AGO1_HUMAN
ID AGO1_HUMAN Reviewed; 857 AA.
AC Q9UL18; Q5TA57; Q6P4S0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Protein argonaute-1;
DE Short=Argonaute1;
DE Short=hAgo1;
DE AltName: Full=Argonaute RISC catalytic component 1;
DE AltName: Full=Eukaryotic translation initiation factor 2C 1;
DE Short=eIF-2C 1;
DE Short=eIF2C 1;
DE AltName: Full=Putative RNA-binding protein Q99;
GN Name=AGO1; Synonyms=EIF2C1;
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 [MRNA].
RX PubMed=10534406; DOI=10.1006/geno.1999.5951;
RA Koesters R., Adams V., Betts D., Moos R., Schmid M., Siermann A.,
RA Hassam S., Weitz S., Lichter P., Heitz P.U., von Knebel Doeberitz M.,
RA Briner J.;
RT "Human eukaryotic initiation factor EIF2C1 gene: cDNA sequence, genomic
RT organization, localization to chromosomal bands 1p34-p35, and expression.";
RL Genomics 61:210-218(1999).
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].
RC TISSUE=Placenta;
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 FUNCTION, INTERACTION WITH DICER1; MOV10; PRMT5 AND TNRC6B, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16289642; DOI=10.1016/j.cub.2005.10.048;
RA Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H., Luehrmann R.,
RA Tuschl T.;
RT "Identification of novel argonaute-associated proteins.";
RL Curr. Biol. 15:2149-2155(2005).
RN [6]
RP FUNCTION.
RX PubMed=16936728; DOI=10.1038/nsmb1140;
RA Janowski B.A., Huffman K.E., Schwartz J.C., Ram R., Nordsell R.,
RA Shames D.S., Minna J.D., Corey D.R.;
RT "Involvement of AGO1 and AGO2 in mammalian transcriptional silencing.";
RL Nat. Struct. Mol. Biol. 13:787-792(2006).
RN [7]
RP INTERACTION WITH DDX6 AND AGO2.
RX PubMed=16756390; DOI=10.1371/journal.pbio.0040210;
RA Chu C.-Y., Rana T.M.;
RT "Translation repression in human cells by microRNA-induced gene silencing
RT requires RCK/p54.";
RL PLoS Biol. 4:E210-E210(2006).
RN [8]
RP ASSOCIATION WITH POLYSOMES AND MNRP, AND INTERACTION WITH DDB1; DDX5;
RP DHX30; DHX36; DDX47; ELAVL1; HNRNPF; IGF2BP1; ILF3; MATR3; PABPC1; RBM4;
RP SART3; UPF1 AND YBX1.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [9]
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 [10]
RP INTERACTION WITH IMP8.
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 [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LIMD1; WTIP AND AJUBA.
RX PubMed=20616046; DOI=10.1073/pnas.0914987107;
RA James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
RA Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
RA Longmore G.D., Bushell M., Sharp T.V.;
RT "LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-
RT mediated gene silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 225-369, AND RNA-BINDING.
RX PubMed=15152257; DOI=10.1038/nature02519;
RA Ma J.-B., Ye K., Patel D.J.;
RT "Structural basis for overhang-specific small interfering RNA recognition
RT by the PAZ domain.";
RL Nature 429:318-322(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH RNA, RNA-BINDING,
RP MUTAGENESIS OF PRO-670; PRO-675 AND ARG-805, AND LACK OF CATALYTIC
RP ACTIVITY.
RX PubMed=23809764; DOI=10.1016/j.celrep.2013.06.010;
RA Nakanishi K., Ascano M., Gogakos T., Ishibe-Murakami S., Serganov A.A.,
RA Briskin D., Morozov P., Tuschl T., Patel D.J.;
RT "Eukaryote-specific insertion elements control human ARGONAUTE slicer
RT activity.";
RL Cell Rep. 3:1893-1900(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH RNA, LACK OF
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-674 AND ARG-805.
RX PubMed=23746446; DOI=10.1016/j.celrep.2013.05.033;
RA Faehnle C.R., Elkayam E., Haase A.D., Hannon G.J., Joshua-Tor L.;
RT "The making of a slicer: activation of human Argonaute-1.";
RL Cell Rep. 3:1901-1909(2013).
