A0MQH0 (DICER_CRIGR) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 38.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Endoribonuclease Dicer EC=3.1.26.- | ||||
| Gene names |
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| Organism | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) | ||||
| Taxonomic identifier | 10029 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus![]() |
Protein attributes
| Sequence length | 1917 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, EIF2C2/AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto EIF2C2/AGO2. EIF2C2/AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Also cleaves double-stranded RNA to produce short interfering RNAs (siRNAs) which target the selective destruction of complementary RNAs By similarity. |
| Cofactor | Binds 2 magnesium or manganese ions per subunit By similarity. |
| Subunit structure | Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, EIF2C2/AGO2 and TARBP2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with DHX9, EIF2C1, PIWIL1 and PRKRA. Associates with the 60S ribosome. Interacts with BCDIN3D By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the helicase family. Dicer subfamily. Contains 1 Dicer dsRNA-binding fold domain. Contains 1 DRBM (double-stranded RNA-binding) domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 PAZ domain. Contains 2 RNase III domains. |
| Caution | It is uncertain whether Met-1 or Met-11 is the initiator. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1917 | 1917 | Endoribonuclease Dicer | PRO_0000373983 | |||||
Regions | |||||||||
| Domain | 51 – 227 | 177 | Helicase ATP-binding | ||||||
| Domain | 433 – 602 | 170 | Helicase C-terminal | ||||||
| Domain | 630 – 722 | 93 | Dicer dsRNA-binding fold | ||||||
| Domain | 898 – 1042 | 145 | PAZ | ||||||
| Domain | 1276 – 1403 | 128 | RNase III 1 | ||||||
| Domain | 1661 – 1819 | 159 | RNase III 2 | ||||||
| Domain | 1844 – 1909 | 66 | DRBM | ||||||
| Nucleotide binding | 64 – 71 | 8 | ATP By similarity | ||||||
| Region | 256 – 595 | 340 | Required for interaction with PRKRA and TARBP2 By similarity | ||||||
| Motif | 175 – 178 | 4 | DECH box | ||||||
Sites | |||||||||
| Metal binding | 1316 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 1395 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 1398 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 1700 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Metal binding | 1805 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Metal binding | 1808 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Site | 1801 | 1 | Important for activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 413 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 415 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1016 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | Wallerstorfer D. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EF031271 mRNA. Translation: ABK28790.1. |
| RefSeq | NP_001231198.1. NM_001244269.1. |
3D structure databases | |
| ProteinModelPortal | A0MQH0. |
| SMR | A0MQH0. Positions 1649-1911. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100689239. |
Organism-specific databases | |
| CTD | 23405. |
Family and domain databases | |
| Gene3D | 1.10.1520.10. 4 hits. 3.30.160.20. 1 hit. |
| InterPro | IPR005034. Dicer_dsRNA_binding_fold. IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR001159. Ds-RNA-bd. IPR014720. dsRNA-bd-like_dom. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR003100. PAZ. IPR000999. RNase_III_dom. [Graphical view] |
| Pfam | PF00270. DEAD. 1 hit. PF03368. dsRNA_bind. 1 hit. PF00271. Helicase_C. 1 hit. PF02170. PAZ. 1 hit. PF00636. Ribonuclease_3. 2 hits. [Graphical view] |
| SMART | SM00487. DEXDc. 1 hit. SM00358. DSRM. 1 hit. SM00490. HELICc. 1 hit. SM00949. PAZ. 1 hit. SM00535. RIBOc. 2 hits. [Graphical view] |
| SUPFAM | SSF101690. PAZ. 1 hit. SSF69065. RNase_III. 2 hits. |
| PROSITE | PS51327. DICER_DSRBF. 1 hit. PS50137. DS_RBD. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS50821. PAZ. 1 hit. PS00517. RNASE_3_1. 1 hit. PS50142. RNASE_3_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DICER_CRIGR | ||||||||
| Accession | Primary (citable) accession number: A0MQH0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
