AGO3_HUMAN
ID AGO3_HUMAN Reviewed; 860 AA.
AC Q9H9G7; B1ALI0; Q5TA55; Q9H1U6;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein argonaute-3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE Short=Argonaute3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE Short=hAgo3;
DE EC=3.1.26.n2 {ECO:0000269|PubMed:29040713};
DE AltName: Full=Argonaute RISC catalytic component 3;
DE AltName: Full=Eukaryotic translation initiation factor 2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE Short=eIF-2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE Short=eIF2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
GN Name=AGO3; Synonyms=EIF2C3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Leukocyte;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ASSOCIATION WITH MIRNA.
RX PubMed=15260970; DOI=10.1016/j.molcel.2004.07.007;
RA Meister G., Landthaler M., Patkaniowska A., Dorsett Y., Teng G., Tuschl T.;
RT "Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs.";
RL Mol. Cell 15:185-197(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16081698; DOI=10.1126/science.1115079;
RA Pillai R.S., Bhattacharyya S.N., Artus C.G., Zoller T., Cougot N.,
RA Basyuk E., Bertrand E., Filipowicz W.;
RT "Inhibition of translational initiation by Let-7 MicroRNA in human cells.";
RL Science 309:1573-1576(2005).
RN [6]
RP FUNCTION.
RX PubMed=18771919; DOI=10.1016/j.cub.2008.07.072;
RA Wu L., Fan J., Belasco J.G.;
RT "Importance of translation and nonnucleolytic ago proteins for on-target
RT RNA interference.";
RL Curr. Biol. 18:1327-1332(2008).
RN [7]
RP INTERACTION WITH EIF4B; IMP8; PRMT5 AND TNRC6B.
RX PubMed=19167051; DOI=10.1016/j.cell.2008.12.023;
RA Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P.,
RA Kremmer E., Benes V., Urlaub H., Meister G.;
RT "Importin 8 is a gene silencing factor that targets argonaute proteins to
RT distinct mRNAs.";
RL Cell 136:496-507(2009).
RN [8]
RP INTERACTION WITH APOBEC3F; APOBEC3G AND APOBEC3H.
RX PubMed=22915799; DOI=10.1128/jvi.00595-12;
RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by P
RT bodies.";
RL J. Virol. 86:11712-11724(2012).
RN [9]
RP FUNCTION, AND INTERACTION WITH EDC4.
RX PubMed=23064648; DOI=10.1038/nsmb.2400;
RA Hu Q., Tanasa B., Trabucchi M., Li W., Zhang J., Ohgi K.A., Rose D.W.,
RA Glass C.K., Rosenfeld M.G.;
RT "DICER- and AGO3-dependent generation of retinoic acid-induced DR2 Alu RNAs
RT regulates human stem cell proliferation.";
RL Nat. Struct. Mol. Biol. 19:1168-1175(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12] {ECO:0007744|PDB:5VM9}
RP X-RAY CRYSTALLOGRAPHY (3.28 ANGSTROMS) IN COMPLEX WITH GUIDE RNA, GUIDE
RP RNA-BINDING, FUNCTION, CATALYTIC ACTIVITY, METAL-BINDING SITES, MUTAGENESIS
RP OF GLU-638, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29040713; DOI=10.1093/nar/gkx916;
RA Park M.S., Phan H.D., Busch F., Hinckley S.H., Brackbill J.A.,
RA Wysocki V.H., Nakanishi K.;
RT "Human Argonaute3 has slicer activity.";
RL Nucleic Acids Res. 45:11867-11877(2017).
CC -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to
CC short RNAs such as microRNAs (miRNAs) and represses the translation of
CC mRNAs which are complementary to them. Proposed to be involved in
CC stabilization of small RNA derivates (siRNA) derived from processed RNA
CC polymerase III-transcribed Alu repeats containing a DR2 retinoic acid
CC response element (RARE) in stem cells and in the subsequent siRNA-
CC dependent degradation of a subset of RNA polymerase II-transcribed
CC coding mRNAs by recruiting a mRNA decapping complex involving EDC4.
CC Possesses RNA slicer activity but only on select RNAs bearing 5'- and
CC 3'-flanking sequences to the region of guide-target complementarity
CC (PubMed:29040713). {ECO:0000255|HAMAP-Rule:MF_03032,
CC ECO:0000269|PubMed:18771919, ECO:0000269|PubMed:23064648,
CC ECO:0000269|PubMed:29040713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=endonucleolytic cleavage to 5'-phosphomonoester.;
CC EC=3.1.26.n2; Evidence={ECO:0000269|PubMed:29040713};
CC -!- SUBUNIT: Interacts with EIF4B, IMP8, PRMT5 and TNRC6B. Interacts with
CC APOBEC3F, APOBEC3G and APOBEC3H. Interacts with EDC4.
CC {ECO:0000255|HAMAP-Rule:MF_03032, ECO:0000269|PubMed:19167051,
CC ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23064648}.
