Q23972 · SMG_DROME
- ProteinProtein Smaug
- Genesmg
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids999 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevents their translation. Prevents translation of unlocalized nanos in the bulk cytoplasm via the recruitment of cup.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | P-body | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | mRNA binding | |
Molecular Function | mRNA regulatory element binding translation repressor activity | |
Molecular Function | myosin binding | |
Molecular Function | translation repressor activity | |
Biological Process | establishment of RNA localization | |
Biological Process | negative regulation of translation | |
Biological Process | nuclear-transcribed mRNA poly(A) tail shortening | |
Biological Process | piRNA-mediated gene silencing by mRNA destabilization | |
Biological Process | positive regulation of nuclear-transcribed mRNA poly(A) tail shortening | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of mRNA stability |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein Smaug
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ23972
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In the cytoplasm of syncytial embryos, accumulates in discrete foci.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 606 | Reduced RNA-binding. Complete loss; when associated with R-609. | ||||
Sequence: K → A | ||||||
Mutagenesis | 609 | Reduced RNA-binding. Complete loss; when associated with A-606. | ||||
Sequence: R → A | ||||||
Mutagenesis | 611 | Reduced RNA-binding. | ||||
Sequence: H → S or Q | ||||||
Mutagenesis | 612 | Loss of RNA-binding. | ||||
Sequence: K → Q | ||||||
Mutagenesis | 613 | Reduced RNA-binding. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 632 | No effect on RNA-binding; when associated with L-634. | ||||
Sequence: F → L | ||||||
Mutagenesis | 634 | No effect on RNA-binding; when associated with L-632. | ||||
Sequence: Q → L | ||||||
Mutagenesis | 640 | Reduced RNA-binding. | ||||
Sequence: K → S | ||||||
Mutagenesis | 642 | Loss of RNA-binding. | ||||
Sequence: A → H or Q | ||||||
Mutagenesis | 658 | No effect on RNA-binding; when associated with R-665; I-724 and R-749. | ||||
Sequence: N → D | ||||||
Mutagenesis | 665 | No effect on RNA-binding; when associated with D-658; I-724 and R-749. | ||||
Sequence: Q → R | ||||||
Mutagenesis | 724 | No effect on RNA-binding; when associated with D-658; R-665 and R-749. | ||||
Sequence: V → I | ||||||
Mutagenesis | 739 | No effect on RNA-binding. | ||||
Sequence: R → S | ||||||
Mutagenesis | 749 | No effect on RNA-binding; when associated with D-658; I-724 and R-665. | ||||
Sequence: H → R |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000071972 | 1-999 | Protein Smaug | |||
Sequence: MKYATGTDNAMTSGISGQTNNSNSASNEMQPTTSTPTAAHKEATSTATTTATYANGNPNSNANPSQSQPSNALFCEQVTTVTNLFEKWNDCERTVVMYALLKRLRYPSLKFLQYSIDSNLTQNLGTSQTNLSSVVIDINANNPVYLQNLLNAYKTFQPCDLLDAMSSSSSDKDSMPCYGSDFQITTSAQCDERKLYARKEDILHEVLNMLPLLKPGNEEAKLIYLTLIPVAVKDTMQQIVPTELVQQIFSYLLIHPAITSEDRRSLNIWLRHLEDHIQAAAAGLTNRSYFLQPSPQLVAGGSSTGSGSCSSSATSSSTASCSSVASSSLCPASGSRSSRTNDWQTIAPPSKQLQNKLAGDWRGNGGGSSSGSINPLCDNLNGITLNELASSQNSLGLSLEGSSSLVNGVVAGAGSMLGIAGGDDHDTSFSKNGTEILDFDPVTADMGEACSLASSSLCGRNGGNPVEDRSQPPPNLQQQLLQPPPYASILMGNVGDQFGEINRWSLDSKIAALKTRRSNSLTTQTISSCSSSSNSSVITVNDNCSNSTENLAQFANKPRSFSLSIEHQRGALMNSGSDTRLDEFKPNYIKFHTRNVGMSGIGLWLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGVTKGASHKLALCIDKLKERANILNRVEQELLSGQMELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYAVQDDETLGVLMWILDRSIHNEAFMNHASQLKDLKFKLSKMKISMVPKMHHVKPAGVGPNNGNINKPRWNGKTRKCDTKNGSNDRINNRKNSNDMLNFSLNCLPHPLPHHSQQAPPPLPQFDYNGYGGGPSHQPQYKSSSYPSFMGNPQQQPPPPPSSKSHHHPQQMQQMLQQHNHFPALPQQTPPQSHRRSLNNLILVAGGPQQPQQLIFKPGQGVLTNNGSNDNLVLERNQQSQQQQQQRKLSGGVSSAEQQPKKTMAAVVMENLAKFDQHFTLF | ||||||
Modified residue | 564 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 575 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 972 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
At syncytial blastoderm, it is located throughout the bulk cytoplasm and pole plasm. By the time of cellularization, it concentrates at the posterior pole.
