Primary Information |
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| BoMiProt ID | Bomi8364 |
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| Protein Name | Protein LSM14 homolog A/Protein FAM61A/RNA-associated protein 55A |
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| Organism | Bos taurus |
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| Uniprot ID | Q3MHF8 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001029826.1 |
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| Aminoacid Length | 463 |
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| Molecular Weight | 50636 |
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| FASTA Sequence |
Download |
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| Gene Name | LSM14A/RAP55A |
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| Gene ID | 538838 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for translationally inactive mRNAs and protect them from degradation.Acts as a repressor of mRNA translation |
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| Biochemical Properties | The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing.The N-terminal LSM domain of LSM14 is a common fold among decapping factors and is also found in the LSM1-7 proteins and EDC3. However, in contrast to LSM1-7 proteins, whose LSM domains interact to form a heteroheptameric ring-like structure with RNA-binding properties, the LSM domains in LSM14 and EDC3 diverge functionally and serve as interaction platforms for other protein factors |
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| PTMs | Acetylation,Methylation and Phosphorylation at Ser and Thr |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q3MHF8|LS14A_BOVIN Protein LSM14 homolog A OS=Bos taurus OX=9913 GN=LSM14A PE=2 SV=1
MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDE
VFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSTSSFQSVGSYGPFGRMPTY
SQFSPSSLVGQQFGAVGVAGSSLTSFGTEASSSSALSQSSVVGSAFTQDSRALKTQLS*178QG
RS*182S*183PQLDPLRKS*192PT*194MEQAVQTASAHLPAPAPVGRRS*216PVSTRPLPSTS*227QKPIENQEHRRAEVHKVSRPENEQLRNDSKRQIVPGAPSAPRRGRGGHRGGRGRFGIRRDGPMKFEKDFDFES
ANAQFNKEEIDREFHNKLKLKEDKLEKQEKPVNGEDKGDSGVDTQNSEGNADEEDPLGPN
CYYDKTKSFFDNISCDDNRERRPTWAEERRLNAETFGIPLR*401PNRGRGGYRGRGGLGFRGG
RGRGSGRGGAFTTPRGFRGGFRGGRGGREFADFEYRKDNKVAA
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| Predicted Disorder Regions | 172-288, 322-359, 398-448 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | SCD6 efficiently interacts with eIF4G1 in a manner dependent on Hmt1-mediated methylation of the SCD6 RGG motif, and that this is required to induce translational repression. |
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| Bibliography | 1.Yang WH, Yu JH, Gulick T, Bloch KD, Bloch DB. RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and stress granules. RNA. 2006 Apr;12(4):547-54. doi: 10.1261/rna.2302706. Epub 2006 Feb 16. PMID: 16484376; PMCID: PMC1421083. 2.Brandmann T, Fakim H, Padamsi Z, Youn JY, Gingras AC, Fabian MR, Jinek M. Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes. EMBO J. 2018 Apr 3;37(7):e97869. doi: 10.15252/embj.201797869. Epub 2018 Mar 6. PMID: 29510985; PMCID: PMC5881628. 3.Poornima G, Shah S, Vignesh V, Parker R, Rajyaguru PI (2016) Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6. Nucleic Acids Res 44: 9358–9368 |
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