WAGO4_CAEEL
ID WAGO4_CAEEL Reviewed; 965 AA.
AC O62275;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Argonaute protein wago-4 {ECO:0000305};
DE AltName: Full=Worm-specific argonaute protein 4 {ECO:0000312|WormBase:F58G1.1};
GN Name=wago-4 {ECO:0000312|WormBase:F58G1.1};
GN ORFNames=F58G1.1 {ECO:0000312|WormBase:F58G1.1};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=29791857; DOI=10.1016/j.celrep.2018.04.072;
RA Xu F., Feng X., Chen X., Weng C., Yan Q., Xu T., Hong M., Guang S.;
RT "A Cytoplasmic Argonaute Protein Promotes the Inheritance of RNAi.";
RL Cell Rep. 23:2482-2494(2018).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ZNFX-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=29769721; DOI=10.1038/s41586-018-0132-0;
RA Wan G., Fields B.D., Spracklin G., Shukla A., Phillips C.M., Kennedy S.;
RT "Spatiotemporal regulation of liquid-like condensates in epigenetic
RT inheritance.";
RL Nature 557:679-683(2018).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MINA-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=30728462; DOI=10.1038/s41418-019-0291-z;
RA Sendoel A., Subasic D., Ducoli L., Keller M., Michel E., Kohler I.,
RA Singh K.D., Zheng X., Bruemmer A., Imig J., Kishore S., Wu Y., Kanitz A.,
RA Kaech A., Mittal N., Matia-Gonzalez A.M., Gerber A.P., Zavolan M.,
RA Aebersold R., Hall J., Allain F.H., Hengartner M.O.;
RT "MINA-1 and WAGO-4 are part of regulatory network coordinating germ cell
RT death and RNAi in C. elegans.";
RL Cell Death Differ. 26:2157-2178(2019).
CC -!- FUNCTION: Argonaute protein which is involved in the endogenous small
CC interfering RNA (endo-siRNA) pathway and is required for RNA-mediated
CC gene silencing (RNAi) in the germline (PubMed:17110334,
CC PubMed:29791857, PubMed:30728462). Interacts with secondary 22G-RNAs,
CC which are RNA-dependent RNA polymerase-derived endo-siRNAs, typically
CC 22 nucleotides in length with a 5'guanosine residue (PubMed:29791857).
CC Also interacts with the mRNA targets of 22G-RNAs (PubMed:29791857).
CC Associates with znfx-1 to mediate small RNA-directed transgenerational
CC epigenetic inheritance of both germline- and soma-expressed genes
CC (PubMed:29791857, PubMed:29769721). {ECO:0000269|PubMed:17110334,
CC ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857,
CC ECO:0000269|PubMed:30728462}.
CC -!- SUBUNIT: Interacts with znfx-1; the interaction promotes the
CC transmission of epigenetic information across generations
CC (PubMed:29769721). May interact with mina-1 (PubMed:30728462).
CC {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:30728462}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857,
CC ECO:0000269|PubMed:30728462}. Cytoplasmic granule
CC {ECO:0000269|PubMed:29769721}. Cytoplasm {ECO:0000269|PubMed:29791857}.
CC Note=Co-localizes with znfx-1 in P-granules in germline blastomeres
CC until the 100-cell stage (PubMed:29769721). During oocyte maturation,
CC co-localizes with znfx-1 in liquid-like condensates in the cytoplasm
CC called Z granules (PubMed:29769721). Localizes to cytoplasmic P-
CC granules in germline blastomeres. {ECO:0000269|PubMed:29769721}.
CC -!- TISSUE SPECIFICITY: Expressed in the hermaphrodite germline and in
CC oocytes (PubMed:29791857, PubMed:29769721, PubMed:30728462). Expressed
CC at a low level in the male germline (PubMed:29791857). Not expressed in
CC the soma of hermaphrodites or males (PubMed:29791857).
CC {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857,
CC ECO:0000269|PubMed:30728462}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development (PubMed:29769721,
CC PubMed:29791857, PubMed:30728462). Following fertilization, in the
CC zygotes and early embryos, it is expressed in the germline
CC (PubMed:29791857). Evenly distributed in one-cell stage embryos
CC (PubMed:29791857). In early embryos, segregates to germline precursor
CC cells and is expressed in P1-P4 germline cells (PubMed:29791857,
CC PubMed:29769721, PubMed:30728462). Also expressed in the endomesodermal
CC (EMS) precursor cell (PubMed:29791857). Exclusively expressed in Z2 and
CC Z3 larval cells at hatching (PubMed:29791857).
