Primary Information
BoMiProt ID	Bomi43
Protein Name	AP-2 complex subunit alpha-2
Organism	Bos taurus
Uniprot ID	Q0VCK5
Milk Fraction	Exosome
Ref Sequence ID	NP_001069170.1
Aminoacid Length	938
Molecular Weight	103769
FASTA Sequence	Download
Gene Name	AP2A2
Gene ID	515216
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Protein Function	AP-2 facilitates clathrin-mediated endocytosis of a wide range of proteins including receptors, adhesion molecules and viral proteins; mediate intracellular membrane trafficking along endocytic and secretory transport pathways; AP complexes localize to different intracellular compartments and mediate membrane trafficking in distinct pathways; recognize and concentrate cargo proteins into vesicular carriers that mediate transport from a donor membrane to a target organellar membrane; play important roles in maintaining the normal physiological function of eukaryotic cells
Biochemical Properties	heterotetrameric protein complexes; five different AP complexes: AP-1, AP-2 and AP-3 are clathrin-associated complexes; whereas AP-4 and AP-5 are not; selective recruitment of AP-2 to plasma membrane occurs by binding of the α and μ2 subunits to PIP2; ADP-ribosylation factor) 6 may also contribute to the membrane recruitment of AP-2;
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	609-621,622-677
DisProt Annotation
TM Helix Prediction	No TM helices
Linking IDs
Bibliography	1. Nolen, B. J., Littlefield, R. S., & Pollard, T. D. (2004). Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP. Proceedings of the National Academy of Sciences of the United States of America, 101(44), 15627–15632. https://doi.org/10.1073/pnas.0407149101. 2. Jackson, L. P., Kelly, B. T., McCoy, A. J., Gaffry, T., James, L. C., Collins, B. M., … Owen, D. J. (2010). A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. Cell, 141(7), 1220–1229. https://doi.org/10.1016/j.cell.2010.05.006. 3. Rappoport, J. Z., & Simon, S. M. (2009). Endocytic trafficking of activated EGFR is AP-2 dependent and occurs through preformed clathrin spots. Journal of Cell Science, 122(Pt 9), 1301–1305. https://doi.org/10.1242/jcs.040030. 4. Holloway, Z. G., Velayos-Baeza, A., Howell, G. J., Levecque, C., Ponnambalam, S., Sztul, E., & Monaco, A. P. (2013). Trafficking of the Menkes copper transporter ATP7A is regulated by clathrin-, AP-2-, AP-1-, and Rab22-dependent steps. Molecular Biology of the Cell, 24(11), 1735–1748, S1-8. https://doi.org/10.1091/mbc.E12-08-0625. 5. Kastning, K., Kukhtina, V., Kittler, J. T., Chen, G., Pechstein, A., Enders, S., … Haucke, V. (2007). Molecular determinants for the interaction between AMPA receptors and the clathrin adaptor complex AP-2. Proceedings of the National Academy of Sciences of the United States of America, 104(8), 2991–2996. https://doi.org/10.1073/pnas.0611170104.