Developmental stage
Expressed maternally. The protein accumulates during the first 3 hours after fertilization, and then decreases rapidly.
Gene expression databases
Interaction
Subunit
Interacts with oskar (osk). Binds to the 3'-UTR of nanos (nos). Interacts with cup, which in turn recruits eIF4-E, leading to an indirect interaction between smg and eIF4-E that prevents mRNA translation. Forms a complex with aub, twin, AGO3, nanos mRNA and piRNAs that targets the nanos 3'-untranslated region, in early embryos.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q23972 | cup Q9VMA3 | 4 | EBI-108638, EBI-95398 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-69 | Disordered | ||||
Sequence: MKYATGTDNAMTSGISGQTNNSNSASNEMQPTTSTPTAAHKEATSTATTTATYANGNPNSNANPSQSQP | ||||||
Region | 329-349 | Disordered | ||||
Sequence: LCPASGSRSSRTNDWQTIAPP | ||||||
Region | 583-763 | Interaction with cup | ||||
Sequence: EFKPNYIKFHTRNVGMSGIGLWLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGVTKGASHKLALCIDKLKERANILNRVEQELLSGQMELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYAVQDDETLGVLMWILDRSIHNEAFMNHASQLKDLKFKLSKM | ||||||
Domain | 600-654 | SAM | ||||
Sequence: GIGLWLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGVTKGASHKLALCIDKLK | ||||||
Region | 773-892 | Disordered | ||||
Sequence: HVKPAGVGPNNGNINKPRWNGKTRKCDTKNGSNDRINNRKNSNDMLNFSLNCLPHPLPHHSQQAPPPLPQFDYNGYGGGPSHQPQYKSSSYPSFMGNPQQQPPPPPSSKSHHHPQQMQQM | ||||||
Compositional bias | 792-806 | Basic and acidic residues | ||||
Sequence: NGKTRKCDTKNGSND | ||||||
Compositional bias | 807-821 | Polar residues | ||||
Sequence: RINNRKNSNDMLNFS | ||||||
Compositional bias | 853-868 | Polar residues | ||||
Sequence: SHQPQYKSSSYPSFMG | ||||||
Region | 955-977 | Disordered | ||||
Sequence: QQSQQQQQQRKLSGGVSSAEQQP |
Domain
The SAM domain mediates the association with the 3'-UTR of specific mRNAs.
Sequence similarities
Belongs to the SMAUG family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q23972-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameA
- SynonymsB, C, E
- Length999
- Mass (Da)109,065
- Last updated2004-02-02 v2
- Checksum6EBB615435F07190
Q23972-2
- NameD
- Differences from canonical
- 987-999: ENLAKFDQHFTLF → VSNPNQNQDQHDQPQILINNNNNNSMLNNNLINQQQLQLLAAAAAAVGSGSCLCSNGGGGACVHNICHQSSKNNNHGVDHCLSQSPLGSLGMSPHVTEYKMNDFKSLEQLETLCRQMTEQAMN
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 792-806 | Basic and acidic residues | ||||
Sequence: NGKTRKCDTKNGSND | ||||||
Compositional bias | 807-821 | Polar residues | ||||
Sequence: RINNRKNSNDMLNFS | ||||||
Compositional bias | 853-868 | Polar residues | ||||
Sequence: SHQPQYKSSSYPSFMG | ||||||
Alternative sequence | VSP_039395 | 987-999 | in isoform D | |||
Sequence: ENLAKFDQHFTLF → VSNPNQNQDQHDQPQILINNNNNNSMLNNNLINQQQLQLLAAAAAAVGSGSCLCSNGGGGACVHNICHQSSKNNNHGVDHCLSQSPLGSLGMSPHVTEYKMNDFKSLEQLETLCRQMTEQAMN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF159852 EMBL· GenBank· DDBJ | AAD54965.1 EMBL· GenBank· DDBJ | mRNA | ||
AF132213 EMBL· GenBank· DDBJ | AAF61321.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF50333.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF50334.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | ACL83279.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | ACL83280.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAN11981.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY058607 EMBL· GenBank· DDBJ | AAL13836.1 EMBL· GenBank· DDBJ | mRNA | ||
U03277 EMBL· GenBank· DDBJ | AAA03462.1 EMBL· GenBank· DDBJ | Unassigned DNA | Sequence problems. |