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Database: UniProt
Entry: Q8CJF8
LinkDB: Q8CJF8
Original site: Q8CJF8 
ID   AGO4_MOUSE              Reviewed;         861 AA.
AC   Q8CJF8; Q4VBD7; Q6ZPM6; Q8BTF4;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   16-OCT-2019, entry version 123.
DE   RecName: Full=Protein argonaute-4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE            Short=Argonaute4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE            Short=mAgo4;
DE   AltName: Full=Argonaute RISC catalytic component 4;
DE   AltName: Full=Eukaryotic translation initiation factor 2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE            Short=eIF-2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE            Short=eIF2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE   AltName: Full=Piwi/argonaute family protein meIF2C4;
GN   Name=Ago4; Synonyms=Eif2c4, Kiaa1567;
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] (ISOFORM 1).
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 MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-861 (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [6]
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).
CC   -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds
CC       to short RNAs such as microRNAs (miRNAs) and represses the
CC       translation of mRNAs which are complementary to them. Lacks
CC       endonuclease activity and does not appear to cleave target mRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_03033, ECO:0000269|PubMed:19174539}.
CC   -!- SUBUNIT: Interacts with EIF4B, IMP8, PRMT5, TNRC6A and TNRC6B.
CC       Interacts with ZFP36. {ECO:0000255|HAMAP-Rule:MF_03033}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC       Rule:MF_03033}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CJF8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CJF8-2; Sequence=VSP_036487;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03033}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26738.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC98205.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
DR   EMBL; AB081474; BAC15769.1; -; mRNA.
DR   EMBL; AK030018; BAC26738.1; ALT_INIT; mRNA.
DR   EMBL; AL606935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096023; AAH96023.1; -; mRNA.
DR   EMBL; AK129395; BAC98205.2; ALT_SEQ; Transcribed_RNA.
DR   CCDS; CCDS18654.1; -. [Q8CJF8-1]
DR   RefSeq; NP_694817.2; NM_153177.3. [Q8CJF8-1]
DR   SMR; Q8CJF8; -.
DR   STRING; 10090.ENSMUSP00000081312; -.
DR   iPTMnet; Q8CJF8; -.
DR   PhosphoSitePlus; Q8CJF8; -.
DR   PaxDb; Q8CJF8; -.
DR   PeptideAtlas; Q8CJF8; -.
DR   PRIDE; Q8CJF8; -.
DR   Ensembl; ENSMUST00000084289; ENSMUSP00000081312; ENSMUSG00000042500. [Q8CJF8-1]
DR   GeneID; 76850; -.
DR   KEGG; mmu:76850; -.
DR   UCSC; uc008utk.2; mouse. [Q8CJF8-1]
DR   CTD; 192670; -.
DR   MGI; MGI:1924100; Ago4.
DR   eggNOG; KOG1041; Eukaryota.
DR   eggNOG; ENOG410XP07; LUCA.
DR   GeneTree; ENSGT00940000158729; -.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; Q8CJF8; -.
DR   KO; K11593; -.
DR   OMA; MFKHLKL; -.
DR   OrthoDB; 159407at2759; -.
DR   PhylomeDB; Q8CJF8; -.
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   ChiTaRS; Ago4; mouse.
DR   PRO; PR:Q8CJF8; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000042500; Expressed in 230 organ(s), highest expression level in ear.
DR   Genevisible; Q8CJF8; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
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:0016442; C:RISC complex; IDA:MGI.
DR   GO; GO:0070578; C:RISC-loading complex; ISO:MGI.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR   GO; GO:0035198; F:miRNA binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IDA:MGI.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR   GO; GO:0008584; P:male gonad development; IMP:MGI.
DR   GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
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; IMP:MGI.
DR   GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP: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:0022604; P:regulation of cell morphogenesis; IMP:MGI.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
DR   GO; GO:0007130; P:synaptonemal complex assembly; IMP:MGI.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_03033; AGO4; 1.
DR   InterPro; IPR028604; AGO4.
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   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Cytoplasm;
KW   Reference proteome; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation.
FT   CHAIN         1    861       Protein argonaute-4.
FT                                /FTId=PRO_0000194064.
FT   DOMAIN      225    338       PAZ. {ECO:0000255|HAMAP-Rule:MF_03033}.
FT   DOMAIN      509    820       Piwi. {ECO:0000255|HAMAP-Rule:MF_03033}.
FT   VAR_SEQ     399    460       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14621295}.
FT                                /FTId=VSP_036487.
FT   CONFLICT    128    128       V -> A (in Ref. 1; BAC15769).
FT                                {ECO:0000305}.
FT   CONFLICT    541    541       V -> I (in Ref. 1; BAC15769).
FT                                {ECO:0000305}.
FT   CONFLICT    570    570       L -> P (in Ref. 1; BAC15769).
FT                                {ECO:0000305}.
FT   CONFLICT    622    622       R -> W (in Ref. 1; BAC15769).
FT                                {ECO:0000305}.
FT   CONFLICT    631    631       T -> A (in Ref. 1; BAC15769).
FT                                {ECO:0000305}.
FT   CONFLICT    649    649       R -> W (in Ref. 5; BAC98205).
FT                                {ECO:0000305}.
SQ   SEQUENCE   861 AA;  97037 MW;  5C570D5A22414E14 CRC64;
     MEALGPGPPA SLFQPPRRPG LGTVGKPIRL LANHFQVQIP KIDVYHYDVD IKPEKRPRRV
     NREVVDTMVR HFKMQIFGDR QPGYDGKRNM YTAHPLPIGR DRIDMEVTLP GEGKDQTFKV
     SVQWVSVVSL QLLLEALAGH LNEVPDDSVQ ALDVITRHLP SMRYTPVGRS FFSPPEGYYH
     PLGGGREVWF GFHQSVRPAM WNMMLNIDVS ATAFYRAQPI IEFMCEVLDI QNINEQTKPL
     TDSQRVKFTK EIRGLKVEVT HCGQMKRKYR VCNVTRRPAS HQTFPLQLEN GQAMECTVAQ
     YFKQKYSLQL KHPHLPCLQV GQEQKHTYLP LEVCNIVAGQ RCIKKLTDNQ TSTMIKATAR
     SAPDRQEEIS RLVKSNSMVG GPDPYLKEFG IVVHNEMTEL TGRVLPAPML QYGGRNKTVA
     TPSQGVWDMR GKQFYAGIEI KVWAVACFAP QKQCREDLLK SFTDQLRKIS KDAGMPIQGQ
     PCFCKYAQGA DSVEPMFKHL KMTYVGLQLI VVILPGKTPV YAEVKRVGDT LLGMATQCVQ
     VKNVVKTSPQ TLSNLCLKMN AKLGGINNVL VPHQRPSVFQ QPVIFLGADV THPPAGDGKK
     PSIAAVVGSM DGHPSRYCAT VRVQTSRQEI TQELLYSQEV VQDLTSMARE LLIQFYKSTR
     FKPTRIIYYR GGVSEGQMKQ VAWPELIAIR KACISLEEDY RPGITYIVVQ KRHHTRLFCA
     DKMERVGKSG NVPAGTTVDS TVTHPSEFDF YLCSHAGIQG TSRPSHYQVL WDDNCFTADE
     LQLLTYQLCH TYVRCTRSVS IPAPAYYARL VAFRARYHLV DKDHDSAEGS HVSGQSNGRD
     PQALAKAVQI HHDTQHTMYF A
//
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