ERGO1_CAEEL
ID ERGO1_CAEEL Reviewed; 1121 AA.
AC O61931;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Piwi-like protein ergo-1 {ECO:0000255|RuleBase:RU361178};
DE AltName: Full=Endogenous RNA interference deficient argonaute protein 1 {ECO:0000312|WormBase:R09A1.1a};
GN Name=ergo-1 {ECO:0000312|WormBase:R09A1.1a};
GN ORFNames=R09A1.1 {ECO:0000312|WormBase:R09A1.1a};
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.
RX PubMed=17110334; DOI=10.1016/j.cell.2006.09.033;
RA Yigit E., Batista P.J., Bei Y., Pang K.M., Chen C.C., Tolia N.H.,
RA Joshua-Tor L., Mitani S., Simard M.J., Mello C.C.;
RT "Analysis of the C. elegans Argonaute family reveals that distinct
RT Argonautes act sequentially during RNAi.";
RL Cell 127:747-757(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=20133583; DOI=10.1073/pnas.0911908107;
RA Vasale J.J., Gu W., Thivierge C., Batista P.J., Claycomb J.M.,
RA Youngman E.M., Duchaine T.F., Mello C.C., Conte D. Jr.;
RT "Sequential rounds of RNA-dependent RNA transcription drive endogenous
RT small-RNA biogenesis in the ERGO-1/Argonaute pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3582-3587(2010).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=22102828; DOI=10.1371/journal.pgen.1002369;
RA Fischer S.E., Montgomery T.A., Zhang C., Fahlgren N., Breen P.C., Hwang A.,
RA Sullivan C.M., Carrington J.C., Ruvkun G.;
RT "The ERI-6/7 helicase acts at the first stage of an siRNA amplification
RT pathway that targets recent gene duplications.";
RL PLoS Genet. 7:E1002369-E1002369(2011).
RN [5] {ECO:0000305}
RP INTERACTION WITH RDE-10.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=22548001; DOI=10.1371/journal.pgen.1002617;
RA Billi A.C., Alessi A.F., Khivansara V., Han T., Freeberg M., Mitani S.,
RA Kim J.K.;
RT "The Caenorhabditis elegans HEN1 ortholog, HENN-1, methylates and
RT stabilizes select subclasses of germline small RNAs.";
RL PLoS Genet. 8:E1002617-E1002617(2012).
RN [7] {ECO:0000305}
RP INTERACTION WITH RDE-12.
RX PubMed=24684931; DOI=10.1016/j.cub.2014.03.008;
RA Shirayama M., Stanney W., Gu W., Seth M., Mello C.C.;
RT "The vasa homolog rde-12 engages target mRNA and multiple argonaute
RT proteins to promote RNAi in C. elegans.";
RL Curr. Biol. 24:845-851(2014).
CC -!- FUNCTION: Argonaute protein required for gene silencing in the
CC endogenous RNA interference (RNAi) pathway (PubMed:17110334,
CC PubMed:20133583). Involved in the 26G RNAi pathway and associates with
CC both unmethylated and methylated 26G small interfering RNAs (26G-
CC siRNAs), which are a class of 26 nucleotide siRNAs that possess a
CC guanine residue at the 5'-end (PubMed:22102828, PubMed:22548001).
CC Associated 26G-siRNAs are methylated by the methyltransferase henn-1,
CC which stabilizes the siRNAs (PubMed:22548001). Association with 26G-
CC siRNAs is required for the biogenesis of secondary 22G-siRNAs (a class
CC of 22 nucleotide siRNAs that possess a triphosphorylated guanine
CC residue at the 5'-end) (PubMed:22102828). May be involved in passenger
CC strand cleavage of target 26G-siRNAs (PubMed:22102828).
CC {ECO:0000269|PubMed:17110334, ECO:0000269|PubMed:20133583,
CC ECO:0000269|PubMed:22102828, ECO:0000269|PubMed:22548001}.
CC -!- SUBUNIT: Interacts with rde-12 (PubMed:24684931). Interacts with rde-10
CC (PubMed:22542102). {ECO:0000269|PubMed:22542102,
CC ECO:0000269|PubMed:24684931}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22548001}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the germline in hermaphrodites.
