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Q5HZJ0 (RNC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease 3

EC=3.1.26.3
Alternative name(s):
Protein Drosha
Ribonuclease III
Short name=RNase III
Gene names
Name:Drosha
Synonyms:Etohi2, Rn3, Rnasen
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1373 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_00104

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00104

Cofactor

Magnesium or manganese By similarity. HAMAP-Rule MF_00104

Subunit structure

Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8. The microprocessor complex may contain multiple subunit of DGCR8 and DROSHA. Interacts with DGCR8, SP1 and SNIP1 By similarity. Interacts with SRRT/ARS2. Ref.3

Subcellular location

Nucleus By similarity. Nucleusnucleolus By similarity. 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 By similarity. HAMAP-Rule MF_00104

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 By similarity. HAMAP-Rule MF_00104

Sequence similarities

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 2 RNase III domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13731373Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000384374

Regions

Domain875 – 1055181RNase III 1
Domain1106 – 1232127RNase III 2
Domain1259 – 133375DRBM
Region489 – 1373885Necessary for interaction with DGCR8 and pri-miRNA processing activity By similarity
Compositional bias28 – 211184Pro-rich HAMAP-Rule MF_00104
Compositional bias217 – 31599Arg-rich HAMAP-Rule MF_00104

Sites

Metal binding11461Magnesium or manganese By similarity
Metal binding12181Magnesium or manganese By similarity
Metal binding12211Magnesium or manganese By similarity
Site12141Important for activity By similarity

Amino acid modifications

Modified residue3721Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HZJ0 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: ED1DBEE2FFD89A6B

FASTA1,373158,828
        10         20         30         40         50         60 
MQGNTCHRMS YHPGRGCPRG RGGHGARPSA PAFRPQNLRL LHPQQPPAQY QYEPPSAPSS 

        70         80         90        100        110        120 
SYSNSQAPSF MPPRPDFVPY PPPAAPSAQG PLPPCPVRPP YPNHQMRHPF PVPPCFPPMP 

       130        140        150        160        170        180 
PPMPCPNNPP ASGAPPGQGT FPFMVPPPSM PHPPPPPVMP QQVNYQYPPG YSHSFPPPGF 

       190        200        210        220        230        240 
NSYQNNSSSF PPSANSSSTP HFRHLPPYSL PKAQNERRSP ERLKHYDDHR HRDHSHGRGE 

       250        260        270        280        290        300 
RHRSLERRER GRSPERRRPE SRYRSDYDRG RTPPPRHRSY ERSRERDRER HRHREARRSP 

       310        320        330        340        350        360 
SLERSYKKEY KRSGRSYALP VAPEPAGCTP ELPGEMIKTT ESWAPPPENV NHRSPSREKK 

       370        380        390        400        410        420 
RARWEEEKDR WSDSQGSGKE KNYTSIKEKE AEEVPPEKTE EEEEELLKPV WIRCTHSESY 

       430        440        450        460        470        480 
YSSDPMDQVG DSTVVGTSRL RDLYDKFEEE LGNRQEKAKA ARPPWEPPKT KLDEDLESSS 

       490        500        510        520        530        540 
ESECETDDDS TCSSSSDSEV FDVIAEIKRK KAHPDRLHDE LWYNDPGQMN DGPLCKCSAK 

       550        560        570        580        590        600 
ARRTGIRHSI YPGEEAIKPC RPMTNNAGRL FHYRITVSPP TNFLTDRPTV IEYDDHEYIF 

       610        620        630        640        650        660 
EGFSMFAHAP LTNIPLCKVI RFNIDYTIHF IEEMMPENFC VKGLELFSLF LFRDILELYD 

       670        680        690        700        710        720 
WNLKGPLFED SPPCCPRFHF MPRFVRFLPD GGKEVLSMHQ ILLYLLRCSK ALVPEEEIAN 

       730        740        750        760        770        780 
MLQWEELEWQ KYAEECKGMI VTNPGTKPSS VRIDQLDREQ FNPEVITFPI IVHFGIRPAQ 

