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Primary Information | |
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| BoMiProt ID | Bomi51 |
| Protein Name | Coatomer subunit alpha |
| Organism | Bos taurus |
| Uniprot ID | Q27954 |
| Milk Fraction | MFGM, Exosome |
| Ref Sequence ID | NP_001099115.1 |
| Aminoacid Length | 1224 |
| Molecular Weight | 138359 |
| FASTA Sequence | Download |
| Gene Name | COPA |
| Gene ID | 100126041 |
| Protein Existence Status | Reviewed:Experimental evidence at protein level |
Secondary Information | |
| Protein Function | export proteins from the endoplasmic reticulum; retrograde transport of luminal and membrane proteins in the ER-Golgi segment of the secretory pathway; play a role in the correct steady-state distribution of proteins within the Golgi stack. alpha-COPI was found to be required for the formation of RER whorls in midgut epithelial cells of unfed Aa. aegypti mosquitoes, as well as for the expression of late phase midgut proteases. |
| Biochemical Properties | involves members of a family of 23–24 kD type-I transmembrane proteins (the p24 family) that are sorted into coat protein (COPI) vesicles where they become a major constituent; COPI subunits of the cytosolic coatomer complex exhibit significant structural heterogeneity; ß-COP exists as three to five distinct species, while δ-COP exists as up to three species with differing pI but identical molecular weights; Ɣ-COP - pI ;5.9 |
| PTMs | As observed in rat liver, ß and δ-COP are phosphorylated |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| SCOP | Class : All alpha proteins Fold : alpha-alpha superhelix Superfamily : TPR-like Family : Coatomer alpha subunit C-terminal region-like Domain Name : 3MKR B:905-1224 Class : Small proteins Fold : RING/U-box Superfamily : RING/U-box like Family : Domain Name : 3MKR B:905-1224 |
| CATH | Matched CATH superfamily 1.25.40.10 |
| Predicted Disorder Regions | |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | Phosphorylation probably alter solubility characteristics |
| PDB ID | 3MKR, |
| Linking IDs | |
| Bibliography | 1. Tu, L., Tai, W. C. S., Chen, L., & Banfield, D. K. (2008). Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science (New York, N.Y.), 321(5887), 404–407. https://doi.org/10.1126/science.1159411. 2. Cosson, P., & Letourneur, F. (1994). Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science (New York, N.Y.), 263(5153), 1629–1631. https://doi.org/10.1126/science.8128252. 3. Letourneur, F., Gaynor, E. C., Hennecke, S., Démollière, C., Duden, R., Emr, S. D., … Cosson, P. (1994). Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell, 79(7), 1199–1207. https://doi.org/10.1016/0092-8674(94)90011-6. 4. Sohn, K., Orci, L., Ravazzola, M., Amherdt, M., Bremser, M., Lottspeich, F., … Wieland, F. T. (1996). A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding. The Journal of Cell Biology, 135(5), 1239–1248. https://doi.org/10.1083/jcb.135.5.1239. 5. Stamnes, M. A., Craighead, M. W., Hoe, M. H., Lampen, N., Geromanos, S., Tempst, P., & Rothman, J. E. (1995). An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding. Proceedings of the National Academy of Sciences of the United States of America, 92(17), 8011–8015. https://doi.org/10.1073/pnas.92.17.8011. 6 Sheff, D., Lowe, M., Kreis, T. E., & Mellman, I. (1996). Biochemical heterogeneity and phosphorylation of coatomer subunits. The Journal of Biological Chemistry, 271(12), 7230–7236. https://doi.org/10.1074/jbc.271.12.7230. 7.Zhou G, Isoe J, Day WA, Miesfeld RL. Alpha-COPI coatomer protein is required for rough endoplasmic reticulum whorl formation in mosquito midgut epithelial cells. PLoS One. 2011 Mar 31;6(3):e18150. doi: 10.1371/journal.pone.0018150. PMID: 21483820; PMCID: PMC3069061. |