CRYGA

From Wikipedia, the free encyclopedia
Crystallin, gamma A
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsCRYGA; CRY-g-A; CRYG1; CRYG5
External IDsOMIM: 123660 MGI: 88521 HomoloGene: 129704 GeneCards: CRYGA Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez141812964
EnsemblENSG00000168582ENSMUSG00000044429
UniProtP11844P04345
RefSeq (mRNA)NM_014617NM_007774
RefSeq (protein)NP_055432NP_031800
Location (UCSC)Chr 2:
209.03 – 209.03 Mb
Chr 1:
65.1 – 65.1 Mb
PubMed search

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]

References

Further reading

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