AGO2_MOUSE
ID AGO2_MOUSE Reviewed; 860 AA.
AC Q8CJG0; A1A563; Q4VAB3; Q571J6;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE Short=Argonaute2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE Short=mAgo2;
DE EC=3.1.26.n2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE AltName: Full=Argonaute RISC catalytic component 2;
DE AltName: Full=Eukaryotic translation initiation factor 2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE Short=eIF-2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE Short=eIF2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE AltName: Full=Piwi/argonaute family protein meIF2C2;
DE AltName: Full=Protein slicer {ECO:0000255|HAMAP-Rule:MF_03031};
GN Name=Ago2; Synonyms=Eif2c2, Kiaa4215;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12526743; DOI=10.1016/s0960-9822(02)01394-5;
RA Doi N., Zenno S., Ueda R., Ohki-Hamazaki H., Ui-Tei K., Saigo K.;
RT "Short-interfering-RNA-mediated gene silencing in mammalian cells requires
RT Dicer and eIF2C translation initiation factors.";
RL Curr. Biol. 13:41-46(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-860.
RC TISSUE=Embryonic tail;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15284456; DOI=10.1126/science.1102513;
RA Liu J., Carmell M.A., Rivas F.V., Marsden C.G., Thomson J.M., Song J.-J.,
RA Hammond S.M., Joshua-Tor L., Hannon G.J.;
RT "Argonaute2 is the catalytic engine of mammalian RNAi.";
RL Science 305:1437-1441(2004).
RN [5]
RP INTERACTION WITH DICER1 AND TARBP2.
RX PubMed=16357216; DOI=10.1101/gad.1384005;
RA Maniataki E., Mourelatos Z.;
RT "A human, ATP-independent, RISC assembly machine fueled by pre-miRNA.";
RL Genes Dev. 19:2979-2990(2005).
RN [6]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [7]
RP FUNCTION.
RX PubMed=17626790; DOI=10.1101/gad.1565607;
RA O'Carroll D., Mecklenbrauker I., Das P.P., Santana A., Koenig U.,
RA Enright A.J., Miska E.A., Tarakhovsky A.;
RT "A Slicer-independent role for Argonaute 2 in hematopoiesis and the
RT microRNA pathway.";
RL Genes Dev. 21:1999-2004(2007).
RN [8]
RP FUNCTION.
RX PubMed=19174539; DOI=10.1101/gad.1749809;
RA Su H., Trombly M.I., Chen J., Wang X.;
RT "Essential and overlapping functions for mammalian Argonautes in microRNA
RT silencing.";
RL Genes Dev. 23:304-317(2009).
RN [9]
RP INTERACTION WITH TRIM71.
RX PubMed=19898466; DOI=10.1038/ncb1987;
RA Rybak A., Fuchs H., Hadian K., Smirnova L., Wulczyn E.A., Michel G.,
RA Nitsch R., Krappmann D., Wulczyn F.G.;
RT "The let-7 target gene mouse lin-41 is a stem cell specific E3 ubiquitin
RT ligase for the miRNA pathway protein Ago2.";
RL Nat. Cell Biol. 11:1411-1420(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP INTERACTION WITH TRIM71.
RX PubMed=22508726; DOI=10.1101/gad.187641.112;
RA Chen J., Lai F., Niswander L.;
RT "The ubiquitin ligase mLin41 temporally promotes neural progenitor cell
RT maintenance through FGF signaling.";
RL Genes Dev. 26:803-815(2012).
RN [12]
RP INTERACTION WITH TRIM71.
RX PubMed=22735451; DOI=10.1038/ncomms1909;
RA Chang H.M., Martinez N.J., Thornton J.E., Hagan J.P., Nguyen K.D.,
RA Gregory R.I.;
RT "Trim71 cooperates with microRNAs to repress Cdkn1a expression and promote
RT embryonic stem cell proliferation.";
RL Nat. Commun. 3:923-923(2012).
