Search by BoMiProt ID - Bomi5931

Primary Information

BoMiProt ID Bomi5931
Protein Name Gamma-crystallin S/Beta-crystallin S/Gamma-S-crystallin
Organism Bos taurus
Uniprot IDP06504
Milk FractionWhey
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,
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
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.
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.