Search by BoMiProt ID - Bomi51

Primary Information

BoMiProt ID Bomi51
Protein Name Coatomer subunit alpha
Organism Bos taurus
Uniprot IdQ27954
Milk FractionMFGM, Exosome
Ref Sequence Id NP_001099115.1
Amino Acid Lenth 1224
Molecular Weight 138359
Fasta Sequence
Gene Name COPA
Gene Id 100126041
Protein Existence Status Reviewed:Experimental evidence at protein level

Secondry 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
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
Significance of PTMs Phosphorylation probably alter solubility characteristics
Linking IDs Bomi688 Bomi689 Bomi690 Bomi691 Bomi692
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.
2. Cosson, P., & Letourneur, F. (1994). Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science (New York, N.Y.), 263(5153), 1629–1631.
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.
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.
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.
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.