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Primary Information | |
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| BoMiProt ID | Bomi5931 |
| Protein Name | Gamma-crystallin S/Beta-crystallin S/Gamma-S-crystallin |
| Organism | Bos taurus |
| Uniprot ID | P06504 |
| Milk Fraction | Whey |
| Ref Sequence ID | NP_776717.1 |
| Aminoacid Length | 178 |
| Molecular Weight | 20928 |
| FASTA Sequence | Download |
| Gene Name | CRYGS |
| Gene ID | 281724 |
| Protein Existence Status | reviewed |
Secondary Information | |
| Protein Function | structural component of the adult human lens. play an important role in maintaining lens transparency. |
| Biochemical Properties | has an additional alpha helix,which is located between the third and fourth beta sheets.Contain 4 stranded Greek Key beta sheet peptide/crystallin fold which forms Ca2+ binding site and gives rise to the first calcium ligate at the residue next to the conserved aromatic amino acid in the sequence Y/E/WXXXXXXG,located at the end of the first beta strand.Glycine is necessary to form a dihedral angle which is associated with calcium binding and storage ability.contains a single lysine residue at the second position (K2). |
| Significance in milk | Bovine lens formation |
| PTMs | Acetylation |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | NA |
| SCOP | Class : All beta proteins Fold : gamma-Crystallin-like Superfamily : gamma-Crystallin-like Family : Crystallins/Ca-binding development proteins Domain Name : 1A7H A:87-172 |
| CATH | Matched CATH superfamily 2.60.20.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | Lys 2-(K2) and glycine 1 (G1) is acetylated at an early age and that the amount of K2-acetylated γD-crystallin increased with age. The chaperone ability of α-crystallin for acetylated γD-crystallin was lower than that for the nonacetylated protein.The acetylated protein exhibited higher surface hydrophobicity, was unstable against thermal and chemical denaturation, and exhibited a higher propensity to aggregate at 80 °C in comparison to the nonacetylated protein.Acetylation of K2 and G1 reduced the structural stability of the protein and brought the distal cysteine residues (C18 and C78) into close proximity. |
| PDB ID | 1A7H, |
| Bibliography | DiMauro MA, Nandi SK, Raghavan CT, Kar RK, Wang B, Bhunia A, Nagaraj RH, Biswas A. Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin. Biochemistry. 2014 Nov 25;53(46):7269-82. doi: 10.1021/bi501004y. Epub 2014 Nov 13. PMID: 25393041; PMCID: PMC4245984. |