CRYGS

From Wikipedia, the free encyclopedia
Crystallin, gamma S

PDB rendering based on 1a7h.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsCRYGS; CRYG8
External IDsOMIM: 123730 MGI: 1298216 HomoloGene: 40695 GeneCards: CRYGS Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez142712970
EnsemblENSG00000213139ENSMUSG00000033501
UniProtP22914O35486
RefSeq (mRNA)NM_017541NM_009967
RefSeq (protein)NP_060011NP_034097
Location (UCSC)Chr 3:
186.26 – 186.26 Mb
Chr 16:
22.81 – 22.81 Mb
PubMed search

Beta-crystallin S is a protein that in humans is encoded by the CRYGS 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. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue. 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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