ID AGO1_MOUSE Reviewed; 857 AA.
AC Q8CJG1; A1L365;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Protein argonaute-1;
DE Short=Argonaute1;
DE Short=mAgo1;
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=Piwi/argonaute family protein meIF2C1;
GN Name=Ago1; Synonyms=Eif2c1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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).
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. May also be required for transcriptional gene
CC silencing (TGS) of promoter regions which are complementary to bound
CC short antigene RNAs (agRNAs). {ECO:0000269|PubMed:19174539}.
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) (By similarity). Interacts with
CC LIMD1, WTIP and AJUBA (By similarity). Interacts with APOBEC3F,
CC APOBEC3G and APOBEC3H (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8CJG1; Q8CH72: Trim32; NbExp=2; IntAct=EBI-2291996, EBI-773837;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
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DR EMBL; AB081471; BAC15766.1; -; mRNA.
DR EMBL; AL606935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129914; AAI29915.1; -; mRNA.
DR CCDS; CCDS18653.1; -.
DR RefSeq; NP_001304102.1; NM_001317173.1.
DR RefSeq; NP_700452.2; NM_153403.3.
DR AlphaFoldDB; Q8CJG1; -.
DR SMR; Q8CJG1; -.
DR BioGRID; 231767; 32.
DR IntAct; Q8CJG1; 5.
DR MINT; Q8CJG1; -.
DR STRING; 10090.ENSMUSP00000095498; -.
DR iPTMnet; Q8CJG1; -.
DR PhosphoSitePlus; Q8CJG1; -.
DR SwissPalm; Q8CJG1; -.
DR EPD; Q8CJG1; -.
DR MaxQB; Q8CJG1; -.
DR PaxDb; 10090-ENSMUSP00000095498; -.
DR ProteomicsDB; 285623; -.
DR Pumba; Q8CJG1; -.
DR Antibodypedia; 31600; 340 antibodies from 39 providers.
DR DNASU; 236511; -.
DR Ensembl; ENSMUST00000097888.10; ENSMUSP00000095498.4; ENSMUSG00000041530.18.
DR Ensembl; ENSMUST00000239428.2; ENSMUSP00000159361.2; ENSMUSG00000041530.18.
DR GeneID; 236511; -.
DR KEGG; mmu:236511; -.
DR UCSC; uc008utj.2; mouse.
DR AGR; MGI:2446630; -.
DR CTD; 26523; -.
DR MGI; MGI:2446630; Ago1.
DR VEuPathDB; HostDB:ENSMUSG00000041530; -.
DR eggNOG; KOG1041; Eukaryota.
DR GeneTree; ENSGT00940000158568; -.
DR HOGENOM; CLU_004544_4_3_1; -.
DR InParanoid; Q8CJG1; -.
DR OMA; IHDEIFT; -.
DR OrthoDB; 3060088at2759; -.
DR PhylomeDB; Q8CJG1; -.
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 BioGRID-ORCS; 236511; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Ago1; mouse.
DR PRO; PR:Q8CJG1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CJG1; Protein.
DR Bgee; ENSMUSG00000041530; Expressed in floor plate of midbrain and 239 other cell types or tissues.
DR ExpressionAtlas; Q8CJG1; baseline and differential.
DR Genevisible; Q8CJG1; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0016442; C:RISC complex; IDA:MGI.
DR GO; GO:0070578; C:RISC-loading complex; ISO:MGI.
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:0035198; F:miRNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA 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:0000976; F:transcription cis-regulatory region binding; IMP:BHF-UCL.
DR GO; GO:0010586; P:miRNA metabolic process; IDA:MGI.
DR GO; GO:0035196; P:miRNA processing; ISO:MGI.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0031054; P:pre-miRNA processing; ISO:MGI.
DR GO; GO:0070922; P:RISC complex assembly; ISO:MGI.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
DR CDD; cd02846; PAZ_argonaute_like; 1.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.170.260.10; paz domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR032473; Argonaute_Mid_dom.
DR InterPro; IPR032474; Argonaute_N.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR045246; Piwi_ago-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR22891; EUKARYOTIC TRANSLATION INITIATION FACTOR 2C; 1.
DR PANTHER; PTHR22891:SF17; PROTEIN ARGONAUTE-1; 1.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF16488; ArgoL2; 1.
DR Pfam; PF16487; ArgoMid; 1.
DR Pfam; PF16486; ArgoN; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; PAZ domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..857
FT /note="Protein argonaute-1"
FT /id="PRO_0000194056"
FT DOMAIN 227..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 /evidence="ECO:0000250"
FT REGION 522..564
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 670..675
FT /note="Impairs access of bound RNA to the active site"
FT /evidence="ECO:0000250"
FT REGION 708..712
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 751..759
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 788..813
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT CONFLICT 96
FT /note="K -> E (in Ref. 1; BAC15766)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="Y -> H (in Ref. 1; BAC15766)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="Y -> C (in Ref. 1; BAC15766)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="V -> A (in Ref. 1; BAC15766)"
FT /evidence="ECO:0000305"
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
//
