CRYGA
Sign in to saveAlso known as CRY-g-A, CRYG1, CRYG5, crystallin gamma A
Gamma-crystallin A is a protein that in humans is encoded by the CRYGA gene.
Gene data
CRYGA- Name
- crystallin gamma A
- Type
- protein-coding
- Position
- 208,160,740–208,163,589 (−)
- Aliases
- CRY-g-A, CRYG1, CRYG5
- Ensembl
- ENSG00000168582
- RefSeq RNA
- NM_014617.4
- RefSeq protein
- NP_055432.2
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. [provided by RefSeq, Jul 2008].
Gene Ontology
Biological process
Molecular function
via MyGene.info
Wikidata facts
Show 5 more facts
- HomoloGene ID
- 129704
- genomic start
- 209025464
- exact match
- identifiers.org/ncbigene/1418
- genomic end
- 208163589
- cytogenetic location
- 2q33.3
Sources (3)
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Gamma-crystallin A is a protein that in humans is encoded by the CRYGA gene.
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.