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AGO1_MOUSE
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   03-AUG-2022, entry version 141.
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; 31.
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   ProteomicsDB; 285623; -.
DR   Antibodypedia; 31600; 299 antibodies from 39 providers.
DR   DNASU; 236511; -.
DR   Ensembl; ENSMUST00000097888; ENSMUSP00000095498; ENSMUSG00000041530.
DR   Ensembl; ENSMUST00000239428; ENSMUSP00000159361; ENSMUSG00000041530.
DR   GeneID; 236511; -.
DR   KEGG; mmu:236511; -.
DR   UCSC; uc008utj.2; mouse.
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; 159407at2759; -.
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   Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR   BioGRID-ORCS; 236511; 3 hits in 72 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 236 other tissues.
DR   ExpressionAtlas; Q8CJG1; baseline and differential.
DR   Genevisible; Q8CJG1; 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: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: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 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:0070922; P:RISC complex assembly; ISO:MGI.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
DR   CDD; cd04657; Piwi_ago-like; 1.
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; 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; 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          226..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
 
 
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