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Database: UniProt
Entry: Q9UL18
LinkDB: Q9UL18
Original site: Q9UL18 
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   13-NOV-2019, entry version 169.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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,
RT   genomic organization, localization to chromosomal bands 1p34-p35, and
RT   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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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
RT   project: 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.,
RA   Tuschl T.;
RT   "Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
RT   siRNAs.";
RL   Mol. Cell 15:185-197(2004).
RN   [5]
RP   FUNCTION, INTERACTION WITH DICER1; MOV10; PRMT5 AND TNRC6B, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=16289642; DOI=10.1016/j.cub.2005.10.048;
RA   Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H.,
RA   Luehrmann R., 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
RT   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
RT   silencing 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;
RP   RBM4; 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-
RT   protein 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-
RT   target 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
RT   to 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
RT   microRNA-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.,
RA   Buerckstuemmer T., 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
RT   P 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
RT   recognition by the PAZ domain.";
RL   Nature 429:318-322(2004).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH RNA,
RP   RNA-BINDING, MUTAGENESIS OF PRO-670; PRO-675 AND ARG-805, AND LACK OF
RP   CATALYTIC ACTIVITY.
RX   PubMed=23809764; DOI=10.1016/j.celrep.2013.06.010;
RA   Nakanishi K., Ascano M., Gogakos T., Ishibe-Murakami S.,
RA   Serganov A.A., 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
CC       to 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
CC       appear to cleave target mRNAs. Also required for transcriptional
CC       gene silencing (TGS) of promoter regions which are complementary
CC       to bound short antigene RNAs (agRNAs).
CC       {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16936728,
CC       ECO:0000269|PubMed:18771919}.
CC   -!- SUBUNIT: Interacts with DDB1, DDX5, DDX6, DHX30, DHX36, DDX47,
CC       DICER1, AGO2, ELAVL1, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10,
CC       PABPC1, PRMT5, RBM4, SART3, TNRC6B, UPF1 and YBX1. Associates with
CC       polysomes and messenger ribonucleoproteins (mNRPs). Interacts with
CC       LIMD1, WTIP and AJUBA. Interacts with APOBEC3F, APOBEC3G and
CC       APOBEC3H. {ECO:0000269|PubMed:16289642,
CC       ECO:0000269|PubMed:16756390, ECO:0000269|PubMed:17932509,
CC       ECO:0000269|PubMed:19167051, ECO:0000269|PubMed:20616046,
CC       ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23746446,
CC       ECO:0000269|PubMed:23809764}.
CC   -!- INTERACTION:
CC       Q9UKV8:AGO2; NbExp=3; IntAct=EBI-527363, EBI-528269;
CC       Q9UPY3:DICER1; NbExp=5; IntAct=EBI-527363, EBI-395506;
CC       P08238:HSP90AB1; NbExp=3; IntAct=EBI-527363, EBI-352572;
CC       O15397:IPO8; NbExp=2; IntAct=EBI-527363, EBI-358808;
CC       P53041:PPP5C; NbExp=2; IntAct=EBI-527363, EBI-716663;
CC       P04156:PRNP; NbExp=2; IntAct=EBI-527363, EBI-977302;
CC       Q8NDV7:TNRC6A; NbExp=5; IntAct=EBI-527363, EBI-2269715;
CC       Q9UPQ9-2:TNRC6B; NbExp=4; IntAct=EBI-527363, EBI-6514011;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:20616046}.
CC   -!- MISCELLANEOUS: Lacks RNA cleavage activity due to the absence of
CC       the conserved His at position 805, but also because it binds the
CC       RNA in a subtly different manner that precludes efficient
CC       cleavage.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000305}.
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   SMR; Q9UL18; -.
DR   BioGrid; 117726; 62.
DR   DIP; DIP-29193N; -.
DR   IntAct; Q9UL18; 186.
DR   MINT; Q9UL18; -.
DR   STRING; 9606.ENSP00000362300; -.
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   Ensembl; ENST00000373204; ENSP00000362300; ENSG00000092847.
DR   GeneID; 26523; -.
DR   KEGG; hsa:26523; -.
DR   UCSC; uc001bzl.4; human.
DR   CTD; 26523; -.
DR   DisGeNET; 26523; -.
DR   GeneCards; AGO1; -.
DR   HGNC; HGNC:3262; AGO1.
DR   MIM; 606228; gene.
DR   neXtProt; NX_Q9UL18; -.
DR   OpenTargets; ENSG00000092847; -.
DR   PharmGKB; PA27693; -.
DR   eggNOG; KOG1041; Eukaryota.
DR   eggNOG; ENOG410XP07; LUCA.