RN [13]
RP INTERACTION WITH SND1 AND SYT11.
RX PubMed=24882364; DOI=10.1016/j.febslet.2014.05.031;
RA Milochau A., Lagree V., Benassy M.N., Chaignepain S., Papin J.,
RA Garcia-Arcos I., Lajoix A., Monterrat C., Coudert L., Schmitter J.M.,
RA Ochoa B., Lang J.;
RT "Synaptotagmin 11 interacts with components of the RNA-induced silencing
RT complex RISC in clonal pancreatic beta-cells.";
RL FEBS Lett. 588:2217-2222(2014).
RN [14]
RP INTERACTION WITH CLNK.
RX PubMed=26009488; DOI=10.1016/j.bbrc.2015.05.046;
RA Xu M., Cai C., Sun X., Chen W., Li Q., Zhou H.;
RT "Clnk plays a role in TNF-alpha-induced cell death in murine fibrosarcoma
RT cell line L929.";
RL Biochem. Biophys. Res. Commun. 463:275-279(2015).
RN [15]
RP INTERACTION WITH RC3H1.
RX PubMed=25697406; DOI=10.1038/ncomms7253;
RA Srivastava M., Duan G., Kershaw N.J., Athanasopoulos V., Yeo J.H., Ose T.,
RA Hu D., Brown S.H., Jergic S., Patel H.R., Pratama A., Richards S.,
RA Verma A., Jones E.Y., Heissmeyer V., Preiss T., Dixon N.E., Chong M.M.,
RA Babon J.J., Vinuesa C.G.;
RT "Roquin binds microRNA-146a and Argonaute2 to regulate microRNA
RT homeostasis.";
RL Nat. Commun. 6:6253-6253(2015).
RN [16]
RP INTERACTION WITH FAM172A, AND IDENTIFICATION IN A COMPLEX WITH FAM172A;
RP AGO2 AND CHD7.
RX PubMed=29311329; DOI=10.1073/pnas.1715378115;
RA Belanger C., Berube-Simard F.A., Leduc E., Bernas G., Campeau P.M.,
RA Lalani S.R., Martin D.M., Bielas S., Moccia A., Srivastava A.,
RA Silversides D.W., Pilon N.;
RT "Dysregulation of cotranscriptional alternative splicing underlies CHARGE
RT syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E620-E629(2018).
CC -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the RNA-
CC induced silencing complex (RISC). The 'minimal RISC' appears to include
CC AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short
CC interfering RNA (siRNA). These guide RNAs direct RISC to complementary
CC mRNAs that are targets for RISC-mediated gene silencing. The precise
CC mechanism of gene silencing depends on the degree of complementarity
CC between the miRNA or siRNA and its target. Binding of RISC to a
CC perfectly complementary mRNA generally results in silencing due to
CC endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of
CC RISC to a partially complementary mRNA results in silencing through
CC inhibition of translation, and this is independent of endonuclease
CC activity. May inhibit translation initiation by binding to the 7-
CC methylguanosine cap, thereby preventing the recruitment of the
CC translation initiation factor eIF4-E. May also inhibit translation
CC initiation via interaction with EIF6, which itself binds to the 60S
CC ribosomal subunit and prevents its association with the 40S ribosomal
CC subunit. The inhibition of translational initiation leads to the
CC accumulation of the affected mRNA in cytoplasmic processing bodies (P-
CC bodies), where mRNA degradation may subsequently occur. In some cases
CC RISC-mediated translational repression is also observed for miRNAs that
CC perfectly match the 3' untranslated region (3'-UTR). Can also up-
CC regulate the translation of specific mRNAs under certain growth
CC conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-
CC alpha) mRNA and up-regulates translation under conditions of serum
CC starvation. Also required for transcriptional gene silencing (TGS), in
CC which short RNAs known as antigene RNAs or agRNAs direct the
CC transcriptional repression of complementary promoter regions. Regulates
CC lymphoid and erythroid development and function, and this is
CC independent of endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_03031,
CC ECO:0000269|PubMed:15284456, ECO:0000269|PubMed:17626790,
