Reviewed, UniProtKB/Swiss-Prot Q9VCU9 (DCR1_DROME)

Names and origin

Protein names

Recommended name:
    Endoribonuclease Dcr-1
      Short name=Protein dicer-1
    EC=3.1.26.-

Gene names

Name:	Dcr-1
ORF Names:	CG4792

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	2249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential for RNA interference (RNAi); double-stranded RNA (dsRNA) induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger. May carry out the initiation step of RNAi by cleaving dsRNA to produce 22 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs. Ref.4 Ref.5
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Interacts with AGO2 to form components of the RISC. Interacts with Fmr1 to form a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are mRpL5, mRpL11, AGO2 and Rm62. Ref.5 Ref.6
Sequence similarities	Belongs to the helicase family. Dicer subfamily. Contains 1 Dicer dsRNA-binding fold domain. Contains 1 DRBM (double-stranded RNA-binding) domain. Contains 1 helicase C-terminal domain. Contains 1 PAZ domain. Contains 2 RNase III domains.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing
Domain	Repeat
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Endonuclease Helicase Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA interference, production of siRNA Ref.4 Ref.6 Inferred from direct assay. Source: UniProtKB RNA interference, siRNA loading onto RISC Inferred from mutant phenotype. Source: FlyBase dsRNA transport Inferred from mutant phenotype. Source: FlyBase germ-line stem cell division Inferred from mutant phenotype. Source: FlyBase mitotic cell cycle, embryonic Inferred from mutant phenotype. Source: FlyBase pole cell formation Inferred from mutant phenotype. Source: FlyBase pre-microRNA processing Inferred from direct assay. Source: FlyBase segment polarity determination Inferred from genetic interaction. Source: FlyBase
Cellular component	RNA-induced silencing complex Inferred from direct assay. Source: FlyBase cytoplasm Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW bidentate ribonuclease III activity Ref.4 Inferred from direct assay. Source: FlyBase double-stranded RNA binding Inferred from electronic annotation. Source: InterPro helicase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.5 Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGO2	Q9VUQ5	1	EBI-112170,EBI-442476
Fmr1	Q9NFU0	1	EBI-112170,EBI-422631

