Search by BoMiProt ID - Bomi50


Primary Information

BoMiProt ID Bomi50
Protein Name Clathrin light chain A
Organism Bos taurus
Uniprot IdP04973
Milk FractionExosome
Ref Sequence Id NP_776447.1
Amino Acid Lenth 213
Molecular Weight 23308
Fasta Sequence https://www.uniprot.org/uniprot/P04973-2.fasta
Gene Name CLTA
Gene Id 281078
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function essential for clathrin-mediated endocytosis (CME) in mammalian cells; involved in coating membranes that are endocytosed from the plasma membrane and those that move between the trans-Golgi network (TGN) and endosomes
Biochemical Properties Clathrin was found to be a trimeric assembly of three heavy chains each with an associated light chain and three-legged structure (triskelion), that is the assembly unit of a clathrin coat; Clathrin has a sedimentation constant near 8 S; readily released from coated vesicles and can be polymerized to form a polygonal structure closely resembling that found on coated vesicles; When clathrin solutions (pH 8.0, 0.01 M Tris) containing Ca2+ were titrated to pH 6.45, 300S was formed, without Ca2+, only 150S was observed; 300S species was the major product formed at pH 6.5, 0.10 M ammonium acetate and 0.05 M Mes; 150S baskets are exclusively formed either at pH values above 6.40 by dialysis or at lower pH values by titration; Reducing the pH from 6.5 to 6.0 also had no effect on the stability of 150S baskets;
PTMs clathrin coated vescilces are phosphorylated in the following places: subunit, AP2 - S ß1 subunit, API - S ß2 subunit, AP2 - S µ1 of AP 1 - S/ T µ2 of AP2 - S (T) LCa - S LCb - S Clathrin heavy chain - Y S
Significance of PTMs Phosphorylation Regulates Their Interaction with Clathrin
PDB ID 1XI4, 3IYV,
Linking IDs Bomi673
Bibliography 1. Irace, G., Lippoldt, R. E., Edelhoch, H., & Nandi, P. K. (1982). Properties of clathrin coat structures. Biochemistry, 21(23), 5764–5769. https://doi.org/10.1021/bi00266a006.
2. Wilde, A., & Brodsky, F. M. (1996). In vivo phosphorylation of adaptors regulates their interaction with clathrin. The Journal of Cell Biology, 135(3), 635–645. https://doi.org/10.1083/jcb.135.3.635.
3. Kirchhausen, T., & Harrison, S. C. (1981). Protein organization in clathrin trimers. Cell, 23(3), 755–761. https://doi.org/10.1016/0092-8674(81)90439-6.