CRYGS: Difference between revisions

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(This gene was incorrectly identified as encoding for a beta-crystallin S protein, when it actually encodes for a gamma-crystallin S protein.)
 
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'''Beta-crystallin S''' is a [[protein]] that in humans is encoded by the ''CRYGS'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRYGS crystallin, gamma S| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1427| accessdate = }}</ref>
'''Gamma-crystallin S''' is a [[protein]] that in humans is encoded by the ''CRYGS'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRYGS crystallin, gamma S| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1427| accessdate = }}</ref>


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| 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. 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.<ref name="entrez" />
| summary_text = [[Crystallins]] are separated into two classes: taxon-specific, or [[enzyme]], and ubiquitous. The latter class constitutes the major [[Protein|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.<ref name="entrez" />
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Latest revision as of 19:44, 31 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Gamma-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

  1. ↑ 1.0 1.1 "Entrez Gene: CRYGS crystallin, gamma S".

External links

Further reading



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