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Ribonuclease 3 (EC 3.1.26.3) (Protein Drosha) (Ribonuclease III) (RNase III)

 RNC_MOUSE               Reviewed;        1373 AA.
Q5HZJ0;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
20-JUN-2018, entry version 128.
RecName: Full=Ribonuclease 3;
EC=3.1.26.3 {ECO:0000250|UniProtKB:Q9NRR4};
AltName: Full=Protein Drosha;
AltName: Full=Ribonuclease III;
Short=RNase III;
Name=Drosha; Synonyms=Etohi2, Rn3, Rnasen;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Sympathetic ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH SRRT.
PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
Dreyfuss G., Thompson C.B.;
"Ars2 links the nuclear cap-binding complex to RNA interference and
cell proliferation.";
Cell 138:328-339(2009).
-!- FUNCTION: Ribonuclease III double-stranded (ds) RNA-specific
endoribonuclease that is involved in the initial step of microRNA
(miRNA) biogenesis. Component of the microprocessor complex that
is required to process primary miRNA transcripts (pri-miRNAs) to
release precursor miRNA (pre-miRNA) in the nucleus. Within the
microprocessor complex, DROSHA cleaves the 3' and 5' strands of a
stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-
ssRNA junction) to release hairpin-shaped pre-miRNAs that are
subsequently cut by the cytoplasmic DICER to generate mature
miRNAs. Involved also in pre-rRNA processing. Cleaves double-
strand RNA and does not cleave single-strand RNA. Involved in the
formation of GW bodies. {ECO:0000250|UniProtKB:Q9NRR4}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000250|UniProtKB:Q9NRR4}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9NRR4};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q9NRR4};
Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+)
ion. {ECO:0000250|UniProtKB:Q9NRR4};
-!- SUBUNIT: Component of the microprocessor complex, or pri-miRNA
processing protein complex, which is composed of DROSHA and DGCR8.
The microprocessor complex is a heterotrimer; each of the two
DROSHA RNase III domains binds one DGCR8 (via C-terminal region).
Interacts with SP1 and SNIP1 (By similarity). Interacts with
SRRT/ARS2 (PubMed:19632182). {ECO:0000250|UniProtKB:Q9NRR4,
ECO:0000269|PubMed:19632182}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRR4}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NRR4}. Note=A fraction
is translocated to the nucleolus during the S phase of the cell
cycle. Localized in GW bodies (GWBs), also known as P-bodies.
{ECO:0000250|UniProtKB:Q9NRR4}.
-!- DOMAIN: The 2 RNase III domains form an intramolecular dimer where
the domain 1 cuts the 3'strand while the domain 2 cleaves the
5'strand of pri-miRNAs, independently of each other.
{ECO:0000250|UniProtKB:Q9NRR4}.
-!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK144147; BAE25729.1; -; mRNA.
EMBL; AK148640; BAE28629.1; -; mRNA.
EMBL; BC088999; AAH88999.1; -; mRNA.
CCDS; CCDS49583.1; -.
RefSeq; NP_001123621.1; NM_001130149.1.
RefSeq; NP_081075.3; NM_026799.3.
UniGene; Mm.293142; -.
ProteinModelPortal; Q5HZJ0; -.
SMR; Q5HZJ0; -.
BioGrid; 199531; 4.
ComplexPortal; CPX-3081; Microprocessor complex.
CORUM; Q5HZJ0; -.
IntAct; Q5HZJ0; 1.
STRING; 10090.ENSMUSP00000087762; -.
iPTMnet; Q5HZJ0; -.
PhosphoSitePlus; Q5HZJ0; -.
EPD; Q5HZJ0; -.
MaxQB; Q5HZJ0; -.
PaxDb; Q5HZJ0; -.
PeptideAtlas; Q5HZJ0; -.
PRIDE; Q5HZJ0; -.
Ensembl; ENSMUST00000090292; ENSMUSP00000087762; ENSMUSG00000022191.
Ensembl; ENSMUST00000169061; ENSMUSP00000129279; ENSMUSG00000022191.
GeneID; 14000; -.
KEGG; mmu:14000; -.
UCSC; uc007via.2; mouse.
CTD; 29102; -.
MGI; MGI:1261425; Drosha.
eggNOG; KOG1817; Eukaryota.
eggNOG; COG0571; LUCA.
GeneTree; ENSGT00730000111052; -.
HOGENOM; HOG000122291; -.
InParanoid; Q5HZJ0; -.
KO; K03685; -.
OMA; LSRKVQH; -.
OrthoDB; EOG091G02A9; -.
PhylomeDB; Q5HZJ0; -.
TreeFam; TF314734; -.
ChiTaRS; Drosha; mouse.
PRO; PR:Q5HZJ0; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022191; -.
Genevisible; Q5HZJ0; MM.
GO; GO:0070877; C:microprocessor complex; ISO:MGI.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
GO; GO:0004521; F:endoribonuclease activity; IDA:MGI.
GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070878; F:primary miRNA binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0004525; F:ribonuclease III activity; ISO:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
GO; GO:0010586; P:miRNA metabolic process; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
GO; GO:0031053; P:primary miRNA processing; ISO:MGI.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IBA:GO_Central.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
GO; GO:2000628; P:regulation of miRNA metabolic process; IMP:MGI.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IMP:MGI.
GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
CDD; cd00593; RIBOc; 2.
Gene3D; 1.10.1520.10; -; 1.
HAMAP; MF_00104; RNase_III; 1.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR011907; RNase_III.
InterPro; IPR000999; RNase_III_dom.