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2249	2249	Endoribonuclease Dcr-1		PRO_0000180474
Regions
	Domain	485 – 648	164	Helicase C-terminal
	Domain	825 – 920	96	Dicer dsRNA-binding fold
	Domain	1099 – 1246	148	PAZ
	Domain	1698 – 1919	222	RNase III 1
	Domain	1993 – 2150	158	RNase III 2
	Domain	2175 – 2241	67	DRBM
	Nucleotide binding	37 – 44	8	ATP Potential
Sites
	Metal binding	2032	1	Magnesium or manganese By similarity
	Metal binding	2136	1	Magnesium or manganese By similarity
	Metal binding	2139	1	Magnesium or manganese By similarity
	Site	2132	1	Important for activity By similarity
Amino acid modifications
	Modified residue	1423	1	Phosphoserine Ref.7
	Modified residue	1877	1	Phosphoserine Ref.7
	Modified residue	1880	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	1338 – 1339	2	PT → AI Ref.3
	Sequence conflict	1345	1	L → I Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9VCU9-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D693F0432AC8033D	FASTA	2,249	255,330
	10 20 30 40 50 60 MAFHWCDNNL HTTVFTPRDF QVELLATAYE RNTIICLGHR SSKEFIALKL LQELSRRARR 70 80 90 100 110 120 HGRVSVYLSC EVGTSTEPCS IYTMLTHLTD LRVWQEQPDM QIPFDHCWTD YHVSILRPEG 130 140 150 160 170 180 FLYLLETREL LLSSVELIVL EDCHDSAVYQ RIRPLFENHI MPAPPADRPR ILGLAGPLHS 190 200 210 220 230 240 AGCELQQLSA MLATLEQSVL CQIETASDIV TVLRYCSRPH EYIVQCAPFE MDELSLVLAD 250 260 270 280 290 300 VLNTHKSFLL DHRYDPYEIY GTDQFMDELK DIPDPKVDPL NVINSLLVVL HEMGPWCTQR 310 320 330 340 350 360 AAHHFYQCNE KLKVKTPHER HYLLYCLVST ALIQLYSLCE HAFHRHLGSG SDSRQTIERY 370 380 390 400 410 420 SSPKVRRLLQ TLRCFKPEEV HTQADGLRRM RHQVDQADFN RLSHTLESKC RMVDQMDQPP 430 440 450 460 470 480 TETRALVATL EQILHTTEDR QTNRSAARVT PTPTPAHAKP KPSSGANTAQ PRTRRRVYTR 490 500 510 520 530 540 RHHRDHNDGS DTLCALIYCN QNHTARVLFE LLAEISRRDP DLKFLRCQYT TDRVADPTTE 550 560 570 580 590 600 PKEAELEHRR QEEVLKRFRM HDCNVLIGTS VLEEGIDVPK CNLVVRWDPP TTYRSYVQCK 610 620 630 640 650 660 GRARAAPAYH VILVAPSYKS PTVGSVQLTD RSHRYICATG DTTEADSDSD DSAMPNSSGS 670 680 690 700 710 720 DPYTFGTARG TVKILNPEVF SKQPPTACDI KLQEIQDELP AAAQLDTSNS SDEAVSMSNT 730 740 750 760 770 780 SPSESSTEQK SRRFQCELSS LTEPEDTSDT TAEIDTAHSL ASTTKDLVHQ MAQYREIEQM 790 800 810 820 830 840 LLSKCANTEP PEQEQSEAER FSACLAAYRP KPHLLTGASV DLGSAIALVN KYCARLPSDT 850 860 870 880 890 900 FTKLTALWRC TRNERAGVTL FQYTLRLPIN SPLKHDIVGL PMPTQTLARR LAALQACVEL 910 920 930 940 950 960 HRIGELDDQL QPIGKEGFRA LEPDWECFEL EPEDEQIVQL SDEPRPGTTK RRQYYYKRIA 970 980 990 1000 1010 1020 SEFCDCRPVA GAPCYLYFIQ LTLQCPIPEE QNTRGRKIYP PEDAQQGFGI LTTKRIPKLS 1030 1040 1050 1060 1070 1080 AFSIFTRSGE VKVSLELAKE RVILTSEQIV CINGFLNYTF TNVLRLQKFL MLFDPDSTEN 1090 1100 1110 1120 1130 1140 CVFIVPTVKA PAGGKHIDWQ FLELIQANGN TMPRAVPDEE RQAQPFDPQR FQDAVVMPWY 1150 1160 1170 1180 1190 1200 RNQDQPQYFY VAEICPHLSP LSCFPGDNYR TFKHYYLVKY GLTIQNTSQP LLDVDHTSAR 1210 1220 1230 1240 1250 1260 LNFLTPRYVN RKGVALPTSS EETKRAKREN LEQKQILVPE LCTVHPFPAS LWRTAVCLPC 1270 1280 1290 1300 1310 1320 ILYRINGLLL ADDIRKQVSA DLGLGRQQIE DEDFEWPMLD FGWSLSEVLK KSRESKQKES 1330 1340 1350 1360 1370 1380 LKDDTINGKD LADVEKKPTS EETQLDKDSK DDKVEKSAIE LIIEGEEKLQ EADDFIEIGT 1390 1400 1410 1420 1430 1440 WSNDMADDIA SFNQEDDDED DAFHLPVLPA NVKFCDQQTR YGSPTFWDVS NGESGFKGPK 1450 1460 1470 1480 1490 1500 SSQNKQGGKG KAKGPAKPTF NYYDSDNSLG SSYDDDDNAG PLNYMHHNYS SDDDDVADDI 1510 1520 1530 1540 1550 1560 DAGRIAFTSK NEAETIETAQ EVEKRQKQLS IIQATNANER QYQQTKNLLI GFNFKHEDQK 1570 1580 1590 1600 1610 1620 EPATIRYEES IAKLKTEIES GGMLVPHDQQ LVLKRSDAAE AQVAKVSMME LLKQLLPYVN 1630 1640 1650 1660 1670 1680 EDVLAKKLGD RRELLLSDLV ELNADWVARH EQETYNVMGC GDSFDNYNDH HRLNLDEKQL 1690 1700 1710 1720 1730 1740 KLQYERIEIE PPTSTKAITS AILPAGFSFD RQPDLVGHPG PSPSIILQAL TMSNANDGIN 1750 1760 1770 1780 1790 1800 LERLETIGDS FLKYAITTYL YITYENVHEG KLSHLRSKQV ANLNLYRLGR RKRLGEYMIA 1810 1820 1830 1840 1850 1860 TKFEPHDNWL PPCYYVPKEL EKALIEAKIP THHWKLADLL DIKNLSSVQI CEMVREKADA 1870 1880 1890 1900 1910 1920 LGLEQNGGAQ NGQLDDSNDS CNDFSCFIPY NLVSQHSIPD KSIADCVEAL IGAYLIECGP 1930 1940 1950 1960 1970 1980 RGALLFMAWL GVRVLPITRQ LDGGNQEQRI PGSTKPNAEN VVTVYGAWPT PRSPLLHFAP 1990 2000 2010 2020 2030 2040 NATEELDQLL SGFEEFEESL GYKFRDRSYL LQAMTHASYT PNRLTDCYQR LEFLGDAVLD 2050 2060 2070 2080 2090 2100 YLITRHLYED PRQHSPGALT DLRSALVNNT IFASLAVRHG FHKFFRHLSP GLNDVIDRFV 2110 2120 2130 2140 2150 2160 RIQQENGHCI SEEYYLLSEE ECDDAEDVEV PKALGDVFES IAGAIFLDSN MSLDVVWHVY 2170 2180 2190 2200 2210 2220 SNMMSPEIEQ FSNSVPKSPI RELLELEPET AKFGKPEKLA DGRRVRVTVD VFCKGTFRGI 2230 2240 GRNYRIAKCT AAKCALRQLK KQGLIAKKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1338-2249. Strain: Berkeley. Tissue: Embryo.
[4]	"Role for a bidentate ribonuclease in the initiation step of RNA interference." Bernstein E., Caudy A.A., Hammond S.M., Hannon G.J. Nature 409:363-366(2001) [PubMed: 11201747] [Abstract] Cited for: FUNCTION.
[5]	"Argonaute2, a link between genetic and biochemical analyses of RNAi." Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J. Science 293:1146-1150(2001) [PubMed: 11498593] [Abstract] Cited for: FUNCTION, INTERACTION WITH AGO2.
[6]	"A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins." Ishizuka A., Siomi M.C., Siomi H. Genes Dev. 16:2497-2508(2002) [PubMed: 12368261] [Abstract] Cited for: INTERACTION WITH FMR1.
[7]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1423; SER-1877 AND SER-1880, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF56056.1. AY050230 mRNA. Translation: AAK84929.1. Different initiation.
RefSeq	NP_524453.1.
UniGene	Dm.1283
3D structure databases
HSSP	HSSP built from PDB template 1JFZ based on UniProtKB O67082.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VCU9. 6 interactions.
Proteomic databases
PRIDE	Q9VCU9.
Genome annotation databases
Ensembl	FBgn0039016. Drosophila melanogaster. [Contig view]
GeneID	42693.
KEGG	dme:Dmel_CG4792.
NMPDR	fig|7227.3.peg.14136.
Organism-specific databases
FlyBase	FBgn0039016. Dcr-1.
Phylogenomic databases
HOGENOM	Q9VCU9.
OMA	Q9VCU9. FLKYAIT.
Gene expression databases
ArrayExpress	Q9VCU9.
GermOnline	CG4792. Drosophila melanogaster.
Family and domain databases
InterPro	IPR005034. Dicer_dsRNA_binding_fold. IPR001650. DNA/RNA_helicase_C. IPR001159. Ds-RNA_bd. IPR003100. PAZ. IPR000999. RNase_III. [Graphical view]
Gene3D	G3DSA:1.10.1520.10. RNase_III. 2 hits.
Pfam	PF03368. dsRNA_bind. 1 hit. PF00271. Helicase_C. 1 hit. PF02170. PAZ. 1 hit. PF00636. Ribonuclease_3. 2 hits. [Graphical view]
SMART	SM00358. DSRM. 1 hit. SM00490. HELICc. 1 hit. SM00535. RIBOc. 2 hits. [Graphical view]
PROSITE	PS51327. DICER_DSRBF. 1 hit. PS50137. DS_RBD. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS50821. PAZ. 1 hit. PS00517. RNASE_3_1. 1 hit. PS50142. RNASE_3_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	830091.

Entry information

Entry name

DCR1_DROME

Accession

Primary (citable) accession number: Q9VCU9
Secondary accession number(s): Q961S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project