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Drosha

 
Known abbreviations: p241, RN3, RNASE3L, RNASEN

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.

CATALYTIC ACTIVITY:

Endonucleolytic cleavage to 5'-phosphomonoester.

COFACTOR:

Magnesium or manganese (By similarity).

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. Interacts with SRRT/ARS2.

CELLULAR LOCALIZATION:

Nucleus. Nucleus › nucleolus. 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.

TISSUE SPECIFICITY:

Ubiquitous.

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.



Activities in which Drosha is involved: Pathways in which Drosha is involved:

NCBI GI number(s): 155030233
155030234
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9NRR4 Q9NRR4
BRENDA - -
KEGG hsa:29102 hsa:29102
PFAM: - Q9NRR4 (Link - using uniprot id)
InterPro: - Q9NRR4 (Link - using uniprot id)
CATH: - -
SCOP: - -
Solved crystal structures: 2KHX
[PDB] [details]


Protein sequence:
MMQGNTCHRMSFHPGRGCPRGRGGHGARPSAPSFRPQNLRLLHPQQPPVQ
YQYEPPSAPSTTFSNSPAPNFLPPRPDFVPFPPPMPPSAQGPLPPCPIRP
PFPNHQMRHPFPVPPCFPPMPPPMPCPNNPPVPGAPPGQGTFPFMMPPPS
MPHPPPPPVMPQQVNYQYPPGYSHHNFPPPSFNSFQNNPSSFLPSANNSS
SPHFRHLPPYPLPKAPSERRSPERLKHYDDHRHRDHSHGRGERHRSLDRR
ERGRSPDRRRQDSRYRSDYDRGRTPSRHRSYERSRERERERHRHRDNRRS
PSLERSYKKEYKRSGRSYGLSVVPEPAGCTPELPGEIIKNTDSWAPPLEI
VNHRSPSREKKRARWEEEKDRWSDNQSSGKDKNYTSIKEKEPEETMPDKN
EEEEEELLKPVWIRCTHSENYYSSDPMDQVGDSTVVGTSRLRDLYDKFEE
ELGSRQEKAKAARPPWEPPKTKLDEDLESSSESECESDEDSTCSSSSDSE
VFDVIAEIKRKKAHPDRLHDELWYNDPGQMNDGPLCKCSAKARRTGIRHS
IYPGEEAIKPCRPMTNNAGRLFHYRITVSPPTNFLTDRPTVIEYDDHEYI
FEGFSMFAHAPLTNIPLCKVIRFNIDYTIHFIEEMMPENFCVKGLELFSL
FLFRDILELYDWNLKGPLFEDSPPCCPRFHFMPRFVRFLPDGGKEVLSMH
QILLYLLRCSKALVPEEEIANMLQWEELEWQKYAEECKGMIVTNPGTKPS
SVRIDQLDREQFNPDVITFPIIVHFGIRPAQLSYAGDPQYQKLWKSYVKL
RHLLANSPKVKQTDKQKLAQREEALQKIRQKNTMRREVTVELSSQGFWKT
GIRSDVCQHAMMLPVLTHHIRYHQCLMHLDKLIGYTFQDRCLLQLAMTHP
SHHLNFGMNPDHARNSLSNCGIRQPKYGDRKVHHMHMRKKGINTLINIMS
RLGQDDPTPSRINHNERLEFLGDAVVEFLTSVHLYYLFPSLEEGGLATYR
TAIVQNQHLAMLAKKLELDRFMLYAHGPDLCRESDLRHAMANCFEALIGA
VYLEGSLEEAKQLFGRLLFNDPDLREVWLNYPLHPLQLQEPNTDRQLIET
SPVLQKLTEFEEAIGVIFTHVRLLARAFTLRTVGFNHLTLGHNQRMEFLG
DSIMQLVATEYLFIHFPDHHEGHLTLLRSSLVNNRTQAKVAEELGMQEYA
ITNDKTKRPVALRTKTLADLLESFIAALYIDKDLEYVHTFMNVCFFPRLK
EFILNQDWNDPKSQLQQCCLTLRTEGKEPDIPLYKTLQTVGPSHARTYTV
AVYFKGERIGCGKGPSIQQAEMGAAMDALEKYNFPQMAHQKRFIERKYRQ
ELKEMRWEREHQEREPDETEDIKK

Drosha (Homo sapiens) is product of expression of Drosha gene.

