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Primary Information | |
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| BoMiProt ID | Bomi50 |
| Protein Name | Clathrin light chain A |
| Organism | Bos taurus |
| Uniprot ID | P04973 |
| Milk Fraction | Exosome |
| Ref Sequence ID | NP_776447.1 |
| Aminoacid Length | 213 |
| Molecular Weight | 23308 |
| FASTA Sequence | Download |
| Gene Name | CLTA |
| Gene ID | 281078 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary 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 |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| CATH | Matched CATH superfamily n/a |
| Predicted Disorder Regions | 1-172,184-208,215-243 |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | Phosphorylation Regulates Their Interaction with Clathrin |
| PDB ID | 1XI4, 3IYV, |
| Linking IDs | |
| 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. |