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Database: UniProt
Entry: P34529
LinkDB: P34529
Original site: P34529 
ID   DCR1_CAEEL              Reviewed;        1910 AA.
AC   P34529;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   16-OCT-2019, entry version 169.
DE   RecName: Full=Endoribonuclease dcr-1;
DE            EC=3.1.26.- {ECO:0000269|PubMed:11641272, ECO:0000269|PubMed:20223951};
DE   Contains:
DE     RecName: Full=Death-promoting deoxyribonuclease {ECO:0000305|PubMed:20223951};
DE              Short=tDCR-1 {ECO:0000303|PubMed:20223951};
DE              EC=3.1.21.- {ECO:0000269|PubMed:20223951};
GN   Name=dcr-1 {ECO:0000303|PubMed:11641272};
GN   ORFNames=K12H4.8 {ECO:0000312|WormBase:K12H4.8};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
RA   Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
RA   Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
RA   Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
RA   Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
RA   Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
RA   Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
RA   Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
RA   Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
RA   Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J.,
RA   Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11641272; DOI=10.1101/gad.927801;
RA   Ketting R.F., Fischer S.E.J., Bernstein E., Sijen T., Hannon G.J.,
RA   Plasterk R.H.A.;
RT   "Dicer functions in RNA interference and in synthesis of small RNA
RT   involved in developmental timing in C. elegans.";
RL   Genes Dev. 15:2654-2659(2001).
RN   [4]
RP   INTERACTION WITH PIR-1.
RX   PubMed=16439208; DOI=10.1016/j.cell.2005.11.036;
RA   Duchaine T.F., Wohlschlegel J.A., Kennedy S., Bei Y., Conte D. Jr.,
RA   Pang K., Brownell D.R., Harding S., Mitani S., Ruvkun G.,
RA   Yates J.R. III, Mello C.C.;
RT   "Functional proteomics reveals the biochemical niche of C. elegans
RT   DCR-1 in multiple small-RNA-mediated pathways.";
RL   Cell 124:343-354(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PROTEOLYTIC CLEAVAGE,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-1537; GLU-1682; ASP-1686
RP   AND GLU-1794.
RX   PubMed=20223951; DOI=10.1126/science.1182374;
RA   Nakagawa A., Shi Y., Kage-Nakadai E., Mitani S., Xue D.;
RT   "Caspase-dependent conversion of Dicer ribonuclease into a death-
RT   promoting deoxyribonuclease.";
RL   Science 328:327-334(2010).
CC   -!- FUNCTION: Involved in cleaving double-stranded RNA in the RNA
CC       interference (RNAi) pathway (PubMed:11641272, PubMed:20223951). It
CC       produces 21 to 23 bp dsRNAs (siRNAs) which target the selective
CC       destruction of homologous RNAs (PubMed:11641272, PubMed:20223951).
CC       Seems to process the precursor of the small temporal RNA let-7
CC       which is involved in developmental timing (PubMed:11641272).
CC       {ECO:0000269|PubMed:11641272, ECO:0000269|PubMed:20223951}.
CC   -!- FUNCTION: tDCR-1 acts as a deoxyribonuclease (DNase) initiating
CC       DNA fragmentation during apoptosis, upstream of nucleases cps-6,
CC       crn-2 and nuc-1. {ECO:0000269|PubMed:20223951}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:20223951};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPY3};
CC   -!- SUBUNIT: May interact with pir-1. {ECO:0000269|PubMed:16439208}.
CC   -!- INTERACTION:
CC       G5EDI8:drh-1; NbExp=9; IntAct=EBI-326716, EBI-327837;
CC       O44406:eri-1; NbExp=4; IntAct=EBI-326716, EBI-863689;
CC       Q9GZI7:eri-3; NbExp=5; IntAct=EBI-326716, EBI-866569;
CC       Q95XS0:eri-5; NbExp=8; IntAct=EBI-326716, EBI-866573;
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a cps-6 mutant
CC       background reduces the number of DNA breaks in embryonic cells
CC       undergoing apoptosis. {ECO:0000269|PubMed:20223951}.
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000305}.
DR   EMBL; FO081380; CCD71200.2; -; Genomic_DNA.
DR   PIR; S44849; S44849.
DR   RefSeq; NP_498761.2; NM_066360.3.
DR   BioGrid; 41344; 39.
DR   DIP; DIP-25340N; -.
DR   IntAct; P34529; 88.
DR   STRING; 6239.K12H4.8; -.
DR   EPD; P34529; -.
DR   PaxDb; P34529; -.
DR   PeptideAtlas; P34529; -.
DR   PRIDE; P34529; -.
DR   EnsemblMetazoa; K12H4.8.1; K12H4.8.1; WBGene00000939.
DR   EnsemblMetazoa; K12H4.8.2; K12H4.8.2; WBGene00000939.
DR   GeneID; 176138; -.
DR   KEGG; cel:CELE_K12H4.8; -.
DR   UCSC; K12H4.8; c. elegans.
DR   CTD; 42693; -.
DR   WormBase; K12H4.8; CE47418; WBGene00000939; dcr-1.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   GeneTree; ENSGT00940000156287; -.
DR   HOGENOM; HOG000022395; -.
DR   InParanoid; P34529; -.
DR   KO; K11592; -.
DR   OMA; YLMLFDP; -.
DR   OrthoDB; 1337630at2759; -.
DR   Reactome; R-CEL-203927; MicroRNA (miRNA) biogenesis.
DR   Reactome; R-CEL-426486; Small interfering RNA (siRNA) biogenesis.
DR   PRO; PR:P34529; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000939; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005829; C:cytosol; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0016442; C:RISC complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004530; F:deoxyribonuclease I activity; IDA:WormBase.
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; IDA:WormBase.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IGI:WormBase.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:WormBase.
DR   GO; GO:0031050; P:dsRNA processing; IDA:WormBase.
DR   GO; GO:0035262; P:gonad morphogenesis; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0008355; P:olfactory learning; IMP:WormBase.
DR   GO; GO:2000636; P:positive regulation of primary miRNA processing; IMP:WormBase.
DR   GO; GO:0031054; P:pre-miRNA processing; IMP:WormBase.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IMP:WormBase.
DR   GO; GO:0040034; P:regulation of development, heterochronic; IMP:WormBase.
DR   GO; GO:0000003; P:reproduction; IMP:WormBase.
DR   GO; GO:0006401; P:RNA catabolic process; IDA:WormBase.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
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   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
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; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF03368; Dicer_dimer; 1.
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; 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   1: Evidence at protein level;
KW   Apoptosis; ATP-binding; Coiled coil; Complete proteome; Endonuclease;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding;
KW   RNA-mediated gene silencing.
FT   CHAIN         1   1910       Endoribonuclease dcr-1.
FT                                /FTId=PRO_0000180473.
FT   CHAIN      1538   1910       Death-promoting deoxyribonuclease.
FT                                {ECO:0000305}.
FT                                /FTId=PRO_0000441121.
FT   DOMAIN       20    201       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      371    542       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      571    667       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      847   1003       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN     1381   1589       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1643   1805       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1833   1896       DRBM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
FT   NP_BIND      33     40       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED     1245   1280       {ECO:0000255}.
FT   MOTIF       145    148       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   METAL      1682   1682       Magnesium or manganese.
FT                                {ECO:0000305|PubMed:20223951}.
FT   METAL      1791   1791       Magnesium or manganese.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   METAL      1794   1794       Magnesium or manganese.
FT                                {ECO:0000305|PubMed:20223951}.
FT   SITE       1537   1538       Cleavage; by ced-3.
FT                                {ECO:0000269|PubMed:20223951}.
FT   SITE       1787   1787       Important for activity.
FT                                {ECO:0000250|UniProtKB:Q8R418}.
FT   MUTAGEN    1537   1537       D->E: Loss of cleavage by ced-3. Loss of
FT                                deoxyribonuclease (DNase) activity.
FT                                Reduced number of cell corpses in
FT                                embryos. {ECO:0000269|PubMed:20223951}.
FT   MUTAGEN    1682   1682       E->A: Severe reduction in both dsRNA
FT                                dicing and DNase activities; when
FT                                associated with A-1794. Loss of dsRNA
FT                                dicing and DNase activities, bursting and
FT                                protruding vulva and reduction in the
FT                                number of cell corpses in embryos; when
FT                                associated with A-1794 and A-1686.
FT                                {ECO:0000269|PubMed:20223951}.
FT   MUTAGEN    1686   1686       D->A: Loss of dsRNA dicing and DNase
FT                                activities, bursting and protruding vulva
FT                                and reduction in the number of cell
FT                                corpses in embryos; when associated with
FT                                A-1794 and A-1682.
FT                                {ECO:0000269|PubMed:20223951}.
FT   MUTAGEN    1794   1794       E->A: Severe reduction in both dsRNA
FT                                dicing and DNase activities; when
FT                                associated with A-1682. Loss of dsRNA
FT                                dicing and DNase activities, bursting and
FT                                protruding vulva and reduction in the
FT                                number of cell corpses in embryos; when
FT                                associated with A-1682 and A-1686.
FT                                {ECO:0000269|PubMed:20223951}.