DR   GeneTree; ENSGT00940000158568; -.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; Q9UL18; -.
DR   KO; K11593; -.
DR   OMA; VRSTNPN; -.
DR   OrthoDB; 159407at2759; -.
DR   PhylomeDB; Q9UL18; -.
DR   TreeFam; TF101510; -.
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-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   ChiTaRS; AGO1; human.
DR   EvolutionaryTrace; Q9UL18; -.
DR   GeneWiki; EIF2C1; -.
DR   GenomeRNAi; 26523; -.
DR   Pharos; Q9UL18; -.
DR   PRO; PR:Q9UL18; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000092847; Expressed in 219 organ(s), highest expression level in prostate gland.
DR   ExpressionAtlas; Q9UL18; baseline and differential.
DR   Genevisible; Q9UL18; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0001047; F:core promoter 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:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
DR   GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:BHF-UCL.
DR   GO; GO:0035278; P:miRNA mediated inhibition of translation; IDA:UniProtKB.
DR   GO; GO:0010586; P:miRNA metabolic process; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0010629; P:negative regulation of gene expression; TAS:Reactome.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; TAS:Reactome.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0035194; P:posttranscriptional gene silencing by RNA; TAS:Reactome.
DR   GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
DR   GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
DR   GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
DR   GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
DR   GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
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; 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; Complete proteome; Cytoplasm; Disease mutation;
KW   Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Transcription; Transcription regulation;
KW   Translation regulation.
FT   CHAIN         1    857       Protein argonaute-1.
FT                                /FTId=PRO_0000194055.
FT   DOMAIN      226    346       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      515    816       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   REGION      309    314       Interaction with guide RNA.
FT   REGION      522    564       Interaction with guide RNA.
FT   REGION      670    675       Impairs access of bound RNA to the active
FT                                site.
FT   REGION      708    712       Interaction with guide RNA.
FT   REGION      751    759       Interaction with guide RNA.
FT   REGION      788    813       Interaction with guide RNA.
FT   VARIANT     199    199       G -> S (probable disease-associated
FT                                mutation found in a patient with moderate
FT                                intellectual disability and epilepsy).
FT                                {ECO:0000269|PubMed:25003005}.
FT                                /FTId=VAR_078651.
FT   MUTAGEN     670    670       P->S: Confers modest RNA cleavage
FT                                activity; when associated with Q-675 and
FT                                H-805. {ECO:0000269|PubMed:23809764}.
FT   MUTAGEN     674    674       L->F: Confers modest RNA cleavage
FT                                activity; when associated with H-805.
FT                                {ECO:0000269|PubMed:23746446}.
FT   MUTAGEN     675    675       P->Q: Does not confer enzyme activity by
FT                                itself. Confers low RNA cleavage
FT                                activity; when associated with H-805.
FT                                Confers modest RNA cleavage activity;
FT                                when associated with S-670 and H-805.
FT                                {ECO:0000269|PubMed:23809764}.
FT   MUTAGEN     805    805       R->H: Does not confer enzyme activity by
FT                                itself. Confers modest RNA cleavage
FT                                activity; when associated with F-674.
FT                                {ECO:0000269|PubMed:23746446,
FT                                ECO:0000269|PubMed:23809764}.
FT   CONFLICT    242    242       D -> N (in Ref. 3; AAH63275).
FT                                {ECO:0000305}.
FT   STRAND       33     46       {ECO:0000244|PDB:4KRE}.
FT   STRAND       51     62       {ECO:0000244|PDB:4KRE}.
FT   HELIX        66     79       {ECO:0000244|PDB:4KRE}.
FT   HELIX        81     85       {ECO:0000244|PDB:4KRF}.
FT   STRAND       94    102       {ECO:0000244|PDB:4KRE}.
FT   TURN        105    108       {ECO:0000244|PDB:4KXT}.
FT   STRAND      110    115       {ECO:0000244|PDB:4KRE}.
FT   STRAND      125    137       {ECO:0000244|PDB:4KRE}.
FT   HELIX       138    147       {ECO:0000244|PDB:4KRE}.
FT   HELIX       154    171       {ECO:0000244|PDB:4KRE}.
FT   STRAND      172    175       {ECO:0000244|PDB:4KRE}.
FT   STRAND      178    180       {ECO:0000244|PDB:4KRE}.
FT   STRAND      189    191       {ECO:0000244|PDB:4KRE}.
FT   STRAND      194    206       {ECO:0000244|PDB:4KRE}.
FT   STRAND      208    223       {ECO:0000244|PDB:4KRE}.
