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 27-MAR-2024, entry version 168. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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. DR RefSeq; XP_016856015.1; XM_017000526.1. [Q9H9G7-2] DR RefSeq; XP_016856016.1; XM_017000527.1. DR PDB; 5VM9; X-ray; 3.28 A; A/C=1-860. DR PDBsum; 5VM9; -. DR AlphaFoldDB; Q9H9G7; -. DR SMR; Q9H9G7; -. DR BioGRID; 128177; 146. DR DIP; DIP-54486N; -. DR IntAct; Q9H9G7; 84. 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; 9606-ENSP00000362287; -. DR PeptideAtlas; Q9H9G7; -. DR ProteomicsDB; 81320; -. [Q9H9G7-1] DR ProteomicsDB; 81321; -. [Q9H9G7-2] DR Pumba; Q9H9G7; -. DR Antibodypedia; 31609; 219 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 AGR; HGNC:18421; -. 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; RGRCYIH; -. DR OrthoDB; 3060088at2759; -. 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 Reactome; R-HSA-9759811; Regulation of CDH11 mRNA translation by microRNAs. DR Reactome; R-HSA-9768778; Regulation of NPAS4 mRNA translation. DR SignaLink; Q9H9G7; -. DR BioGRID-ORCS; 192669; 11 hits in 1150 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 179 other cell types or tissues. DR ExpressionAtlas; Q9H9G7; baseline and differential. 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: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:0004521; F:RNA endonuclease activity; IMP: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 non-canonical NF-kappaB signal transduction; 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; cd02846; PAZ_argonaute_like; 1. DR CDD; cd04657; Piwi_ago-like; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 2.170.260.10; paz domain; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 PANTHER; PTHR22891; EUKARYOTIC TRANSLATION INITIATION FACTOR 2C; 1. DR PANTHER; PTHR22891:SF3; PROTEIN ARGONAUTE-3; 1. 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; PAZ domain; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR PROSITE; PS50821; PAZ; 1. DR PROSITE; PS50822; PIWI; 1. DR Genevisible; Q9H9G7; HS. 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 230..349 FT /note="PAZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142" 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 //