CC ECO:0000269|PubMed:19174539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=endonucleolytic cleavage to 5'-phosphomonoester.;
CC EC=3.1.26.n2; Evidence={ECO:0000255|HAMAP-Rule:MF_03031};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with DICER1 through its Piwi domain and with TARBP2
CC during assembly of the RNA-induced silencing complex (RISC). Together,
CC DICER1, AGO2 and TARBP2 constitute the trimeric RISC loading complex
CC (RLC), or micro-RNA (miRNA) loading complex (miRLC). Within the
CC RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs
CC (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound
CC to the mature miRNA constitutes the minimal RISC and may subsequently
CC dissociate from DICER1 and TARBP2. Note however that the term RISC has
CC also been used to describe the trimeric RLC/miRLC. The formation of
CC RISC complexes containing siRNAs rather than miRNAs appears to occur
CC independently of DICER1 (PubMed:16357216). Interacts with AGO1. Also
CC interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9,
CC ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, PABPC1, PRMT5,
CC P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with
CC the P-body components DCP1A and XRN1. Associates with polysomes and
CC messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the
CC interaction is modulated under stress-induced conditions, occurs under
CC both cell proliferation and differentiation conditions and in an
CC RNA- and phosphorylation-independent manner. Interacts with LIMD1, WTIP
CC and AJUBA (By similarity). Interacts with TRIM71 (PubMed:19898466,
CC PubMed:22508726, PubMed:22735451). Interacts with APOBEC3G in an RNA-
CC dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F and
CC APOBEC3H. Interacts with DICER1, TARBP2, EIF6, MOV10 and RPL7A (60S
CC ribosome subunit); they form a large RNA-induced silencing complex
CC (RISC). Interacts with FMR1. Interacts with ZFP36 (By similarity).
CC Interacts with RC3H1; the interaction is RNA independent
CC (PubMed:25697406). Interacts with FAM172A (PubMed:29311329). Found in a
CC complex composed of AGO2, CHD7 and FAM172A (PubMed:29311329). Interacts
CC with SND1 and SYT11 (PubMed:24882364). Interacts with CLNK
CC (PubMed:26009488). Interacts with GARRE1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UKV8, ECO:0000255|HAMAP-Rule:MF_03031,
CC ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:19898466,
CC ECO:0000269|PubMed:22508726, ECO:0000269|PubMed:22735451,
CC ECO:0000269|PubMed:25697406, ECO:0000269|PubMed:26009488,
CC ECO:0000269|PubMed:29311329}.
CC -!- INTERACTION:
CC Q8CJG0; Q4VGL6: Rc3h1; NbExp=2; IntAct=EBI-528299, EBI-2366263;
CC Q8CJG0; Q9UPY3: DICER1; Xeno; NbExp=2; IntAct=EBI-528299, EBI-395506;
CC Q8CJG0; P04156: PRNP; Xeno; NbExp=2; IntAct=EBI-528299, EBI-977302;
CC Q8CJG0; P04273: PRNP; Xeno; NbExp=2; IntAct=EBI-528299, EBI-986426;
CC Q8CJG0; Q9HCJ0: TNRC6C; Xeno; NbExp=3; IntAct=EBI-528299, EBI-6507625;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03031}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03031}.
CC Note=Translational repression of mRNAs results in their recruitment to
CC P-bodies. Translocation to the nucleus requires IMP8.
CC {ECO:0000255|HAMAP-Rule:MF_03031}.
CC -!- TISSUE SPECIFICITY: Ubiquitous expression in 9.5 day embryos with
CC highest levels in forebrain, heart, limb buds, and branchial arches.
CC {ECO:0000269|PubMed:15284456}.
CC -!- DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism similar
CC to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp-
CC Glu (DDE) for metal ion coordination, this protein appears to utilize a
CC triad of Asp-Asp-His (DDH). {ECO:0000255|HAMAP-Rule:MF_03031}.
