CRYGA

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Crystallin, gamma A
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CRYGA ; CRY-g-A; CRYG1; CRYG5
External IDs OMIM123660 MGI88521 HomoloGene129704 GeneCards: CRYGA Gene
RNA expression pattern
PBB GE CRYGA 207587 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1418 12964
Ensembl ENSG00000168582 ENSMUSG00000044429
UniProt P11844 P04345
RefSeq (mRNA) NM_014617 NM_007774
RefSeq (protein) NP_055432 NP_031800
Location (UCSC) Chr 2:
209.03 – 209.03 Mb
Chr 1:
65.1 – 65.1 Mb
PubMed search [1] [2]

Gamma-crystallin A is a protein that in humans is encoded by the CRYGA 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]

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