SQ   SEQUENCE   1910 AA;  218423 MW;  B49D19D7B3730F80 CRC64;
     MVRVRADLQC FNPRDYQVEL LDKATKKNTI VQLGTGSGKT FIAVLLLKEY GVQLFAPLDQ
     GGKRAFFVVE KVNLVEQQAI HIEVHTSFKV GQVHGQTSSG LWDSKEQCDQ FMKRHHVVVI
     TAQCLLDLIR HAYLKIEDMC VLIFDECHHA LGSQHPYRSI MVDYKLLKKD KPVPRVLGLT
     ASLIKAKVAP EKLMEQLKKL ESAMDSVIET ASDLVSLSKY GAKPYEVVII CKDFEIGCLG
     IPNFDTVIEI FDETVAFVNT TTEFHPDLDL DPRRPIKDSL KTTRAVFRQL GPWAAWRTAQ
     VWEKELGKII KSQVLPDKTL RFLNMAKTSM ITIKRLLEPE MKKIKSIEAL RPYVPQRVIR
     LFEILETFNP EFQKERMKLE KAEHLSAIIF VDQRYIAYSL LLMMRHIKSW EPKFKFVNPD
     YVVGASGRNL ASSDSQGLHK RQTEVLRRFH RNEINCLIAT SVLEEGVDVK QCNLVIKFDR
     PLDMRSYVQS KGRARRAGSR YVITVEEKDT AACDSDLKDF QQIEKILLSR HRTVNNPIED
     DSDRFEEFDV DSQMEPYVVE KTGATLKMST AIALINRYCS KLPSDIFTRL VPHNQIIPIE
     ENGVTKYCAE LLLPINSPIK HAIVLKNPMP NKKTAQMAVA LEACRQLHLE GELDDNLLPK
     GRESIAKLLE HIDEEPDEYA PGIAAKVGSS KRKQLYDKKI ARALNESFVE ADKECFIYAF
     ELERFREAEL TLNPKRRKFE DPFNYEYCFG FLSAKEIPKI PPFPVFLRQG NMKVRLIVAP
     KKTTVTAAQL QEIQLFHNYL FTQVLQMCKT GNLEFDGTSN APLNTLIVPL NKRKDDMSYT
     INMKYVSEVV ANMENMPRIP KDEVRRQYKF NAEDYKDAIV MPWYRNLEQP VFYYVAEILP
     EWRPSSKFPD THFETFNEYF IKKYKLEIYD QNQSLLDVDF TSTRLNLLQP RIQNQPRRSR
     TVSNSSTSNI PQASASDSKE SNTSVPHSSQ RQILVPELMD IHPISATLWN VIAALPSIFY
     RVNQLLLTDE LRETILVKAF GKEKTKLDDN VEWNSLAYAT EYEEKQTIIV KKIQQLRDLN
     QKSIEDQERE TRENDKIDDG EELFNIGVWD PEEAVRIGVE ISSRDDRMDG EDQDTVGLTQ
     GLHDGNISDE DDELPFVMHD YTARLTSNRN GIGAWSGSES IVPSGWGDWD GPEPDNSPMP
     FQILGGPGGL NVQALMADVG RVFDPSTASS SLSQTVQEST VSPPKQLTKE EEQFKKLQND
     LLKQAKERLE ALEMSEDMEK PRRLEDTVNL EDYGDDQENQ EDENTPTNFP KTIDEEIEEL
     SIGARKKQEI DDNAAKTDVL ERENCEVLPV AINEKSRSFS FEKESKAING RLIRQRSEEY
     VSHIDSDIGL GVSPCLLLTA LTTSNAADGM SLERFETIGD SFLKFATTDY LYHTLLDQHE
     GKLSFARSKE VSNCNLYRLG KKLGIPQLIV ANKFDAHDSW LPPCYIPTCD FKAPNTDDAE
     EKDNEIERIL DGQVIEEKPE NKTGWDIGGD VSKSTTDGIE TITFPKQARV GNDDISPLPY
     NLLTQQHISD KSIADAVEAL IGVHLLTLGP NPTLKVMNWM GLKVIQKDQK SDVPSPLLRF
     IDTPTNPNAS LNFLNNLWQQ FQFTQLEEKI GYRFKERAYL VQAFTHASYI NNRVTGCYQR
     LEFLGDAVLD YMITRYLFED SRQYSPGVLT DLRSALVNNT IFASLAVKFE FQKHFIAMCP
     GLYHMIEKFV KLCSERNFDT NFNAEMYMVT TEEEIDEGQE EDIEVPKAMG DIFESVAGAI
     YLDSGRNLDT TWQVIFHMMR GTIELCCANP PRSPIRELME FEQSKVRFSK MERILESGKV
     RVTVEVVNNM RFTGMGRNYR IAKATAAKRA LKYLHQIEQQ RRQSPSLTTV
//
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