DICER_BOVIN
ID DICER_BOVIN Reviewed; 1923 AA.
AC Q6TUI4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Endoribonuclease Dicer;
DE EC=3.1.26.3;
GN Name=DICER1; Synonyms=DICER;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Golding M.C., Long C.R., Westhusin M.E.;
RT "Overexpression of bovine Dicer in mammalian cells.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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 hairpin
CC pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three
CC nucleotides with 3' overhang of two nucleotides, producing respectively
CC short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs
CC serve as guide to direct the RNA-induced silencing complex (RISC) to
CC complementary RNAs to degrade them or prevent their translation. Gene
CC silencing mediated by siRNAs, also called RNA interference, controls
CC the elimination of transcripts from mobile and repetitive DNA elements
CC of the genome but also the degradation of exogenous RNA of viral origin
CC for instance. The miRNA pathway on the other side is a mean to
CC specifically regulate the expression of target genes (By similarity).
CC {ECO:0000250|UniProtKB:Q9UPY3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; 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. {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 and
CC TARBP2; DICER1 and TARBP2 are required to process precursor miRNAs
CC (pre-miRNAs) to mature miRNAs and then load them onto AGO2. Note that
CC the trimeric RLC/miRLC is also referred to as RISC. Interacts with
CC DHX9, AGO1, PIWIL1 and PRKRA. Interacts with AGO2, TARBP2, EIF6, MOV10
CC and RPL7A (60S ribosome subunit); they form a large RNA-induced
CC silencing complex (RISC). Interacts with BCDIN3D (By similarity).
CC Interacts (via Dicer dsRNA-binding fold domain) with ALOX5 (via PLAT
CC domain); this interaction enhances arachidonate 5-lipoxygenase activity
CC and modifies the miRNA precursor processing activity of DICER1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9UPY3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPY3}.
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AY386968; AAR26432.1; -; mRNA.
DR RefSeq; NP_976235.1; NM_203359.1.
DR AlphaFoldDB; Q6TUI4; -.
DR SMR; Q6TUI4; -.
DR STRING; 9913.ENSBTAP00000017080; -.
DR PaxDb; Q6TUI4; -.
DR PRIDE; Q6TUI4; -.
DR GeneID; 337871; -.
DR KEGG; bta:337871; -.
DR CTD; 23405; -.
DR eggNOG; KOG0701; Eukaryota.
DR InParanoid; Q6TUI4; -.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
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:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; ISS:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0030422; P:siRNA processing; ISS:UniProtKB.
DR CDD; cd10843; DSRM_DICER; 1.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR Gene3D; 3.30.160.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR044441; DICER_DSRM.
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; 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; Cytoplasm; Endonuclease; Helicase; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..1923
FT /note="Endoribonuclease Dicer"
FT /id="PRO_0000373982"
FT DOMAIN 51..227
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 433..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 629..721
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 890..1041
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 1276..1404
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1667..1825
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1853..1915
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 256..595
FT /note="Required for interaction with PRKRA and TARBP2"
FT /evidence="ECO:0000250"
FT REGION 410..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..178
FT /note="DECH box"
FT COMPBIAS 412..427
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1396
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1399
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1706
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1811
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1814
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 1807
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY3"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY3"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY3"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY3"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY3"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R418"
FT MOD_RES 1471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY3"
FT MOD_RES 1869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY3"
SQ SEQUENCE 1923 AA; 218258 MW; 3580CB8537484BAE CRC64;
MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT
IVCLNTGSGK TFIAVLLTKE LSYQIRGDFN RNGKRTVFLV NSANQVAQQV SAVRTHSDLK
VGEYSNLEVS ASWTKEKWNQ EFTKHQVLIM TCYVALNVLK NGYLSLSDIN LLVFDECHLA
ILDHPYREIM KLCENCPSCP RILGLTASIL NGKCDPEELE EKIQKLEKIL KSNAETATDL
VVLDRYTSQP CEIVVDCGPF TDRSGLYERL LMELEEALNF INDCNISVHS KERDSTLISK
QILSDCRAVL VVLGPWCADK VAGMMVRELQ KHIKHEQEEL HRKFLLFTDT FLRKIHALCE
EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDEE
DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT
GHGIGKNQPR NKQMEAEFRK QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP
TEYRSYVQSK GRARAPISNY VMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTGEAD
TEPVVDDDDV FPPYVLRPED GPRVTINTAI GHVNRYCARL PSDPFTHLAP KCRTRELPDG
TFYSTLYLPI NSPLRASIVG PPMSCIRLAE RVVALICCEK LHKIGELDDH LMPVGKETVK
YEEELDLHDE EETSVPGRPG STKRRQCYPK AIPECLRESY PRPGQPCYLY VIGMVLTTPL
PDELNFRRRK LYPPEDTTRC FGILTAKPIP QIPHFPVYTR SGEVTISIEL KKSGFTLSLQ
MLELITRLHQ YIFSHILRLE KPALEFKPTD ADSAYCVLPL NVVNDSSTLD IDFKFMEDIE
KSEARIGIPS TKYSKETPFV FKLEDYQDAV IIPRYRNFDQ PHRFYVADVY TDLTPLSKFP
SPEYETFAEY YKTKYNLDLT NLNQPLLDVD HTSSRLNLLT PRHLNQKGKA LPLSSAEKRK
AKWESLQNKQ ILVPELCAIH PIPASLWRKA VCLPSILYRL HCLLTAEELR AQTASDAGVG
VRSLPVDFRY PNLDFGWKKS IDSKSFISIA NSSSAENENY CKHSTIVVPE NAAHQGANRT
SPLENHDQMS VNCRTLFSES PGKLQIEVST DLTAINGLSY NKSLANGSYD LANRDFCQGN
HLNYYKQEIP VQPTTSYPIQ NLYNYENQPK PSDECTLLSN KYLDGNANTS TSDGSPVTAA
VPGTTETGEA PPDRTASEQS PSPGYSSRTL GPNPGLILQA LTLSNASDGF NLERLEMLGD
SFLKHAITTV SLSALILDAH EGRLSYMRSK KVSNCNLYRL GKKKGLPSRM VVSIFDPPVN
GLPPGYVVNQ DKSNTEKWEK DEMTKDCMLA NGKLDDDFEE EEEEEEDLMW RAHKEDADDE
DDFLEYDQEH IKFIDNMLMG SGAFVKKISL SPFSATDSAY EWKMPKKSSL GSLPFSSDFE
DFDYSSWDAM CYLDPSKAVE EDDFVVGFWN PSEENCGVDT GKQSISYDLH TEQCIADKSI
ADCVEALLGC YLTSCGERAA QLFLCSLGLK VLPVIKRTDR EKAMCPTREN FTSQQKNLSG
SRAAASGAGY RASVLKDLEY GCLKIPPRCM FDHPEADRTL RHLISGFENF EKKINYRFKN
KAYLLQAFTH ASYHYNTITD CYQRLEFLGD AILDYLITKH LYEDPRQHSP GVLTDLRSAL
VNNTIFASLA VKYDYHKYFK AVSPELFHVI DDFVQFQLEK NEMQGMDSEL RRSEEDEEKE
EDIEVPKAMG DIFESLAGAI YMDSGMSLET VWQVYYPMMR PLIEKFSANV PRSPVRELLE
MEPEITKFSP AERTYDGKVR VTVEVVGKGK FKGVGRSYRI AKSAAARRAL RSLKANQPQV
PNS
