DICER_CHICK
ID DICER_CHICK Reviewed; 1921 AA.
AC Q25BN1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Endoribonuclease Dicer;
DE EC=3.1.26.3;
GN Name=DICER1; Synonyms=DICER;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15247924; DOI=10.1038/ncb1155;
RA Fukagawa T., Nogami M., Yoshikawa M., Ikeno M., Okazaki T., Takami Y.,
RA Nakayama T., Oshimura M.;
RT "Dicer is essential for formation of the heterochromatin structure in
RT vertebrate cells.";
RL Nat. Cell Biol. 6:784-791(2004).
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}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AB253768; BAE87103.1; -; mRNA.
DR RefSeq; NP_001035555.1; NM_001040465.1.
DR AlphaFoldDB; Q25BN1; -.
DR SMR; Q25BN1; -.
DR STRING; 9031.ENSGALP00000036777; -.
DR PaxDb; Q25BN1; -.
DR GeneID; 423437; -.
DR KEGG; gga:423437; -.
DR CTD; 23405; -.
DR VEuPathDB; HostDB:geneid_423437; -.
DR eggNOG; KOG0701; Eukaryota.
DR InParanoid; Q25BN1; -.
DR OrthoDB; 1337630at2759; -.
DR PhylomeDB; Q25BN1; -.
DR PRO; PR:Q25BN1; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; IEA:InterPro.
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; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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: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; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR044441; DICER_DSRM.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF04851; ResIII; 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..1921
FT /note="Endoribonuclease Dicer"
FT /id="PRO_0000373984"
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 630..722
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 891..1042
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 1277..1404
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1665..1823
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1848..1913
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 409..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1782..1801
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 BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1317
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 1704
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1809
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1812
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 1805
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1921 AA; 218610 MW; E1F9C9BE1D8CD611 CRC64;
MKSPALQSLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT
IVCLNTGSGK TFIAVLLTKE LSYQIRGDFN KNGKRTVFLV NSANQVAQQV SAVRTHSDLK
VGEYSSLEVT ESWTKEKWSQ EFSKHQVLVM TCHVALTVLR NEYLSLSNIN LLVFDECHLA
IQDHPYREIM KICEDYPSCP RILGLTASIL NGKCDPAELE EKIKKLEKIL KSNAETATDL
VVLDRYTSQP CEIVVDCGPY TDKSGLYGRL LRELDEALHF LNDCNISVHS KERDSTLISK
QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT FLRKIHALCE
EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDDE
DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT
GHGIGKNQPR NKQMEVEFRK QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP
TEYRSYVQSK GRARAPISNY IMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTSETE
TEPIVDDDDV FPPYVLRTDE NSPRVTINTA IGHINRYCAR LPSDPFTHLA PKCKTRELPD
HTFYSTLYLP INSPLRASIV GPPMSCARLA ERVVALICCE KLHKIGELDD HLMPVGKETV
KYEEELDLHD EEETSVPGRP GSTKRRQCYP KAIPECLRDS YPKPDQPCYL YVIGMVLTTP
LPDELNFRRR KLYPPEDTTR CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFTLSL
QMLELITRLH QYIFSHILRL EKPALEFKPT EADSAYCVLP LNIVDDSSTL DIDFKFMEDI
EKSEARTGIP STQYTKEMPF IFKLEDYQDA VIIPRYRNFD QPHRFYVADV YTDLTPLSKF
PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL TPRHLNQKGK ALPLSSAEKR
KAKWESLQNK QILVPELCAI HPIPASLWRK AVCLPSILYR LHCLLTAEEL RAQTATDAGV
GVKSLPADFR YPNLDFGWKK SIDSKSFISI PSSSLVENEN YCKHSTIVVP ENAAHQGANR
TSSAEKHDQM SVSYRTLLDE SPSKLQIDVS AELAAINGVS YNKNLANGNC DLVNRDFCQG
NQLNYCRQEI PVQPTTSYPI QNLYSSENQP KPSNECTLLS NKYLDGNANR STSDGCPKMT
VTTSTSTALN LSKDKVDSEK NTSSGYSSKT LGPNPGLILQ ALTLSNASDG FNLERLEMLG
DSFLKHAITT YLFCTYPDAH EGRLSYMRSK KVSNCNLYRL GKKKGLPSRM VVSIFDPPVN
WLPPGYIVNQ DKSNTDKWEK EETTKENLLA NGKLDYDDDD EEDEDLMWRL PKEETDFEDD
FLEYDQEHIK FIDSMLMGSG AFVKKISLSH FSTTDSNYEW KAPKKSSLGN VPFSSDFDDF
DYSSWDAMCY LDPSKAVEED DFVVGFWNPS EENCGVDAGK QSISYDLHTE QCIADKSIAD
CVEALLGCYL TSCGERAAQL FLCSLGLKVL PVIKKTDWES TLCATGENCN SEQKNLSPNS
VSACIVNSEP SLYKDLEYGC LKIPPRCMFD HPDAEKTLNH LISGFENFEK KINYSFKNKA
YLLQAFTHAS YHYNTITDCY QRLEFLGDAI LDYLITKHLY EDPRQHSPGV LTDLRSALVN
NTIFASLAVK YDYHKYFKAV SPELFHVIDD FVQFQMEKNE MQGMDSELRR SEEDEEKEED
IEVPKAMGDI FESLAGAIYM DSGMSLEMVW QVYYPMMRPL IEKFSANVPR SPVRELLEME
PETAKFSPAE RTYDGKVRVT VEVVGKGKFK GVGRSYRIAK SAAARRALRS LKANQPQVPN
S
