Use of the ND evidence code for Gene Ontology (GO) terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Gene duplication and separation of functions in alphaB-crystallin from zebrafish (Danio rerio).
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Zebrafish express two alphaB-crystallins. cryabb (alphaB2) has constitutive expression in heart, brain, skeletal muscle, liver, and lens, retaining the broad expression of mammalian CRYAB. cryabb shows greater chaperone-like activity than human CRYAB at 25-30 degrees C. After gene duplication, cryabb maintained the widespread protective role of mammalian CRYAB while cryaba adopted a lens-specific role.
"zebrafish alphaB2 maintained the widespread protective role also found in mammalian alphaB-crystallin, while zebrafish alphaB1 adopted a more restricted, nonchaperone role in the lens."
In vivo characterization of human myofibrillar myopathy genes in zebrafish.
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Morpholino knockdown of myofibrillar myopathy genes including cryabb in zebrafish led to compromised skeletal muscle function, myofibrillar degeneration, and severe heart failure.
"targeted ablation of MFM genes in zebrafish led to compromised skeletal muscle function mostly due to myofibrillar degeneration as well as severe heart failure."
Loss of αBa-crystallin, but not αA-crystallin, increases age-related cataract in the zebrafish lens.
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The study examined all three alpha-crystallin mutant zebrafish lines for age-related cataract. cryabb contributes to lens maintenance alongside cryaa and cryaba.
"zebrafish express one lens-specific alphaA-crystallin gene (cryaa), they express two alphaB-crystallin genes, with one evolving lens specificity (cryaba) and the other retaining the broad expression of its mammalian ortholog (cryabb)."
Falcon deep research report on zebrafish cryabb (alphaB-crystallin B b)
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Crystallins are soluble cytoplasmic proteins in vertebrate optical
tissues, supporting a primary intracellular/cytosolic localization for
cryabb. ECM mentions for the alphaB-crystallin family should be read as
tissue-level association, not as evidence that cryabb itself is secreted.
"crystallins are described as **soluble cytoplasmic** proteins in vertebrate optical tissues, supporting a primary **intracellular/cytosolic** localization"
Gene Ontology annotation through association of InterPro records with GO terms
Genome-wide analysis and expression profiling of the small heat shock proteins in zebrafish.
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cryabb (hspb5b) is one of thirteen zebrafish sHSPs; EST data place the lens alpha-crystallins hspb4, hspb5a and hspb5b predominantly in lens libraries, and hspb5b is not among the sHSPs upregulated more than five-fold by a one-hour 37 degrees C heat shock.
"In response to a one-hour heat shock at 37°C, we found the expression of several sHSPs, hspb1, hspb4, hspb8, hspb9 , and hspb11 , to be upregulated more than five-fold at one or more stages of development"
Interplay between Nrf2 and αB-crystallin in the lens and heart of zebrafish under proteostatic stress.
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cryabb transcription is induced by oxidative (tBHP) and glucocorticoid (dexamethasone) stress and strongly upregulated in Nrf2-deficient heart and brain; cryabb null embryos show lens defects and stress-potentiated cardiac edema.
"Our data suggest that cryabb functions as a stress–response gene regulated by both glucocorticoid stress and oxidative stress."
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Loss of either zebrafish alphaB-crystallin causes embryonic lens defects and a cardiac edema phenotype.
"In addition to lens defects, the loss of αB-crystallin function is associated with a cardiac phenotype that presents as embryonic cardiac edema (Mishra et al., 2018)."