CRYGD
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1H4A, 1HK0, 2G98, 2KFB, 2KLJ, 4GR7, 4JGF
Identifiers
Aliases	CRYGD, CACA, CCA3, CCP, CRYG4, CTRCT4, PCC, cry-g-D, crystallin gamma D
External IDs	OMIM: 123690 MGI: 88524 HomoloGene: 36213 GeneCards: CRYGD
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q33.3 Start 208,121,607 bp[1] End 208,124,524 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 C2|1 32.8 cM Start 65,101,031 bp[2] End 65,102,611 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence lens hypothalamus substantia nigra prefrontal cortex temporal lobe amygdala dorsolateral prefrontal cortex Brodmann area 9 putamen Top expressed in conjunctival fornix retinal pigment epithelium occiput ciliary body occipital bone iris Meckel's cartilage rib sphenoid bone lateral part of occipital bone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding structural constituent of eye lens Cellular component nucleus cytoplasm Biological process cellular response to reactive oxygen species response to stimulus visual perception lens development in camera-type eye lens fiber cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1421 12967 Ensembl ENSG00000118231 ENSG00000285434 ENSMUSG00000067299 UniProt P07320 P04342 RefSeq (mRNA) NM_006891 NM_007776 RefSeq (protein) NP_008822 NP_031802 Location (UCSC) Chr 2: 208.12 – 208.12 Mb Chr 1: 65.1 – 65.1 Mb PubMed search [3] [4]
Wikidata
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Gamma-crystallin D is a protein that in humans is encoded by the CRYGD gene.^[5]

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.^[5]