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Database: UniProt
Entry: Q8CJG1
LinkDB: Q8CJG1
Original site: Q8CJG1 
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   16-OCT-2019, entry version 127.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   requires 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
RT   microRNA 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
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. May also be required for
CC       transcriptional gene silencing (TGS) of promoter regions which are
CC       complementary to bound short antigene RNAs (agRNAs).
CC       {ECO:0000269|PubMed:19174539}.
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) (By
CC       similarity). Interacts with LIMD1, WTIP and AJUBA (By similarity).
CC       Interacts with APOBEC3F, APOBEC3G and APOBEC3H (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8CH72:Trim32; NbExp=2; IntAct=EBI-2291996, EBI-773837;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000305}.
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   SMR; Q8CJG1; -.
DR   BioGrid; 231767; 5.
DR   IntAct; Q8CJG1; 5.
DR   MINT; Q8CJG1; -.
DR   STRING; 10090.ENSMUSP00000095498; -.
DR   iPTMnet; Q8CJG1; -.
DR   PhosphoSitePlus; Q8CJG1; -.
DR   EPD; Q8CJG1; -.
DR   MaxQB; Q8CJG1; -.
DR   PaxDb; Q8CJG1; -.
DR   PRIDE; Q8CJG1; -.
DR   Ensembl; ENSMUST00000097888; ENSMUSP00000095498; ENSMUSG00000041530.
DR   GeneID; 236511; -.
DR   KEGG; mmu:236511; -.
DR   UCSC; uc008utj.2; mouse.
DR   CTD; 26523; -.
DR   MGI; MGI:2446630; Ago1.
DR   eggNOG; KOG1041; Eukaryota.
DR   eggNOG; ENOG410XP07; LUCA.
DR   GeneTree; ENSGT00940000158568; -.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; Q8CJG1; -.
DR   KO; K11593; -.
DR   OMA; VRSTNPN; -.
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; Ago1; mouse.
DR   PRO; PR:Q8CJG1; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000041530; Expressed in 243 organ(s), highest expression level in floor plate of midbrain.
DR   ExpressionAtlas; Q8CJG1; baseline and differential.
DR   Genevisible; Q8CJG1; MM.
DR   GO; GO:0005737; C:cytoplasm; 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; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0016442; C:RISC complex; IDA:MGI.
DR   GO; GO:0070578; C:RISC-loading complex; ISO:MGI.
DR   GO; GO:0001047; F:core promoter 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:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IMP:BHF-UCL.
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: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 NIK/NF-kappaB signaling; 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:0035196; P:production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
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   Complete proteome; Cytoplasm; Reference proteome; Repressor;
KW   Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing;
KW   Transcription; Transcription regulation; Translation regulation.
FT   CHAIN         1    857       Protein argonaute-1.
FT                                /FTId=PRO_0000194056.
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                                {ECO:0000250}.
FT   REGION      522    564       Interaction with guide RNA.
FT                                {ECO:0000250}.
FT   REGION      670    675       Impairs access of bound RNA to the active
FT                                site. {ECO:0000250}.
FT   REGION      708    712       Interaction with guide RNA.
FT                                {ECO:0000250}.
FT   REGION      751    759       Interaction with guide RNA.
FT                                {ECO:0000250}.
FT   REGION      788    813       Interaction with guide RNA.
FT                                {ECO:0000250}.
FT   CONFLICT     96     96       K -> E (in Ref. 1; BAC15766).
FT                                {ECO:0000305}.
FT   CONFLICT    309    309       Y -> H (in Ref. 1; BAC15766).
FT                                {ECO:0000305}.
FT   CONFLICT    386    386       Y -> C (in Ref. 1; BAC15766).
FT                                {ECO:0000305}.
FT   CONFLICT    550    550       V -> A (in Ref. 1; BAC15766).
FT                                {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
//
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