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- Sequence Verification
CRYBA1, crystallin beta A1
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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'. [provided by RefSeq, Jul 2008]
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Gene Synonyms (beta-crystallin A3, beta crystallin A3 chain transcript CN, beta crystallin A3 chain transcript LAM, beta crystallin A3 chain transcript PS, beta crystallin A3 chain transcript TC, crystallin beta A3/A1, crystallin, beta A3, eye lens structural protein, truncated beta crystallin A3/A1 chain, truncated beta-crystallin A3, CRYB1, CTRCT10,)
- NCBI Gene ID:
1411
- Species:
Homo sapiens (Human)
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UNIPROT ID#>>P05813
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for this Gene »
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crystallin beta A1 interacts with:
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