Drosha (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal Publication date (Issue) PubMed ID
Recognition and cleavage of primary microRNA precursors by the nuclear processing enzyme Drosha. Zeng Y, Yi R, Cullen BR EMBO J 2005-02-12 (24) 15565168
Efficient processing of primary microRNA hairpins by Drosha requires flanking nonstructured RNA sequences. Zeng Y, Cullen BR J Biol Chem 2005-07-29 (280) 15932881
Role of Dicer and Drosha for endothelial microRNA expression and angiogenesis. Kuehbacher A, Urbich C, Zeiher AM, Dimmeler S Circ Res 2007-07-06 (101) 17540974
DEAD-box RNA helicase subunits of the Drosha complex are required for processing of rRNA and a subset of microRNAs. Fukuda T, Yamagata K, Fujiyama S, Matsumoto T, Koshida I, Yoshimura K, Mihara M, Naitou M, Endoh H, Nakamura T, Akimoto C, Yamamoto Y, Katagiri T, Foulds C, Takezawa S, Kitagawa H, Takeyama K, O'Malley BW, Kato S Nat Cell Biol 2007-05-01 (9) 17435748
Molecular basis for the recognition of primary microRNAs by the Drosha-DGCR8 complex. Han J, Lee Y, Yeom KH, Nam JW, Heo I, Rhee JK, Sohn SY, Cho Y, Zhang BT, Kim VN Cell 2006-06-02 (125) 16751099
Drosha in primary microRNA processing. Lee Y, Han J, Yeom KH, Jin H, Kim VN Cold Spring Harb Symp Quant Bi 2006-01-01 (71) 17381280
The nuclear RNase III Drosha initiates microRNA processing. Lee Y, Ahn C, Han J, Choi H, Kim J, Yim J, Lee J, Provost P, Radmark O, Kim S, Kim VN Nature 2003-09-25 (425) 14508493
The Drosha-DGCR8 complex in primary microRNA processing. Han J, Lee Y, Yeom KH, Kim YK, Jin H, Kim VN Genes Dev 2004-12-15 (18) 15574589
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell 2006-11-03 (127) 17081983
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
The DNA sequence and comparative analysis of human chromosome 5. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W Nature 2004-09-16 (431) 15372022
Human RNase III is a 160-kDa protein involved in preribosomal RNA processing. Wu H, Xu H, Miraglia LJ, Crooke ST J Biol Chem 2000-11-24 (275) 10948199
A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening. Gunther M, Laithier M, Brison O Mol Cell Biochem 2000-07-01 (210) 10976766
The human DiGeorge syndrome critical region gene 8 and Its D. melanogaster homolog are required for miRNA biogenesis. Landthaler M, Yalcin A, Tuschl T Curr Biol 2004-12-14 (14) 15589161
The Microprocessor complex mediates the genesis of microRNAs. Gregory RI, Yan KP, Amuthan G, Chendrimada T, Doratotaj B, Cooch N, Shiekhattar R Nature 2004-11-11 (432) 15531877
Formation of GW bodies is a consequence of microRNA genesis. Pauley KM, Eystathioy T, Jakymiw A, Hamel JC, Fritzler MJ, Chan EK EMBO Rep 2006-09-01 (7) 16906129
Heme is involved in microRNA processing. Faller M, Matsunaga M, Yin S, Loo JA, Guo F Nat Struct Mol Biol 2007-02-01 (14) 17159994
The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis. Yu B, Bi L, Zheng B, Ji L, Chevalier D, Agarwal M, Ramachandran V, Li W, Lagrange T, Walker JC, Chen X Proc Natl Acad Sci U S A 2008-07-22 (105) 18632581



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Last modification of this entry: Sept. 25, 2012.

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