=VSP_061023;
CC -!- TISSUE SPECIFICITY: Expressed in the somatic developing gonads and in a
CC subset of neurons. In adults, it is specifically expressed in neurons
CC and in spermatheca. {ECO:0000269|PubMed:14961122}.
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DR EMBL; BX284604; CCD73976.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD73975.1; -; Genomic_DNA.
DR EMBL; BX284604; CDH93472.1; -; Genomic_DNA.
DR EMBL; BX284604; CDH93473.1; -; Genomic_DNA.
DR PIR; T32575; T32575.
DR PIR; T32576; T32576.
DR RefSeq; NP_001294645.1; NM_001307716.1.
DR RefSeq; NP_001294646.1; NM_001307717.1.
DR RefSeq; NP_741292.1; NM_171244.4. [O44406-1]
DR RefSeq; NP_741293.1; NM_171245.4. [O44406-2]
DR AlphaFoldDB; O44406; -.
DR SMR; O44406; -.
DR BioGRID; 42029; 13.
DR DIP; DIP-35116N; -.
DR IntAct; O44406; 2.
DR STRING; 6239.T07A9.5b; -.
DR EPD; O44406; -.
DR PaxDb; O44406; -.
DR PeptideAtlas; O44406; -.
DR PRIDE; O44406; -.
DR EnsemblMetazoa; T07A9.5a.1; T07A9.5a.1; WBGene00001332. [O44406-2]
DR EnsemblMetazoa; T07A9.5b.1; T07A9.5b.1; WBGene00001332. [O44406-1]
DR EnsemblMetazoa; T07A9.5c.1; T07A9.5c.1; WBGene00001332. [O44406-3]
DR EnsemblMetazoa; T07A9.5d.1; T07A9.5d.1; WBGene00001332. [O44406-4]
DR GeneID; 176868; -.
DR KEGG; cel:CELE_T07A9.5; -.
DR UCSC; T07A9.5b; c. elegans. [O44406-1]
DR CTD; 176868; -.
DR WormBase; T07A9.5a; CE17214; WBGene00001332; eri-1. [O44406-2]
DR WormBase; T07A9.5b; CE30163; WBGene00001332; eri-1. [O44406-1]
DR WormBase; T07A9.5c; CE49054; WBGene00001332; eri-1. [O44406-3]
DR WormBase; T07A9.5d; CE48636; WBGene00001332; eri-1. [O44406-4]
DR eggNOG; KOG0542; Eukaryota.
DR GeneTree; ENSGT00530000063205; -.
DR HOGENOM; CLU_034684_0_0_1; -.
DR InParanoid; O44406; -.
DR OMA; AQYYRKE; -.
DR OrthoDB; 809000at2759; -.
DR PhylomeDB; O44406; -.
DR Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O44406; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001332; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O44406; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:WormBase.
DR GO; GO:0003676; F:nucleic acid binding; ISS:WormBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:WormBase.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IMP:WormBase.
DR GO; GO:1900369; P:negative regulation of post-transcriptional gene silencing by RNA; IMP:WormBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:WormBase.
DR GO; GO:0006401; P:RNA catabolic process; IDA:WormBase.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR003034; SAP_dom.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Exonuclease; Hydrolase; Nuclease;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..582
FT /note="3'-5' exonuclease eri-1"
FT /id="PRO_0000187010"
FT DOMAIN 92..126
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 151..330
FT /note="Exonuclease"
FT REGION 27..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..206
FT /note="Missing (in isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_061023"
FT VAR_SEQ 420..448
FT /note="NDEAAFQEKMAIREYLENKQTEDFAKIAA -> VKHLHSCDIYEIFDEKTSA
FT SFTDSKCLIC (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_009699"
FT VAR_SEQ 449..582
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_009700"
SQ SEQUENCE 582 AA; 67214 MW; BFE82B9EF52DCED6 CRC64;
MSADEPSPED EKYLESLRDL LKISQEFDAS NAKQNDEPEK TAVEVESAET RTDESEKSID
IPREQQLLPS ERVEPLKSMV EPEYVKKVIR QMDTMTAEQL KQALMKIKVS TGGNKKTLRK
RVAQYYRKEN ALLNRKMEPN ADKTARFFDY LIAIDFECTC VEIIYDYPHE IIELPAVLID
VREMKIISEF RTYVRPVRNP KLSEFCMQFT KIAQETVDAA PYFREALQRL YTWMRKFNLG
QKNSRFAFVT DGPHDMWKFM QFQCLLSNIR MPHMFRSFIN IKKTFKEKFN GLIKGNGKSG
IENMLERLDL SFVGNKHSGL DDATNIAAIA IQMMKLKIEL RINQKCSYKE NQRSAARKDE
ERELEDAANV DLTSVDISRR DFQLWMRRLP LKLSSVTRRE FINEEYLDCD SCDDLTDDKN
DEAAFQEKMA IREYLENKQT EDFAKIAAER GIFKIGEIKS YQTARPIIED DDVDVESEEE
DYGTEFEMLE VVERMPPVSS TLHTEVDLDA VWERDGGSDS ERENLSNAPS LHEFPSSSTS
SPHATSEHVT SSSPLHIDDD VDRVLNAPPK NSLASSSNRS SF
