UniProt functional annotation for Q9NRR4



	UniProt functional annotation for Q9NRR4

UniProt code: Q9NRR4.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

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:0000269|PubMed:10948199, ECO:0000269|PubMed:14508493, ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15565168, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718}.

Catalytic activity: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000269|PubMed:15565168, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:15574589}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:15574589}; Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+) ion. {ECO:0000305};

Subunit: Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8 (PubMed:15589161, PubMed:15574589, PubMed:15531877, PubMed:16751099, PubMed:26027739, PubMed:26748718). The microprocessor complex is a heterotrimer; each of the two DROSHA RNase III domains binds one DGCR8 (via C-terminal region) (PubMed:26027739, PubMed:26748718). Interacts with SP1 and SNIP1 (PubMed:10976766, PubMed:18632581). Interacts with SRRT/ARS2 (By similarity). Interacts with CPSF3 and ISY1; this interaction is in an RNA dependent manner (By similarity). Interacts with PUS10; interaction promotes pri-miRNAs processing (PubMed:31819270). {ECO:0000250|UniProtKB:Q5HZJ0, ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:18632581, ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718, ECO:0000269|PubMed:31819270}.

Subcellular location: Nucleus {ECO:0000269|PubMed:10948199, ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:22118463}. Nucleus, nucleolus {ECO:0000269|PubMed:10948199}. 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:0000269|PubMed:10948199, ECO:0000269|PubMed:22118463}.

Tissue specificity: Ubiquitous. {ECO:0000269|PubMed:10948199}.

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:0000269|PubMed:15574589}.

Similarity: Belongs to the ribonuclease III family. {ECO:0000305}.

Sequence caution: Sequence=AAD29637.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAA91511.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



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:0000269\|PubMed:10948199, ECO:0000269\|PubMed:14508493, ECO:0000269\|PubMed:15531877, ECO:0000269\|PubMed:15565168, ECO:0000269\|PubMed:15574589, ECO:0000269\|PubMed:15589161, ECO:0000269\|PubMed:16751099, ECO:0000269\|PubMed:16906129, ECO:0000269\|PubMed:17159994, ECO:0000269\|PubMed:26027739, ECO:0000269\|PubMed:26748718}.


Catalytic activity:		Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000269\|PubMed:15565168, ECO:0000269\|PubMed:15574589, ECO:0000269\|PubMed:26027739, ECO:0000269\|PubMed:26748718};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305\|PubMed:15574589}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305\|PubMed:15574589}; Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+) ion. {ECO:0000305};
Subunit:		Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8 (PubMed:15589161, PubMed:15574589, PubMed:15531877, PubMed:16751099, PubMed:26027739, PubMed:26748718). The microprocessor complex is a heterotrimer; each of the two DROSHA RNase III domains binds one DGCR8 (via C-terminal region) (PubMed:26027739, PubMed:26748718). Interacts with SP1 and SNIP1 (PubMed:10976766, PubMed:18632581). Interacts with SRRT/ARS2 (By similarity). Interacts with CPSF3 and ISY1; this interaction is in an RNA dependent manner (By similarity). Interacts with PUS10; interaction promotes pri-miRNAs processing (PubMed:31819270). {ECO:0000250\|UniProtKB:Q5HZJ0, ECO:0000269\|PubMed:10976766, ECO:0000269\|PubMed:15531877, ECO:0000269\|PubMed:15574589, ECO:0000269\|PubMed:15589161, ECO:0000269\|PubMed:16751099, ECO:0000269\|PubMed:18632581, ECO:0000269\|PubMed:26027739, ECO:0000269\|PubMed:26748718, ECO:0000269\|PubMed:31819270}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:10948199, ECO:0000269\|PubMed:16906129, ECO:0000269\|PubMed:22118463}. Nucleus, nucleolus {ECO:0000269\|PubMed:10948199}. 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:0000269\|PubMed:10948199, ECO:0000269\|PubMed:22118463}.
Tissue specificity:		Ubiquitous. {ECO:0000269\|PubMed:10948199}.
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:0000269\|PubMed:15574589}.
Similarity:		Belongs to the ribonuclease III family. {ECO:0000305}.
Sequence caution:		Sequence=AAD29637.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAA91511.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};