RDE10_CAEEL
ID RDE10_CAEEL Reviewed; 627 AA.
AC Q9N3S2;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=RNA interference defective protein 10 {ECO:0000312|WormBase:Y47G6A.4};
GN Name=rde-10 {ECO:0000312|WormBase:Y47G6A.4};
GN ORFNames=Y47G6A.4 {ECO:0000312|WormBase:Y47G6A.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RDE-11 AND ERGO-1, AND DISRUPTION PHENOTYPE.
RX PubMed=22542102; DOI=10.1016/j.cub.2012.04.011;
RA Zhang C., Montgomery T.A., Fischer S.E., Garcia S.M., Riedel C.G.,
RA Fahlgren N., Sullivan C.M., Carrington J.C., Ruvkun G.;
RT "The Caenorhabditis elegans RDE-10/RDE-11 complex regulates RNAi by
RT promoting secondary siRNA amplification.";
RL Curr. Biol. 22:881-890(2012).
RN [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH RDE-11.
RX PubMed=22508728; DOI=10.1101/gad.180679.111;
RA Yang H., Zhang Y., Vallandingham J., Li H., Li H., Florens L., Mak H.Y.;
RT "The RDE-10/RDE-11 complex triggers RNAi-induced mRNA degradation by
RT association with target mRNA in C. elegans.";
RL Genes Dev. 26:846-856(2012).
CC -!- FUNCTION: In complex with rde-11, required in the endogenous and
CC exogenous siRNA pathway for biogenesis and accumulation of secondary
CC small interfering RNA (siRNA) intermediates, such as 22G-siRNAs derived
CC from ergo-1 targets. {ECO:0000269|PubMed:22508728,
CC ECO:0000269|PubMed:22542102}.
CC -!- SUBUNIT: Interacts with rde-11 (via RING-type zinc finger domain)
CC (PubMed:22508728, PubMed:22542102). Interacts with ergo-1
CC (PubMed:22542102). {ECO:0000269|PubMed:22508728,
CC ECO:0000269|PubMed:22542102}.
CC -!- DISRUPTION PHENOTYPE: Insensitive to RNAi-mediated gene silencing.
CC {ECO:0000269|PubMed:22542102}.
CC -!- SIMILARITY: Belongs to the maelstrom family. {ECO:0000305}.
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DR EMBL; BX284601; CCD72548.1; -; Genomic_DNA.
DR RefSeq; NP_491178.1; NM_058777.6.
DR AlphaFoldDB; Q9N3S2; -.
DR ComplexPortal; CPX-1000; Rde-10/Rde-11 complex.
DR STRING; 6239.Y47G6A.4; -.
DR EPD; Q9N3S2; -.
DR PaxDb; Q9N3S2; -.
DR PeptideAtlas; Q9N3S2; -.
DR EnsemblMetazoa; Y47G6A.4.1; Y47G6A.4.1; WBGene00021634.
DR GeneID; 171923; -.
DR KEGG; cel:CELE_Y47G6A.4; -.
DR UCSC; Y47G6A.4; c. elegans.
DR CTD; 171923; -.
DR WormBase; Y47G6A.4; CE24371; WBGene00021634; rde-10.
DR eggNOG; ENOG502QQDI; Eukaryota.
DR HOGENOM; CLU_436308_0_0_1; -.
DR InParanoid; Q9N3S2; -.
DR OrthoDB; 1411703at2759; -.
DR PRO; PR:Q9N3S2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021634; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0031332; C:RNAi effector complex; IC:ComplexPortal.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR024970; Maelstrom.
DR Pfam; PF13017; Maelstrom; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repressor; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..627
FT /note="RNA interference defective protein 10"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434604"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 72155 MW; 837CA8E90358A644 CRC64;
MSNHRSNFRD YQREGIRANN AGTSGDAVRQ NGNPISVAKH VDGKKSVYML FLRQIGQKKF
LTEQGHRYNQ NDQADKDIMT RYYHGMCPDL KQKFEREVAE HNGNRGLVIK TKHQRAQRNR
EMRHRNPDEF QQLRRAHLET LSQTPSVIAL PRDINHVLHI TEDLDAFCLA NRKKAKRIMT
SYIAQRSDDP GNPLLCEDYT MQIVSVFPVA YAFKPSINKL SSYPAEISVT TFNLKNGIIQ
NESRFVKFDA AWFYPDADDI GHEELSRKAM ADELGISPNG PADGCEPYEV FEWLQHLLKQ
HPKSPILCDR AQFNFVYYGI KTLATYTGIN AITFFQEVII PSILSIQDFT SVILEKAPTD
VPRVWRDVDI CNQFQYHFLI PRTELNLFCS FHENKPSPTK YNCVKAHNAR LLDNFFTVIK
GNRLQGFVIS PPVHEICIQD GSDTSLPQTI LARTISRNDA EVYAARQRDT DEQYDVHQEG
PSNHDQYEFA SEPLDFEEDS DEENYNEQLD VPYSYNDHFI SSSSVREPEH PSARSRDVAP
NVQQESVVVP APRRLSPQRA PRPSQNSPNA YSERKSFSAF PSEDPSEDYE TPIISHIMNR
NEADQYFNIL DSVKPGQKYK IIKFDDF