CC -!- INTERACTION:
CC Q9H9G7; Q6P2E9: EDC4; NbExp=2; IntAct=EBI-2267883, EBI-1006038;
CC Q9H9G7; O15397: IPO8; NbExp=5; IntAct=EBI-2267883, EBI-358808;
CC Q9H9G7; P53041: PPP5C; NbExp=2; IntAct=EBI-2267883, EBI-716663;
CC Q9H9G7; Q8NDV7: TNRC6A; NbExp=5; IntAct=EBI-2267883, EBI-2269715;
CC Q9H9G7; A6NIX2: WTIP; NbExp=3; IntAct=EBI-2267883, EBI-20730502;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03032, ECO:0000269|PubMed:16081698}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H9G7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9G7-2; Sequence=VSP_041084;
CC -!- PTM: Ubiquitinated on surface-exposed lysines by a SCF-like E3
CC ubiquitin-protein ligase complex containing ZSWIM8 during target-
CC directed microRNA degradation (TDMD), a process that mediates
CC degradation of microRNAs (miRNAs). Ubiquitination by the SCF-like E3
CC ubiquitin-protein ligase complex containing ZSWIM8 leads to its
CC subsequent degradation, thereby exposing miRNAs for degradation. ZSWIM8
CC recognizes and binds AGO3 when it is engaged with a TDMD target.
CC {ECO:0000250|UniProtKB:Q9UKV8}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03032}.
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DR EMBL; AK022827; BAB14262.1; -; mRNA.
DR EMBL; AL139286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025769; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS399.1; -. [Q9H9G7-1]
DR CCDS; CCDS400.1; -. [Q9H9G7-2]
DR RefSeq; NP_079128.2; NM_024852.3. [Q9H9G7-1]
DR RefSeq; NP_803171.1; NM_177422.2. [Q9H9G7-2]
DR RefSeq; XP_005270632.1; XM_005270575.3. [Q9H9G7-1]
DR RefSeq; XP_011539184.1; XM_011540882.2. [Q9H9G7-2]
DR RefSeq; XP_016856012.1; XM_017000523.1. [Q9H9G7-1]
DR RefSeq; XP_016856013.1; XM_017000524.1. [Q9H9G7-2]
DR RefSeq; XP_016856014.1; XM_017000525.1. [Q9H9G7-2]
DR RefSeq; XP_016856015.1; XM_017000526.1. [Q9H9G7-2]
DR RefSeq; XP_016856016.1; XM_017000527.1. [Q9H9G7-2]
DR PDB; 5VM9; X-ray; 3.28 A; A/C=1-860.
DR PDBsum; 5VM9; -.
DR AlphaFoldDB; Q9H9G7; -.
DR SMR; Q9H9G7; -.
DR BioGRID; 128177; 131.
DR DIP; DIP-54486N; -.
DR IntAct; Q9H9G7; 83.
DR MINT; Q9H9G7; -.
DR STRING; 9606.ENSP00000362287; -.
DR GlyGen; Q9H9G7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H9G7; -.
DR PhosphoSitePlus; Q9H9G7; -.
DR BioMuta; AGO3; -.
DR DMDM; 76803660; -.
DR EPD; Q9H9G7; -.
DR jPOST; Q9H9G7; -.
DR MassIVE; Q9H9G7; -.
DR MaxQB; Q9H9G7; -.
DR PaxDb; Q9H9G7; -.
DR PeptideAtlas; Q9H9G7; -.
DR PRIDE; Q9H9G7; -.
DR ProteomicsDB; 81320; -. [Q9H9G7-1]
DR ProteomicsDB; 81321; -. [Q9H9G7-2]
DR Antibodypedia; 31609; 176 antibodies from 30 providers.
DR DNASU; 192669; -.
DR Ensembl; ENST00000246314.10; ENSP00000246314.6; ENSG00000126070.20. [Q9H9G7-2]
DR Ensembl; ENST00000373191.9; ENSP00000362287.3; ENSG00000126070.20. [Q9H9G7-1]
DR GeneID; 192669; -.
DR KEGG; hsa:192669; -.
DR MANE-Select; ENST00000373191.9; ENSP00000362287.3; NM_024852.4; NP_079128.2.
DR UCSC; uc001bzp.4; human. [Q9H9G7-1]
DR CTD; 192669; -.
DR DisGeNET; 192669; -.
DR GeneCards; AGO3; -.
DR HGNC; HGNC:18421; AGO3.
DR HPA; ENSG00000126070; Low tissue specificity.
DR MIM; 607355; gene.
DR neXtProt; NX_Q9H9G7; -.
DR OpenTargets; ENSG00000126070; -.
DR PharmGKB; PA38329; -.
DR VEuPathDB; HostDB:ENSG00000126070; -.
DR eggNOG; KOG1041; Eukaryota.
DR GeneTree; ENSGT00940000155256; -.
DR HOGENOM; CLU_004544_4_3_1; -.
DR InParanoid; Q9H9G7; -.