CC -!- PTM: Hydroxylated. 4-hydroxylation appears to enhance protein stability
CC but is not required for miRNA-binding or endonuclease activity.
CC {ECO:0000255|HAMAP-Rule:MF_03031}.
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 AGO2 when it is engaged with a TDMD target.
CC {ECO:0000250|UniProtKB:Q9UKV8}.
CC -!- PTM: Phosphorylation at Ser-388 by AKT3; leads to up-regulate
CC translational repression of microRNA target and down-regulate
CC endonucleolytic cleavage. {ECO:0000250|UniProtKB:Q9UKV8}.
CC -!- PTM: A phosphorylation cycle of C-terminal serine cluster (Ser-825-Ser-
CC 835) regulates the release of target mRNAs. Target-binding leads to
CC phosphorylation of these residues by CSNK1A1, which reduces the
CC affinity of AGO2 for mRNA and enables target release. The ANKRD52-PPP6C
CC phosphatase complex dephosphorylates the residues, which primes AGO2
CC for binding a new target. {ECO:0000250|UniProtKB:Q9UKV8}.
CC -!- DISRUPTION PHENOTYPE: Embryonic death with a strong defect in neural
CC tube closure and apparent cardiac failure.
CC {ECO:0000269|PubMed:15284456}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03031}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH96465.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB081472; BAC15767.1; -; mRNA.
DR EMBL; BC096465; AAH96465.1; ALT_INIT; mRNA.
DR EMBL; BC128379; AAI28380.1; -; mRNA.
DR EMBL; BC129922; AAI29923.1; -; mRNA.
DR EMBL; AK220193; BAD90378.1; -; mRNA.
DR CCDS; CCDS37098.1; -.
DR RefSeq; NP_694818.3; NM_153178.4.
DR AlphaFoldDB; Q8CJG0; -.
DR SMR; Q8CJG0; -.
DR BioGRID; 232092; 58.
DR ComplexPortal; CPX-1073; RISC-loading complex, PRKRA variant.
DR ComplexPortal; CPX-135; RISC-loading complex, TARBP2 variant.
DR DIP; DIP-35014N; -.
DR IntAct; Q8CJG0; 57.
DR MINT; Q8CJG0; -.
DR STRING; 10090.ENSMUSP00000042207; -.
DR iPTMnet; Q8CJG0; -.
DR PhosphoSitePlus; Q8CJG0; -.
DR SwissPalm; Q8CJG0; -.
DR EPD; Q8CJG0; -.
DR jPOST; Q8CJG0; -.
DR MaxQB; Q8CJG0; -.
DR PaxDb; Q8CJG0; -.
DR PeptideAtlas; Q8CJG0; -.
DR PRIDE; Q8CJG0; -.
DR ProteomicsDB; 285770; -.
DR Antibodypedia; 27626; 355 antibodies from 39 providers.
DR DNASU; 239528; -.
DR Ensembl; ENSMUST00000044113; ENSMUSP00000042207; ENSMUSG00000036698.
DR GeneID; 239528; -.
DR KEGG; mmu:239528; -.
DR UCSC; uc007wbu.2; mouse.
DR CTD; 27161; -.
DR MGI; MGI:2446632; Ago2.
DR VEuPathDB; HostDB:ENSMUSG00000036698; -.
DR eggNOG; KOG1041; Eukaryota.
DR GeneTree; ENSGT00940000155239; -.
DR HOGENOM; CLU_004544_4_3_1; -.
DR InParanoid; Q8CJG0; -.
DR OMA; CFAQQQH; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q8CJG0; -.
DR TreeFam; TF101510; -.
DR Reactome; R-MMU-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
DR Reactome; R-MMU-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 239528; 18 hits in 73 CRISPR screens.
DR ChiTaRS; Ago2; mouse.
DR PRO; PR:Q8CJG0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CJG0; protein.
DR Bgee; ENSMUSG00000036698; Expressed in ascending aorta and 219 other tissues.
