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
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,
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
Predicted Disorder Regions
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Phosphorylation probably alter solubility characteristics
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.
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. 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.