Human Gene DGCR8 (ENST00000383024.6) Description and Page Index
Description: Homo sapiens DGCR8 microprocessor complex subunit (DGCR8), transcript variant 2, mRNA. (from RefSeq NM_001190326) RefSeq Summary (NM_001190326): This gene encodes a subunit of the microprocessor complex which mediates the biogenesis of microRNAs from the primary microRNA transcript. The encoded protein is a double-stranded RNA binding protein that functions as the non-catalytic subunit of the microprocessor complex. This protein is required for binding the double-stranded RNA substrate and facilitates cleavage of the RNA by the ribonuclease III protein, Drosha. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jun 2010]. Gencode Transcript: ENST00000383024.6 Gencode Gene: ENSG00000128191.16 Transcript (Including UTRs) Position: hg38 chr22:20,080,232-20,111,875 Size: 31,644 Total Exon Count: 13 Strand: + Coding Region Position: hg38 chr22:20,085,964-20,110,108 Size: 24,145 Coding Exon Count: 12
ID:DGCR8_HUMAN DESCRIPTION: RecName: Full=Microprocessor complex subunit DGCR8; AltName: Full=DiGeorge syndrome critical region 8; FUNCTION: Component of the microprocessor complex that acts as a RNA- and heme-binding protein 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, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri- miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri- miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding. Involved in the silencing of embryonic stem cells self- renewal. COFACTOR: Binds 1 heme group per homodimer. SUBUNIT: Monomer; in absence of heme. Homodimer; the association with heme promotes its dimerization. Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DGCR8 (heme-free or heme-bound forms) and DROSHA. The microprocessor complex may contain multiple subunit of DGCR8 and DROSHA. Interacts with ILF3, NCL and DROSHA. INTERACTION: Q9NRR4:DROSHA; NbExp=4; IntAct=EBI-528411, EBI-528367; SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Note=Colocalizes with nucleolin and DROSHA in the nucleolus. Mostly detected in the nucleolus as electron-dense granular patches around the fibrillar center (FC) and granular component (GC). Also detected in the nucleoplasm as small foci adjacent to splicing speckles near the chromatin structure. Localized with DROSHA in GW bodies (GWBs), also known as P-bodies. TISSUE SPECIFICITY: Ubiquitously expressed. DOMAIN: Both DRBM domains are required for efficient binding to pri-miRNA. The region between residues 276 and 498 has an autoinhibitory function on pri-miRNA processing activity. SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains. SIMILARITY: Contains 1 WW domain. SEQUENCE CAUTION: Sequence=AAO86726.1; Type=Erroneous initiation; Sequence=BAB15165.1; Type=Erroneous initiation; Sequence=BAB15238.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q8WYQ5
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.