CC {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857,
CC ECO:0000269|PubMed:30728462}.
CC -!- MISCELLANEOUS: Members of the WAGO (worm-specific argonaute) subfamily
CC lack conserved metal-binding residues found in other argonaute proteins
CC and probably do not cleave target mRNAs directly.
CC {ECO:0000303|PubMed:17110334}.
CC -!- SIMILARITY: Belongs to the argonaute family. WAGO subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284602; CAB04524.1; -; Genomic_DNA.
DR PIR; T22933; T22933.
DR RefSeq; NP_496751.1; NM_064350.5.
DR AlphaFoldDB; O62275; -.
DR SMR; O62275; -.
DR IntAct; O62275; 1.
DR STRING; 6239.F58G1.1; -.
DR EPD; O62275; -.
DR PaxDb; O62275; -.
DR PeptideAtlas; O62275; -.
DR EnsemblMetazoa; F58G1.1.1; F58G1.1.1; WBGene00010263.
DR GeneID; 174932; -.
DR KEGG; cel:CELE_F58G1.1; -.
DR UCSC; F58G1.1; c. elegans.
DR CTD; 174932; -.
DR WormBase; F58G1.1; CE17921; WBGene00010263; wago-4.
DR eggNOG; KOG1041; Eukaryota.
DR GeneTree; ENSGT00970000196328; -.
DR HOGENOM; CLU_310185_0_0_1; -.
DR InParanoid; O62275; -.
DR OMA; AWDLNIA; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; O62275; -.
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:O62275; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010263; Expressed in adult organism and 3 other tissues.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IGI:WormBase.
DR GO; GO:0060966; P:regulation of gene silencing by RNA; IMP:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF02170; PAZ; 1.
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; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..965
FT /note="Argonaute protein wago-4"
FT /id="PRO_0000448349"
FT DOMAIN 317..428
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 594..924
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 106509 MW; F6F2F46E1B502171 CRC64;
MPALPPVYTP SGAPSSVHAP PAVPPVPVPT QPLRSEYQTS NDACIKRLEE LNIAPAAKLY
PTPTEPGKCG VEAEIQTNVF GIEMHQDSLF YQYSVNITTE LKNGKEVTFT KKGKDDFVVT
ERHDKCCAIL FRALGDYEEF FKTSDSCLIY DGQSILFSNV DLFQGFREGA VKTKYMQLDG
GEMDHKDLKS LPCIKLEVFP TKNPAVKFTR EAVARRATDS NLDSVSLAYQ QILELALTQP
CLRNTARYVV FDHGKMFFID PLGEGFEKCD VVDVGDGKQV VPGLKKTINF IEGPYGRGRS
NPSVVIDGMK VAFHKNQPIL DKLKEITTQP VEHGLKGLEK DRCAAVIKGL DCYSTYGGRE
RHHKIEGIHH EGARNARFEL NDGGSCTVAQ YFEDVYNITL RYPDTNLIVS KERGNINFYP
MELLKISSHQ RVQIPQLTSA QSQKTTKESA VLPDVRQRLI LTGKNAAQIS SDNEVLGKMG
VSVCEDPLMV KGRSIPAVKL ANAEIGANPI NVKDNKWRAN RFTRPATAPN VWAMYVVGTA
STRITLDTLK KFADEFAAMC KSKGVNMPAP ADISLIHMDA IESRLYDATK ANCTFVFIIT
DDSITTLHQR YKMIEKDTKM IVQDMKLSKA LSVINAGKRL TLENVINKTN VKLGGSNYVF
VDAKKQLDSH LIIGVGISAP PAGTKYAMEN KGVLNPNVIG YAYNAQHNQE FSGDFVLNSA
SQDTLAPIED IVMHSLNEYQ KFHDGGLPRR VIVYRTGTSE GNHGSIMAYE IPLARAAMRD
FSPDIQLVYI VVSKDHSFRF FKPDLASLAS RPQATSSTAS RHSAMPAAPK AWDLNIAPGI
LVDSIVTNPA CKQFFLNSHI TLQGTAKTPL YTVLADDAKV SMTALEDITY KLCHLHQIVG
LPTSLPTPLY VANEYAKRGR NLWNEAVALN NVPTVSGPEA DRLKELTKSI CYKASGDLTG
RRVNA