RN [17]
RP VARIANT SER-199.
RX PubMed=25003005; DOI=10.4161/rdis.26144;
RA Tuzovic L., Yu L., Zeng W., Li X., Lu H., Lu H.M., Gonzalez K.D.,
RA Chung W.K.;
RT "A human de novo mutation in MYH10 phenocopies the loss of function
RT mutation in mice.";
RL Rare Dis. 1:E26144-E26144(2013).
CC -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to
CC short RNAs such as microRNAs (miRNAs) or short interfering RNAs
CC (siRNAs), and represses the translation of mRNAs which are
CC complementary to them. Lacks endonuclease activity and does not appear
CC to cleave target mRNAs. Also required for transcriptional gene
CC silencing (TGS) of promoter regions which are complementary to bound
CC short antigene RNAs (agRNAs). {ECO:0000269|PubMed:16289642,
CC ECO:0000269|PubMed:16936728, ECO:0000269|PubMed:18771919}.
CC -!- SUBUNIT: Interacts with DDB1, DDX5, DDX6, DHX30, DHX36, DDX47, DICER1,
CC AGO2, ELAVL1, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10, PABPC1, PRMT5,
CC RBM4, SART3, TNRC6B, UPF1 and YBX1. Associates with polysomes and
CC messenger ribonucleoproteins (mNRPs). Interacts with LIMD1, WTIP and
CC AJUBA. Interacts with APOBEC3F, APOBEC3G and APOBEC3H.
CC {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16756390,
CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:19167051,
CC ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22915799,
CC ECO:0000269|PubMed:23746446, ECO:0000269|PubMed:23809764}.
CC -!- INTERACTION:
CC Q9UL18; Q9UKV8: AGO2; NbExp=3; IntAct=EBI-527363, EBI-528269;
CC Q9UL18; Q9UPY3: DICER1; NbExp=5; IntAct=EBI-527363, EBI-395506;
CC Q9UL18; P08238: HSP90AB1; NbExp=3; IntAct=EBI-527363, EBI-352572;
CC Q9UL18; O15397: IPO8; NbExp=2; IntAct=EBI-527363, EBI-358808;
CC Q9UL18; Q9UGP4: LIMD1; NbExp=3; IntAct=EBI-527363, EBI-2652871;
CC Q9UL18; P53041: PPP5C; NbExp=2; IntAct=EBI-527363, EBI-716663;
CC Q9UL18; P04156: PRNP; NbExp=2; IntAct=EBI-527363, EBI-977302;
CC Q9UL18; Q8NDV7: TNRC6A; NbExp=5; IntAct=EBI-527363, EBI-2269715;
CC Q9UL18; Q9UPQ9-2: TNRC6B; NbExp=4; IntAct=EBI-527363, EBI-6514011;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16289642,
CC ECO:0000269|PubMed:20616046}.
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 AGO1 when it is engaged with a TDMD target.
CC {ECO:0000250|UniProtKB:Q9UKV8}.
CC -!- MISCELLANEOUS: Lacks RNA cleavage activity due to the absence of the
CC conserved His at position 805, but also because it binds the RNA in a
CC subtly different manner that precludes efficient cleavage.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
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DR EMBL; AF093097; AAF00068.1; -; mRNA.
DR EMBL; AL139286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063275; AAH63275.1; -; mRNA.
DR CCDS; CCDS398.1; -.
DR RefSeq; NP_001304051.1; NM_001317122.1.
DR RefSeq; NP_001304052.1; NM_001317123.1.
DR RefSeq; NP_036331.1; NM_012199.4.
DR PDB; 1SI2; X-ray; 2.60 A; A=225-369.
DR PDB; 1SI3; X-ray; 2.60 A; A=225-369.
DR PDB; 4KRE; X-ray; 1.75 A; A=1-857.
DR PDB; 4KRF; X-ray; 2.10 A; A=1-857.
DR PDB; 4KXT; X-ray; 2.29 A; A=1-857.
DR PDB; 5W6V; X-ray; 2.83 A; A=1-857.
DR PDBsum; 1SI2; -.
DR PDBsum; 1SI3; -.