InterPro; IPR036389; RNase_III_sf.
Pfam; PF00035; dsrm; 1.
Pfam; PF14622; Ribonucleas_3_3; 1.
Pfam; PF00636; Ribonuclease_3; 1.
SMART; SM00358; DSRM; 1.
SMART; SM00535; RIBOc; 2.
SUPFAM; SSF69065; SSF69065; 3.
PROSITE; PS50137; DS_RBD; 1.
PROSITE; PS00517; RNASE_3_1; 2.
PROSITE; PS50142; RNASE_3_2; 2.
1: Evidence at protein level;
Complete proteome; Endonuclease; Hydrolase; Magnesium; Manganese;
Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Ribosome biogenesis; RNA-binding; Zinc.
CHAIN 1 1373 Ribonuclease 3.
/FTId=PRO_0000384374.
DOMAIN 875 1055 RNase III 1.
DOMAIN 1106 1232 RNase III 2.
DOMAIN 1259 1333 DRBM.
REGION 389 1364 Necessary for interaction with DGCR8 and
pri-miRNA processing activity.
{ECO:0000250|UniProtKB:Q9NRR4}.
COMPBIAS 28 211 Pro-rich.
COMPBIAS 217 315 Arg-rich.
METAL 535 535 Zinc 1. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 537 537 Zinc 1. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 548 548 Zinc 1. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 560 560 Zinc 2. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 608 608 Zinc 2. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 675 675 Zinc 2. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 679 679 Zinc 2. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 968 968 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:O67082}.
METAL 1025 1025 Zinc 1. {ECO:0000250|UniProtKB:Q9NRR4}.
METAL 1041 1041 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:O67082}.
METAL 1044 1044 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:O67082,
ECO:0000250|UniProtKB:Q9NRR4}.
METAL 1146 1146 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:O67082}.
METAL 1218 1218 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:O67082}.
METAL 1221 1221 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:O67082,
ECO:0000250|UniProtKB:Q9NRR4}.
SITE 1214 1214 Important for activity. {ECO:0000250}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NRR4}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NRR4}.
SEQUENCE 1373 AA; 158828 MW; ED1DBEE2FFD89A6B CRC64;
MQGNTCHRMS YHPGRGCPRG RGGHGARPSA PAFRPQNLRL LHPQQPPAQY QYEPPSAPSS
SYSNSQAPSF MPPRPDFVPY PPPAAPSAQG PLPPCPVRPP YPNHQMRHPF PVPPCFPPMP
PPMPCPNNPP ASGAPPGQGT FPFMVPPPSM PHPPPPPVMP QQVNYQYPPG YSHSFPPPGF
NSYQNNSSSF PPSANSSSTP HFRHLPPYSL PKAQNERRSP ERLKHYDDHR HRDHSHGRGE
RHRSLERRER GRSPERRRPE SRYRSDYDRG RTPPPRHRSY ERSRERDRER HRHREARRSP
SLERSYKKEY KRSGRSYALP VAPEPAGCTP ELPGEMIKTT ESWAPPPENV NHRSPSREKK
RARWEEEKDR WSDSQGSGKE KNYTSIKEKE AEEVPPEKTE EEEEELLKPV WIRCTHSESY
YSSDPMDQVG DSTVVGTSRL RDLYDKFEEE LGNRQEKAKA ARPPWEPPKT KLDEDLESSS
ESECETDDDS TCSSSSDSEV FDVIAEIKRK KAHPDRLHDE LWYNDPGQMN DGPLCKCSAK
ARRTGIRHSI YPGEEAIKPC RPMTNNAGRL FHYRITVSPP TNFLTDRPTV IEYDDHEYIF
EGFSMFAHAP LTNIPLCKVI RFNIDYTIHF IEEMMPENFC VKGLELFSLF LFRDILELYD
WNLKGPLFED SPPCCPRFHF MPRFVRFLPD GGKEVLSMHQ ILLYLLRCSK ALVPEEEIAN
MLQWEELEWQ KYAEECKGMI VTNPGTKPSS VRIDQLDREQ FNPEVITFPI IVHFGIRPAQ
LSYAGDPQYQ KLWKSYVKLR HLLANSPKVK QTDKQKLAQR EEALQKIRQK NTMRREVTVE
LSSQGFWKTG IRSDVCQHAM MLPVLTHHIR YHQCLMHLDK LIGYTFQDRC LLQLAMTHPS
HHLNFGMNPD HARNSLSNCG IRQPKYGDRK VHHMHMRKKG INTLINIMSR LGQDDPTPSR
INHNERLEFL GDAVVEFLTS VHLYYLFPSL EEGGLATYRT AIVQNQHLAM LAKKLELDRF
MLYAHGPDLC RESDLRHAMA NCFEALIGAV YLEGSLEEAK QLFGRLLFND PDLREVWLNY
PLHPLQLQEP NTDRQLIETS PVLQKLTEFE EAIGVIFTHV RLLARAFTLR TVGFNHLTLG
HNQRMEFLGD SIMQLVATEY LFIHFPDHHE GHLTLLRSSL VNNRTQAKVA EELGMQEYAI
TNDKTKRPVA LRTKTLADLL ESFIAALYID KDLEYVHTFM NVCFFPRLKE FILNQDWNDP
KSQLQQCCLT LRTEGKEPDI PLYKTLQTVG PSHARTYTVA VYFKGERIGC GKGPSIQQAE
MGAAMDALEK YNFPQMAHQK RFIERKYRQE LKEMRWEREH QEREPEEAED IKK


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