CC {ECO:0000269|PubMed:22548001}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and during larval development
CC up to larval stage L2 (PubMed:20133583). Highly expressed in embryos
CC (PubMed:22548001). {ECO:0000269|PubMed:20133583,
CC ECO:0000269|PubMed:22548001}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000255|RuleBase:RU361178, ECO:0000305|PubMed:17110334}.
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DR EMBL; BX284605; CCD62622.1; -; Genomic_DNA.
DR PIR; T33275; T33275.
DR RefSeq; NP_503362.2; NM_070961.7.
DR AlphaFoldDB; O61931; -.
DR SMR; O61931; -.
DR STRING; 6239.R09A1.1; -.
DR EPD; O61931; -.
DR PaxDb; O61931; -.
DR PeptideAtlas; O61931; -.
DR EnsemblMetazoa; R09A1.1a.1; R09A1.1a.1; WBGene00019971.
DR GeneID; 178602; -.
DR KEGG; cel:CELE_R09A1.1; -.
DR UCSC; R09A1.1; c. elegans.
DR CTD; 178602; -.
DR WormBase; R09A1.1a; CE30106; WBGene00019971; ergo-1.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_4_3_1; -.
DR InParanoid; O61931; -.
DR OMA; DRGHQDY; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; O61931; -.
DR Reactome; R-CEL-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-CEL-426486; Small interfering RNA (siRNA) biogenesis.
DR Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR PRO; PR:O61931; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019971; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; O61931; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0035198; F:miRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:WormBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0030422; P:siRNA processing; IMP:GO_Central.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR045246; Piwi_ago-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repressor; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..1121
FT /note="Piwi-like protein ergo-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434602"
FT DOMAIN 421..534
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 774..1081
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 126676 MW; CD210E43705772E6 CRC64;
MSYNNGGGGG GGGYRNDRDD RYHNNDRQNY RSSDQGRSGY NDDRRDNRYD DRRGSNNDRG
CYDQHDRRGS SNDDRRGYRG YNQGGGGYQQ QYSQDARYGS NQRNDNYGNN RGSHGGANMY
SQNGGNRGGG GGRVGGGRTA AGMSNPGDLV GGADQPIHSV SKKSLRHNAQ EFAVRPKTMV
QDKGLGQKTT LLTNHTLVQL PQEPITLHVF NIEVFINGKS SNKRELCGPR FWEILKENKP
TFGMPNQYIF NDVNMMWSTN KLRQSEGRTN NRRMNFVWKY VKQIKFGGNI EDEETMQLLS
TLIDAIATQR ARLPLAPPKY TVFKRLTYLI CEEAYEPELP DVSLCHKLRI GTDARVGVSI
AIRTNLRAGI TACFDLGHTL FTRPAYPLVR LLCDIIEHSV VLDEAFEMKY DAALRACNVS
DENLRVMTQI LTKMTLQLST ETGDYVGEDG EVIVRPAPTI RNPGRNFKFV GLGAPADRYY
FTSDGVELTV ADYYLQKYNI RLRYPNLPCV LKKAPEQCGN KHSAMPLELV SYIVVPTRYG
GFTMPDMRAD MINKTTYTAQ QRGKLLQHII AQKSLSGIEP PVSNNDDYMK KHKLVMKREP
IRVKATILPP PTLVYGDSVF HDEHHIGEWE AVTHDPPRQV LDGAVFRRKL YKSSEQPLMK
RLMGSILLIQ SPRQCRDFDY NQQGYHAIMR AIEDSGQPVL WADENKHSAV IQGELQFNQN
QHGIEVIEQF LQNIKSTIGE YERDGEVIVP IVFAVFQARA TVYSGNNNEY NDYNVLKYLA
DNKYGIHTQG ILEKSLGVVG PSPKNCALTR LMVEKVLGKV GTTHRKLERG GAHKTWTIFT
DPAKPTLVLG IDVSHPSTRD RETGNVLQKM SAATVVGNID LDVTEFRASS RIQDTGVECL
IDFSKEIDER IGEFIDHTGK RPAHIVVYRD GLSEGDFQKY LFEERVCIEE RCLKIDTSFQ
PSITYIVVTK RHHTQFFLED PSQGYESQGY NVLPGTLIED AVTTNKYYDF FLSTQIGNEG
CFRPTHYYVL HDTWTGKPDS FWPTVTHALT YNFCRSTTTV ALPAPVLYAH LAAKRAKETL
DGINTYKSVN NIYCDLESFG DLCEVNKDMN VNEKLEGMTF V
