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- Crystallin,_beta_A1 abstract "Beta-crystallin A3 is a protein that in humans is encoded by the CRYBA1 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. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.".
- Crystallin,_beta_A1 entrezgene "1411".
- Crystallin,_beta_A1 wikiPageID "14798551".
- Crystallin,_beta_A1 wikiPageRevisionID "593884268".
- Crystallin,_beta_A1 hasPhotoCollection Crystallin,_beta_A1.
- Crystallin,_beta_A1 requireManualInspection "no".
- Crystallin,_beta_A1 summaryText "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. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension . Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, encodes two proteins from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.".
- Crystallin,_beta_A1 updateCitations "yes".
- Crystallin,_beta_A1 updatePage "yes".
- Crystallin,_beta_A1 updateProteinBox "yes".
- Crystallin,_beta_A1 updateSummary "yes".
- Crystallin,_beta_A1 type Biomolecule.
- Crystallin,_beta_A1 type Protein.
- Crystallin,_beta_A1 type BiologicalObject.
- Crystallin,_beta_A1 comment "Beta-crystallin A3 is a protein that in humans is encoded by the CRYBA1 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.".
- Crystallin,_beta_A1 label "Crystallin, beta A1".
- Crystallin,_beta_A1 sameAs m.03gybx7.
- Crystallin,_beta_A1 sameAs Q5191428.
- Crystallin,_beta_A1 sameAs Q5191428.
- Crystallin,_beta_A1 sameAs CRYBA1.
- Crystallin,_beta_A1 wasDerivedFrom Crystallin,_beta_A1?oldid=593884268.
- Crystallin,_beta_A1 isPrimaryTopicOf Crystallin,_beta_A1.