Crystallin, gamma D

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Crystallin, gamma D
Protein CRYGD PDB 1h4a.png
PDB rendering based on 1h4a.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CRYGD ; CACA; CCA3; CCP; CRYG4; CTRCT4; PCC; cry-g-D
External IDs OMIM123690 MGI88524 HomoloGene36213 GeneCards: CRYGD Gene
RNA expression pattern
PBB GE CRYGD 207532 at tn.png
More reference expression data
Species Human Mouse
Entrez 1421 12967
Ensembl ENSG00000118231 ENSMUSG00000067299
UniProt P07320 P04342
RefSeq (mRNA) NM_006891 NM_007776
RefSeq (protein) NP_008822 NP_031802
Location (UCSC) Chr 2:
208.99 – 208.99 Mb
Chr 1:
65.06 – 65.06 Mb
PubMed search [1] [2]

Gamma-crystallin D is a protein that in humans is encoded by the CRYGD gene.[1]

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.[1]


Further reading[edit]