FT   HELIX       228    236       {ECO:0000244|PDB:4KRE}.
FT   TURN        241    243       {ECO:0000244|PDB:1SI2}.
FT   HELIX       250    260       {ECO:0000244|PDB:4KRE}.
FT   STRAND      264    268       {ECO:0000244|PDB:4KRE}.
FT   TURN        269    272       {ECO:0000244|PDB:1SI2}.
FT   STRAND      276    286       {ECO:0000244|PDB:4KRE}.
FT   TURN        287    289       {ECO:0000244|PDB:4KRE}.
FT   STRAND      291    295       {ECO:0000244|PDB:4KRE}.
FT   STRAND      301    305       {ECO:0000244|PDB:4KRE}.
FT   HELIX       306    314       {ECO:0000244|PDB:4KRE}.
FT   STRAND      323    328       {ECO:0000244|PDB:4KRE}.
FT   HELIX       331    333       {ECO:0000244|PDB:1SI2}.
FT   STRAND      335    338       {ECO:0000244|PDB:4KRE}.
FT   HELIX       339    341       {ECO:0000244|PDB:4KRE}.
FT   STRAND      342    344       {ECO:0000244|PDB:4KRE}.
FT   HELIX       356    366       {ECO:0000244|PDB:4KRE}.
FT   HELIX       370    384       {ECO:0000244|PDB:4KRE}.
FT   HELIX       386    388       {ECO:0000244|PDB:4KRE}.
FT   HELIX       390    394       {ECO:0000244|PDB:4KRE}.
FT   STRAND      404    410       {ECO:0000244|PDB:4KRE}.
FT   TURN        420    423       {ECO:0000244|PDB:4KRE}.
FT   STRAND      448    453       {ECO:0000244|PDB:4KRE}.
FT   TURN        457    459       {ECO:0000244|PDB:4KRE}.
FT   HELIX       462    478       {ECO:0000244|PDB:4KRE}.
FT   STRAND      488    492       {ECO:0000244|PDB:4KRE}.
FT   HELIX       496    498       {ECO:0000244|PDB:4KRE}.
FT   HELIX       499    509       {ECO:0000244|PDB:4KRE}.
FT   STRAND      515    520       {ECO:0000244|PDB:4KRE}.
FT   HELIX       526    535       {ECO:0000244|PDB:4KRE}.
FT   TURN        536    538       {ECO:0000244|PDB:4KRE}.
FT   STRAND      542    546       {ECO:0000244|PDB:4KRE}.
FT   HELIX       547    551       {ECO:0000244|PDB:4KRE}.
FT   HELIX       555    568       {ECO:0000244|PDB:4KRE}.
FT   HELIX       578    580       {ECO:0000244|PDB:4KRE}.
FT   HELIX       583    586       {ECO:0000244|PDB:4KRE}.
FT   STRAND      589    597       {ECO:0000244|PDB:4KRE}.
FT   STRAND      608    615       {ECO:0000244|PDB:4KRE}.
FT   STRAND      617    620       {ECO:0000244|PDB:4KRE}.
FT   STRAND      623    631       {ECO:0000244|PDB:4KRE}.
FT   HELIX       640    655       {ECO:0000244|PDB:4KRE}.
FT   STRAND      660    666       {ECO:0000244|PDB:4KRE}.
FT   HELIX       671    673       {ECO:0000244|PDB:4KRF}.
FT   HELIX       674    692       {ECO:0000244|PDB:4KRE}.
FT   STRAND      699    706       {ECO:0000244|PDB:4KRE}.
FT   STRAND      713    717       {ECO:0000244|PDB:4KRE}.
FT   HELIX       718    720       {ECO:0000244|PDB:4KRE}.
FT   TURN        723    726       {ECO:0000244|PDB:4KRE}.
FT   STRAND      732    734       {ECO:0000244|PDB:4KRE}.
FT   STRAND      736    739       {ECO:0000244|PDB:4KRE}.
FT   STRAND      741    743       {ECO:0000244|PDB:4KRE}.
FT   STRAND      745    749       {ECO:0000244|PDB:4KRE}.
FT   STRAND      755    757       {ECO:0000244|PDB:4KRE}.
FT   STRAND      761    768       {ECO:0000244|PDB:4KRE}.
FT   HELIX       774    784       {ECO:0000244|PDB:4KRE}.
FT   STRAND      791    793       {ECO:0000244|PDB:5W6V}.
FT   HELIX       799    814       {ECO:0000244|PDB:4KRE}.
FT   HELIX       837    843       {ECO:0000244|PDB:4KRE}.
FT   HELIX       848    851       {ECO:0000244|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
//
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