DR PDBsum; 4KRE; -.
DR PDBsum; 4KRF; -.
DR PDBsum; 4KXT; -.
DR PDBsum; 5W6V; -.
DR AlphaFoldDB; Q9UL18; -.
DR SMR; Q9UL18; -.
DR BioGRID; 117726; 153.
DR DIP; DIP-29193N; -.
DR IntAct; Q9UL18; 192.
DR MINT; Q9UL18; -.
DR STRING; 9606.ENSP00000362300; -.
DR GlyGen; Q9UL18; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UL18; -.
DR PhosphoSitePlus; Q9UL18; -.
DR BioMuta; AGO1; -.
DR DMDM; 88984241; -.
DR EPD; Q9UL18; -.
DR jPOST; Q9UL18; -.
DR MassIVE; Q9UL18; -.
DR MaxQB; Q9UL18; -.
DR PaxDb; Q9UL18; -.
DR PeptideAtlas; Q9UL18; -.
DR PRIDE; Q9UL18; -.
DR ProteomicsDB; 84931; -.
DR Antibodypedia; 31600; 299 antibodies from 39 providers.
DR DNASU; 26523; -.
DR Ensembl; ENST00000373204.6; ENSP00000362300.4; ENSG00000092847.13.
DR Ensembl; ENST00000674304.1; ENSP00000501450.1; ENSG00000092847.13.
DR GeneID; 26523; -.
DR KEGG; hsa:26523; -.
DR MANE-Select; ENST00000373204.6; ENSP00000362300.4; NM_012199.5; NP_036331.1.
DR UCSC; uc001bzl.4; human.
DR CTD; 26523; -.
DR DisGeNET; 26523; -.
DR GeneCards; AGO1; -.
DR HGNC; HGNC:3262; AGO1.
DR HPA; ENSG00000092847; Low tissue specificity.
DR MIM; 606228; gene.
DR neXtProt; NX_Q9UL18; -.
DR OpenTargets; ENSG00000092847; -.
DR PharmGKB; PA27693; -.
DR VEuPathDB; HostDB:ENSG00000092847; -.
DR eggNOG; KOG1041; Eukaryota.
DR GeneTree; ENSGT00940000158568; -.
DR HOGENOM; CLU_004544_4_3_1; -.
DR InParanoid; Q9UL18; -.
DR OMA; IHDEIFT; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q9UL18; -.
DR TreeFam; TF101510; -.
DR PathwayCommons; Q9UL18; -.
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-5578749; Transcriptional regulation 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; Q9UL18; -.
DR BioGRID-ORCS; 26523; 51 hits in 1078 CRISPR screens.
DR ChiTaRS; AGO1; human.
DR EvolutionaryTrace; Q9UL18; -.
DR GeneWiki; EIF2C1; -.
DR GenomeRNAi; 26523; -.
DR Pharos; Q9UL18; Tbio.
DR PRO; PR:Q9UL18; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UL18; protein.
DR Bgee; ENSG00000092847; Expressed in ganglionic eminence and 195 other tissues.
DR ExpressionAtlas; Q9UL18; baseline and differential.
DR Genevisible; Q9UL18; HS.
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:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:BHF-UCL.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP:BHF-UCL.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
DR GO; GO:0035198; F:miRNA binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:BHF-UCL.
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:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
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 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; Cytoplasm; Disease variant; Reference proteome; Repressor;
KW Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation; Ubl conjugation.
FT CHAIN 1..857
FT /note="Protein argonaute-1"
FT /id="PRO_0000194055"
FT DOMAIN 226..346
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 515..816
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 309..314
FT /note="Interaction with guide RNA"
FT REGION 522..564
FT /note="Interaction with guide RNA"
FT REGION 670..675
FT /note="Impairs access of bound RNA to the active site"
FT REGION 708..712
FT /note="Interaction with guide RNA"
FT REGION 751..759
FT /note="Interaction with guide RNA"
FT REGION 788..813
FT /note="Interaction with guide RNA"
FT VARIANT 199
FT /note="G -> S (probable disease-associated variant found in
FT a patient with moderate intellectual disability and
FT epilepsy)"
FT /evidence="ECO:0000269|PubMed:25003005"
FT /id="VAR_078651"
FT MUTAGEN 670
FT /note="P->S: Confers modest RNA cleavage activity; when
FT associated with Q-675 and H-805."
