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Database: UniProt
Entry: Q6TV19
LinkDB: Q6TV19
Original site: Q6TV19 
ID   DICER_DANRE             Reviewed;        1865 AA.
AC   Q6TV19;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   13-NOV-2019, entry version 103.
DE   RecName: Full=Endoribonuclease Dicer;
DE            EC=3.1.26.3;
GN   Name=dicer1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 612-1865.
RX   PubMed=14528306; DOI=10.1038/ng1251;
RA   Wienholds E., Koudijs M.J., van Eeden F.J.M., Cuppen E.,
RA   Plasterk R.H.A.;
RT   "The microRNA-producing enzyme Dicer1 is essential for zebrafish
RT   development.";
RL   Nat. Genet. 35:217-218(2003).
CC   -!- FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a
CC       central role in short dsRNA-mediated post-transcriptional gene
CC       silencing. Cleaves naturally occurring long dsRNAs and short
CC       hairpin pre-microRNAs (miRNA) into fragments of twenty-one to
CC       twenty-three nucleotides with 3' overhang of two nucleotides,
CC       producing respectively short interfering RNAs (siRNA) and mature
CC       microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-
CC       induced silencing complex (RISC) to complementary RNAs to degrade
CC       them or prevent their translation. Gene silencing mediated by
CC       siRNAs, also called RNA interference, controls the elimination of
CC       transcripts from mobile and repetitive DNA elements of the genome
CC       but also the degradation of exogenous RNA of viral origin for
CC       instance. The miRNA pathway on the other side is a mean to
CC       specifically regulate the expression of target genes (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         EC=3.1.26.3;
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       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Component of the RISC loading complex (RLC), or micro-RNA
CC       (miRNA) loading complex (miRLC), which is composed of dicer1, ago2
CC       and tarbp2; dicer1 and tarbp2 are required to process precursor
CC       miRNAs (pre-miRNAs) to mature miRNAs and then load them onto ago2.
CC       Note that the trimeric RLC/miRLC is also referred to as RISC (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00657}.
DR   EMBL; AL772219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY386319; AAQ90464.1; -; mRNA.
DR   RefSeq; NP_001154925.1; NM_001161453.2.
DR   RefSeq; XP_005158722.1; XM_005158665.3.
DR   RefSeq; XP_005158723.1; XM_005158666.3.
DR   SMR; Q6TV19; -.
DR   STRING; 7955.ENSDARP00000045880; -.
DR   PaxDb; Q6TV19; -.
DR   PRIDE; Q6TV19; -.
DR   Ensembl; ENSDART00000045881; ENSDARP00000045880; ENSDARG00000001129.
DR   GeneID; 324724; -.
DR   KEGG; dre:324724; -.
DR   CTD; 23405; -.
DR   ZFIN; ZDB-GENE-030131-3445; dicer1.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   GeneTree; ENSGT00940000156287; -.
DR   HOGENOM; HOG000001567; -.
DR   InParanoid; Q6TV19; -.
DR   KO; K11592; -.
DR   OMA; YLMLFDP; -.
DR   OrthoDB; 1337630at2759; -.
DR   PhylomeDB; Q6TV19; -.
DR   TreeFam; TF330258; -.
DR   Reactome; R-DRE-203927; MicroRNA (miRNA) biogenesis.
DR   Reactome; R-DRE-426486; Small interfering RNA (siRNA) biogenesis.
DR   PRO; PR:Q6TV19; -.
DR   Proteomes; UP000000437; Chromosome 17.
DR   Bgee; ENSDARG00000001129; Expressed in 30 organ(s), highest expression level in retina.
DR   ExpressionAtlas; Q6TV19; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016442; C:RISC complex; ISS:UniProtKB.
DR   GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070883; F:pre-miRNA binding; IDA:ZFIN.
DR   GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR   GO; GO:0035195; P:gene silencing by miRNA; IMP:ZFIN.
DR   GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; IGI:ZFIN.
DR   GO; GO:0031054; P:pre-miRNA processing; IMP:ZFIN.
DR   GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:ZFIN.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; ISS:UniProtKB.
DR   GO; GO:0050767; P:regulation of neurogenesis; IMP:ZFIN.
DR   GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB.
DR   GO; GO:0021591; P:ventricular system development; IMP:ZFIN.
DR   CDD; cd00048; DSRM; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   Gene3D; 3.30.160.380; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003100; PAZ_dom.
DR   InterPro; IPR036085; PAZ_dom_sf.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02170; PAZ; 1.
DR   Pfam; PF00636; Ribonuclease_3; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 2.
DR   PROSITE; PS51327; DICER_DSRBF; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Endonuclease; Helicase;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding; RNA-mediated gene silencing.
FT   CHAIN         1   1865       Endoribonuclease Dicer.
FT                                /FTId=PRO_0000373985.
FT   DOMAIN       41    213       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      419    588       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      616    708       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      877   1028       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN     1262   1385       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1609   1767       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1792   1857       DRBM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
FT   NP_BIND      54     61       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       161    164       DECH box.
FT   COMPBIAS   1394   1402       Poly-Asp.
