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Available structures
PDB Ortholog search: PDBe RCSB
Aliases CRYGA, CRY-g-A, CRYG1, CRYG5, crystallin gamma A
External IDs MGI: 88521 HomoloGene: 129704 GeneCards: CRYGA
Gene location (Human)
Chromosome 2 (human)
Chr. Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for CRYGA
Genomic location for CRYGA
Band 2q33.3 Start 208,160,740 bp[1]
End 208,163,576 bp[1]
RNA expression pattern
PBB GE CRYGA 207587 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 2: 208.16 – 208.16 Mb Chr 1: 65.1 – 65.1 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Gamma-crystallin A is a protein that in humans is encoded by the CRYGA gene.[5]

{{PBB_Summary | section_title = | summary_text = 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] }}


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