FT /evidence="ECO:0000269|PubMed:23809764"
FT MUTAGEN 674
FT /note="L->F: Confers modest RNA cleavage activity; when
FT associated with H-805."
FT /evidence="ECO:0000269|PubMed:23746446"
FT MUTAGEN 675
FT /note="P->Q: Does not confer enzyme activity by itself.
FT Confers low RNA cleavage activity; when associated with H-
FT 805. Confers modest RNA cleavage activity; when associated
FT with S-670 and H-805."
FT /evidence="ECO:0000269|PubMed:23809764"
FT MUTAGEN 805
FT /note="R->H: Does not confer enzyme activity by itself.
FT Confers modest RNA cleavage activity; when associated with
FT F-674."
FT /evidence="ECO:0000269|PubMed:23746446,
FT ECO:0000269|PubMed:23809764"
FT CONFLICT 242
FT /note="D -> N (in Ref. 3; AAH63275)"
FT /evidence="ECO:0000305"
FT STRAND 33..46
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:4KRF"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:4KXT"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 125..137
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 194..206
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 208..223
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1SI2"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:1SI2"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:1SI2"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 370..384
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 448..453
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 462..478
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 499..509
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 526..535
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 547..551
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 555..568
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 608..615
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 617..620
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 623..631
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 640..655
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:4KRF"
FT HELIX 674..692
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 699..706
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 713..717
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 718..720
FT /evidence="ECO:0007829|PDB:4KRE"
FT TURN 723..726
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 745..749
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 761..768
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 774..784
FT /evidence="ECO:0007829|PDB:4KRE"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:5W6V"
FT HELIX 799..814
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 837..843
FT /evidence="ECO:0007829|PDB:4KRE"
FT HELIX 848..851
FT /evidence="ECO:0007829|PDB:4KRE"
SQ SEQUENCE 857 AA; 97214 MW; 1DBB524AE7CBAF66 CRC64;
MEAGPSGAAA GAYLPPLQQV FQAPRRPGIG TVGKPIKLLA NYFEVDIPKI DVYHYEVDIK
PDKCPRRVNR EVVEYMVQHF KPQIFGDRKP VYDGKKNIYT VTALPIGNER VDFEVTIPGE
GKDRIFKVSI KWLAIVSWRM LHEALVSGQI PVPLESVQAL DVAMRHLASM RYTPVGRSFF
SPPEGYYHPL GGGREVWFGF HQSVRPAMWK MMLNIDVSAT AFYKAQPVIE FMCEVLDIRN
IDEQPKPLTD SQRVRFTKEI KGLKVEVTHC GQMKRKYRVC NVTRRPASHQ TFPLQLESGQ
TVECTVAQYF KQKYNLQLKY PHLPCLQVGQ EQKHTYLPLE VCNIVAGQRC IKKLTDNQTS
TMIKATARSA PDRQEEISRL MKNASYNLDP YIQEFGIKVK DDMTEVTGRV LPAPILQYGG
RNRAIATPNQ GVWDMRGKQF YNGIEIKVWA IACFAPQKQC REEVLKNFTD QLRKISKDAG
MPIQGQPCFC KYAQGADSVE PMFRHLKNTY SGLQLIIVIL PGKTPVYAEV KRVGDTLLGM
ATQCVQVKNV VKTSPQTLSN LCLKINVKLG GINNILVPHQ RSAVFQQPVI FLGADVTHPP
AGDGKKPSIT AVVGSMDAHP SRYCATVRVQ RPRQEIIEDL SYMVRELLIQ FYKSTRFKPT
RIIFYRDGVP EGQLPQILHY ELLAIRDACI KLEKDYQPGI TYIVVQKRHH TRLFCADKNE
RIGKSGNIPA GTTVDTNITH PFEFDFYLCS HAGIQGTSRP SHYYVLWDDN RFTADELQIL
TYQLCHTYVR CTRSVSIPAP AYYARLVAFR ARYHLVDKEH DSGEGSHISG QSNGRDPQAL
AKAVQVHQDT LRTMYFA