FT   METAL      1298   1298       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1377   1377       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1380   1380       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1648   1648       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL      1753   1753       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL      1756   1756       Magnesium or manganese 2. {ECO:0000250}.
FT   SITE       1749   1749       Important for activity. {ECO:0000250}.
FT   CONFLICT    739    751       IPECLRGCYPVPE -> VK (in Ref. 2;
FT                                AAQ90464). {ECO:0000305}.
FT   CONFLICT    921    921       R -> K (in Ref. 2; AAQ90464).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1865 AA;  210817 MW;  55B1700E719B2007 CRC64;
     MAGLQLVTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALEHNT IVCLNTGSGK
     TFIAVLLIKE LSHQIRGENG KRTVFLVNAA SSVAQQASTV RTHSDLQVGD YMSEDMTSWP
     EEMWNREMIE NQVLVMTCHI FLHVLKNGVL PLSKINLLVF DECHLAITGH PYREIMKICE
     GCPSCPRILG LTASILNGKC DPCDLEEKIQ NLEKILQSNA ETATDLVVLD RYASQPREEV
     LDCGQYQDQS GLSERLLNEL DEALNFLNDC NLSVHREDRD PTFISKQVLN DCRAVLTVLG
     PWCADKAAGI MVRELQKYIK HEQEELNRKF LLFTDTILRK IHALCEEHFS PASLDLKFVT
     PKVIRLLEIL HEYKPFERQQ FESVEWYNNR NQDNYVSWSD SEDDDEDEEA EAKEKTEANF
     PSPFTNILCG IIFVERRYTA VVLNRLIKEA GKQDPELAYI SSNFITGHSI GKNQPRNKQM
     EVEFRKQEEV LRKFRAHETN LLIATSIVEE GVDIPKCNLV VRFDLPTEYR SYVQSKGRAR
     APVSNYIMLA DSERTKTFQE DLKTYKAIEK ILRNKCSKSA ECNDFELEPV TDDDNVLPPY
     VLRSEDGGPR VTMNTAIGHV NRYCARLPSD PFTHLAPKCK TVEMNTGGYR STLFLPINSP
     LRVPVTGPVM NCARLAEKAV ALLCCEKLHK IGELDDHLMP VGKETVKYEE ELDLHDEEET
     SVPGRPGSTK RRQCSPKAIP ECLRGCYPVP EQPCYLYVIG MVLTTPLPDE LNFRRRKLYP
     PEDTTRCFGI LTAKPIPRIP HFPVYTRSGE VTISIELQKS GFSLSAEQLE LITRLHQYIF
     SHILRLEKPA LEFKPVEADS AYCVLPLNIV EDSNTLDLDF KFMEDIEKSE ARIGIPNTQY
     TKQNPFIFKL EDYQDAVIIP RYRNFDQPHR FYVADVYTDL TPLSKFPSPE YETFAEYYKT
     KYNLDLSNVN QPLLDVDHTS SRLNLLTPRH LNQKGKALPL SSAEKRKAKW ESLQNKQILV
     PELCAIHPIP ASLWRKAVCL PSILYRLHCL LTAEELRSQT AIDAGVGAQT LPPDFRYPNL
     DFGWKKSIDS KSFISCPSAC MEEDDDHCKL GTSSDSNHTA PESCSMEVSQ PPEGAPNTPD
     EKLETLTLPV TDLNKDCFPN LPNGTQADSD DLPHRSDVCQ CSQLGPLERD LSTQTTTSVS
     VRPSPAGEPQ PWPSDECTGR SSDLCDPHVK KPTSKHCPKS ETATSTPAPS ETSSEDCRSA
     CAGPAWDSPK TLGPNPGLIL QALTLSNASD GFNLERLEML GDSFLKHAIT TYLFCTYPDA
     HEGRLSYMRS KKVSNCNLYR LGKKKGLPSR MVVSIFDPPV NWLPPGYVVN QDKSSTDKWD
     SDENKDLANG KASDDEDEDD DDEPEEAEVE PSKEDVNVED DLEYYYEHIR FIDSMLIGSG
     AFGKKISLQP TDPGYEWKAP KKAHNSHFSP DGGADEFDYS SWDAMCYLDP SKAGEEDDFV
     VGFWNPSEEN CGTDIGKQSI SYDLHTEQCI ADKSIADCVE ALLGCYLTSC GERAAQLFLC
     SLGLKVLPPE KQSSGGSAEL QYGWLKIPPR CMFEHPDAER TLNHLISGFL NFESKINYTF
     KNKAYLLQAF THASYHYNTI TDCYQRLEFL GDAILDYLIT KHLYEDPRQH SPGVLTDLRS
     ALVNNTIFAS LAVKYDYHKY FKAVSPELFH VIDDFVQFQL EKNEMQGMDS ELRRSEEDEE
     KEEDIEVPKA MGDIFESLAG AIYMDSGMSL ETVWQVYYPM MRPLIEKFSA NVPRSPVREL
     LEMEPETAKF SPAERTYDGK VRVTVEVVGK GKFKGVGRSY RIAKSAAARR ALRSLKANQP
     QVQNN
//
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