DR Genevisible; Q8CJG0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
DR GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:MGI.
DR GO; GO:0090624; F:endoribonuclease activity, cleaving miRNA-paired mRNA; ISO:MGI.
DR GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-paired mRNA; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0098808; F:mRNA cap binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; IDA:MGI.
DR GO; GO:0035196; P:miRNA processing; IMP:MGI.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; IDA:BHF-UCL.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; ISO:MGI.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
DR GO; GO:0070922; P:RISC complex assembly; ISO:MGI.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
DR GO; GO:0030422; P:siRNA processing; ISO:MGI.
DR GO; GO:0090625; P:siRNA-mediated gene silencing by mRNA destabilization; ISO:MGI.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03031; AGO2; 1.
DR InterPro; IPR028602; AGO2.
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 Cytoplasm; Developmental protein; Differentiation; Endonuclease; Hydrolase;
KW Hydroxylation; Magnesium; Manganese; Metal-binding; Nitration; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
KW RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation; Ubl conjugation.
FT CHAIN 1..860
FT /note="Protein argonaute-2"
FT /id="PRO_0000194058"
FT DOMAIN 236..349
FT /note="PAZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT DOMAIN 518..819
FT /note="Piwi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT REGION 312..317
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 525..567
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 588..591
FT /note="Interaction with GW182 family members"
FT /evidence="ECO:0000255"
FT REGION 651..661
FT /note="Interaction with GW182 family members"
FT /evidence="ECO:0000255"
FT REGION 710..711
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 754..762
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 791..813
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT BINDING 670
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT BINDING 808
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT MOD_RES 2
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV8"
FT MOD_RES 701
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV8"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV8"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV8"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV8"
FT CONFLICT 65
FT /note="E -> G (in Ref. 2; AAH96465)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="C -> R (in Ref. 1; BAC15767)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="F -> L (in Ref. 1; BAC15767)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="N -> D (in Ref. 1; BAC15767)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="N -> D (in Ref. 2; AAH96465)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="R -> P (in Ref. 2; AAH96465)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="S -> G (in Ref. 1; BAC15767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 860 AA; 97304 MW; A4E13C633846062C CRC64;
MYSGAGPVLA SPAPTTSPIP GYAFKPPPRP DFGTTGRTIK LQANFFEMDI PKIDIYHYEL
DIKPEKCPRR VNREIVEHMV QHFKTQIFGD RKPVFDGRKN LYTAMPLPIG RDKVELEVTL
PGEGKDRIFK VSIKWVSCVS LQALHDALSG RLPSVPFETI QALDVVMRHL PSMRYTPVGR
SFFTASEGCS NPLGGGREVW FGFHQSVRPS LWKMMLNIDV SATAFYKAQP VIEFVCEVLD
FKSIEEQQKP LTDSQRVKFT KEIKGLKVEI THCGQMKRKY RVCNVTRRPA SHQTFPLQQE
SGQTVECTVA QYFKDRHKLV LRYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIRATA RSAPDRQEEI SKLMRSASFN TDPYVREFGI MVKDEMTDVT GRVLQPPSIL
YGGRNKAIAT PVQGVWDMRN KQFHTGIEIK VWAIACFAPQ RQCTEVHLKS FTEQLRKISR
DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYAGLQLVV VILPGKTPVY AEVKRVGDTV
LGMATQCVQM KNVQRTTPQT LSNLCLKINV KLGGVNNILL PQGRPPVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPNRYCATV RVQQHRQEII QDLAAMVREL LIQFYKSTRF
KPTRIIFYRD GVSEGQFQQV LHHELLAIRE ACIKLEKDYQ PGITFIVVQK RHHTRLFCTD
KNERVGKSGN IPAGTTVDTK ITHPTEFDFY LCSHAGIQGT SRPSHYHVLW DDNRFSSDEL
QILTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH TSGQSNGRDH
QALAKAVQVH QDTLRTMYFA