DR OMA; KYIADSR; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q9H9G7; -.
DR TreeFam; TF101510; -.
DR PathwayCommons; Q9H9G7; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
DR Reactome; R-HSA-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
DR Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
DR Reactome; R-HSA-8986944; Transcriptional Regulation by MECP2.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; Q9H9G7; -.
DR BioGRID-ORCS; 192669; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; AGO3; human.
DR GenomeRNAi; 192669; -.
DR Pharos; Q9H9G7; Tbio.
DR PRO; PR:Q9H9G7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H9G7; protein.
DR Bgee; ENSG00000126070; Expressed in buccal mucosa cell and 178 other tissues.
DR ExpressionAtlas; Q9H9G7; baseline and differential.
DR Genevisible; Q9H9G7; HS.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
DR GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
DR GO; GO:0004521; F:endoribonuclease activity; IMP:UniProtKB.
DR GO; GO:0090624; F:endoribonuclease activity, cleaving miRNA-paired mRNA; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
DR GO; GO:0035196; P:miRNA processing; IMP:BHF-UCL.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0070922; P:RISC complex assembly; IDA:BHF-UCL.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03032; AGO3; 1.
DR InterPro; IPR028603; AGO3.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR032473; Argonaute_Mid_dom.
DR InterPro; IPR032474; Argonaute_N.
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; PF08699; ArgoL1; 1.
DR Pfam; PF16488; ArgoL2; 1.
DR Pfam; PF16487; ArgoMid; 1.
DR Pfam; PF16486; ArgoN; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 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 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Endonuclease;
KW Hydrolase; Metal-binding; Nuclease; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..860
FT /note="Protein argonaute-3"
FT /id="PRO_0000194061"
FT DOMAIN 236..349
FT /note="PAZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03032"
FT DOMAIN 518..819
FT /note="Piwi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03032"
FT REGION 530..567
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000305|PubMed:29040713"
FT REGION 758..805
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000305|PubMed:29040713"
FT BINDING 598
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:29040713"
FT BINDING 638
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:29040713"
FT BINDING 670
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:29040713"
FT BINDING 808
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:29040713"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041084"
FT MUTAGEN 638
FT /note="E->A: Loss of RNA slicer activity."
FT /evidence="ECO:0000269|PubMed:29040713"
FT CONFLICT 25
FT /note="T -> A (in Ref. 1; BAB14262)"
FT /evidence="ECO:0000305"
FT STRAND 27..40
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 197..210
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 213..226
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 253..263
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 309..315
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 373..386
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 465..481
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 502..512
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 529..539
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 550..554
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 558..571
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 592..600
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 611..618
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 626..633
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 643..657
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 677..692
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 702..707
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 716..719
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:5VM9"
FT TURN 726..729
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 739..742
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 744..752
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 764..771
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 777..788
FT /evidence="ECO:0007829|PDB:5VM9"
FT STRAND 792..796
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 802..812
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 815..818
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 839..845
FT /evidence="ECO:0007829|PDB:5VM9"
FT HELIX 851..853
FT /evidence="ECO:0007829|PDB:5VM9"
SQ SEQUENCE 860 AA; 97360 MW; 6FF1277995E5322E CRC64;
MEIGSAGPAG AQPLLMVPRR PGYGTMGKPI KLLANCFQVE IPKIDVYLYE VDIKPDKCPR
RVNREVVDSM VQHFKVTIFG DRRPVYDGKR SLYTANPLPV ATTGVDLDVT LPGEGGKDRP
FKVSIKFVSR VSWHLLHEVL TGRTLPEPLE LDKPISTNPV HAVDVVLRHL PSMKYTPVGR
SFFSAPEGYD HPLGGGREVW FGFHQSVRPA MWKMMLNIDV SATAFYKAQP VIQFMCEVLD
IHNIDEQPRP LTDSHRVKFT KEIKGLKVEV THCGTMRRKY RVCNVTRRPA SHQTFPLQLE
NGQTVERTVA QYFREKYTLQ LKYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIKATA RSAPDRQEEI SRLVRSANYE TDPFVQEFQF KVRDEMAHVT GRVLPAPMLQ
YGGRNRTVAT PSHGVWDMRG KQFHTGVEIK MWAIACFATQ RQCREEILKG FTDQLRKISK
DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYSGLQLII VILPGKTPVY AEVKRVGDTL
LGMATQCVQV KNVIKTSPQT LSNLCLKINV KLGGINNILV PHQRPSVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPSRYCATV RVQRPRQEII QDLASMVREL LIQFYKSTRF
KPTRIIFYRD GVSEGQFRQV LYYELLAIRE ACISLEKDYQ PGITYIVVQK RHHTRLFCAD
RTERVGRSGN IPAGTTVDTD ITHPYEFDFY LCSHAGIQGT SRPSHYHVLW DDNCFTADEL
QLLTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH VSGQSNGRDP
QALAKAVQIH QDTLRTMYFA
