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Database: UniProt
Entry: Q8CJG0
LinkDB: Q8CJG0
Original site: Q8CJG0 
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   11-DEC-2019, entry version 153.
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). {ECO:0000250|UniProtKB:Q9UKV8, ECO:0000255|HAMAP-
CC       Rule:MF_03031, ECO:0000269|PubMed:16357216,
CC       ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726,
CC       ECO:0000269|PubMed:22735451, ECO:0000269|PubMed:25697406,
CC       ECO:0000269|PubMed:26009488, ECO:0000269|PubMed:29311329}.
CC   -!- INTERACTION:
CC       Q9UPY3:DICER1 (xeno); NbExp=2; IntAct=EBI-528299, EBI-395506;
CC       P04156:PRNP (xeno); NbExp=2; IntAct=EBI-528299, EBI-977302;
CC       P04273:PRNP (xeno); NbExp=2; IntAct=EBI-528299, EBI-986426;
CC       Q4VGL6:Rc3h1; NbExp=2; IntAct=EBI-528299, EBI-2366263;
CC       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   -!- 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};
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   SMR; Q8CJG0; -.
DR   BioGrid; 232092; 9.
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; 55.
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   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   eggNOG; KOG1041; Eukaryota.
DR   eggNOG; ENOG410XP07; LUCA.
DR   GeneTree; ENSGT00940000155239; -.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; Q8CJG0; -.
DR   KO; K11593; -.
DR   OMA; SPDGYYH; -.
DR   OrthoDB; 159407at2759; -.
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   ChiTaRS; Ago2; mouse.
DR   PRO; PR:Q8CJG0; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8CJG0; protein.
DR   Bgee; ENSMUSG00000036698; Expressed in 246 organ(s), highest expression level in mesenteric lymph node.
DR   Genevisible; Q8CJG0; MM.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; 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:0005654; C:nucleoplasm; ISO:MGI.
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:0001047; F:core promoter 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:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; ISO:MGI.
DR   GO; GO:0035278; P:miRNA mediated inhibition of translation; ISS:UniProtKB.
DR   GO; GO:0010586; P:miRNA metabolic process; IDA:MGI.
DR   GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; IDA:BHF-UCL.
DR   GO; GO:0090625; P:mRNA cleavage involved in gene silencing by siRNA; ISO:MGI.
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:1905618; P:positive regulation of miRNA mediated inhibition of translation; ISO: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:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:MGI.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
DR   GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; ISO:MGI.
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; 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.
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   METAL           598
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT   METAL           670
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT   METAL           808
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT   MOD_RES         2
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000244|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         829
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
//
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