       790        800        810        820        830        840 
LSYAGDPQYQ KLWKSYVKLR HLLANSPKVK QTDKQKLAQR EEALQKIRQK NTMRREVTVE 

       850        860        870        880        890        900 
LSSQGFWKTG IRSDVCQHAM MLPVLTHHIR YHQCLMHLDK LIGYTFQDRC LLQLAMTHPS 

       910        920        930        940        950        960 
HHLNFGMNPD HARNSLSNCG IRQPKYGDRK VHHMHMRKKG INTLINIMSR LGQDDPTPSR 

       970        980        990       1000       1010       1020 
INHNERLEFL GDAVVEFLTS VHLYYLFPSL EEGGLATYRT AIVQNQHLAM LAKKLELDRF 

      1030       1040       1050       1060       1070       1080 
MLYAHGPDLC RESDLRHAMA NCFEALIGAV YLEGSLEEAK QLFGRLLFND PDLREVWLNY 

      1090       1100       1110       1120       1130       1140 
PLHPLQLQEP NTDRQLIETS PVLQKLTEFE EAIGVIFTHV RLLARAFTLR TVGFNHLTLG 

      1150       1160       1170       1180       1190       1200 
HNQRMEFLGD SIMQLVATEY LFIHFPDHHE GHLTLLRSSL VNNRTQAKVA EELGMQEYAI 

      1210       1220       1230       1240       1250       1260 
TNDKTKRPVA LRTKTLADLL ESFIAALYID KDLEYVHTFM NVCFFPRLKE FILNQDWNDP 

      1270       1280       1290       1300       1310       1320 
KSQLQQCCLT LRTEGKEPDI PLYKTLQTVG PSHARTYTVA VYFKGERIGC GKGPSIQQAE 

      1330       1340       1350       1360       1370 
MGAAMDALEK YNFPQMAHQK RFIERKYRQE LKEMRWEREH QEREPEEAED IKK 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic stem cell and Sympathetic ganglion.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Embryonic brain.
[3]"Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation."
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.
Cell 138:328-339(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRRT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK144147 mRNA. Translation: BAE25729.1.
AK148640 mRNA. Translation: BAE28629.1.
BC088999 mRNA. Translation: AAH88999.1.
CCDSCCDS49583.1.
RefSeqNP_001123621.1. NM_001130149.1.
NP_081075.3. NM_026799.3.
UniGeneMm.293142.

3D structure databases

ProteinModelPortalQ5HZJ0.
SMRQ5HZJ0. Positions 961-1336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199531. 1 interaction.
STRING10090.ENSMUSP00000087762.

PTM databases

PhosphoSiteQ5HZJ0.

Proteomic databases

PaxDbQ5HZJ0.
PRIDEQ5HZJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090292; ENSMUSP00000087762; ENSMUSG00000022191.
ENSMUST00000169061; ENSMUSP00000129279; ENSMUSG00000022191.
GeneID14000.
KEGGmmu:14000.
UCSCuc007via.2. mouse.

Organism-specific databases

CTD29102.
MGIMGI:1261425. Drosha.

Phylogenomic databases

eggNOGCOG0571.
GeneTreeENSGT00730000111052.
HOGENOMHOG000122291.
InParanoidQ5HZJ0.
KOK03685.
OMAESYYSND.
OrthoDBEOG773XF7.
PhylomeDBQ5HZJ0.
TreeFamTF314734.

Gene expression databases

ArrayExpressQ5HZJ0.
BgeeQ5HZJ0.
GenevestigatorQ5HZJ0.

Family and domain databases

Gene3D1.10.1520.10. 3 hits.
3.30.160.20. 1 hit.
HAMAPMF_00104. RNase_III.
InterProIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PANTHERPTHR11207. PTHR11207. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
PF00636. Ribonuclease_3. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMSSF69065. SSF69065. 3 hits.
PROSITEPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 2 hits.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDROSHA. mouse.
NextBio284892.
PROQ5HZJ0.
SOURCESearch...

Entry information

Entry nameRNC_MOUSE
AccessionPrimary (citable) accession number: Q5HZJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 15, 2005
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot