Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Genetic Screen for Postembryonic Development in the Zebrafish (Danio rerio): Dominant Mutations Affecting Adult Form.
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dmh29 is a dominant glycine substitution in col1a1b with a short-stature skeletal phenotype similar to the col1a1a alleles.
"while the dmh29 mutants exhibit mutations in a glycine residue of the col1a1b gene (G1123D), leading to a very similar phenotype."
Zebrafish Collagen Type I: Molecular and Biochemical Characterization of the Major Structural Protein in Bone and Skin.
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col1a1b is translated; alpha3(I) is present in embryonic and adult type I collagen.
"The identification of α3(I) peptides demonstrated for the first time the translation of the col1a1b gene in zebrafish."
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Adult bone, skin and scales contain about equal amounts of the three chains; homotrimers are not significant.
"a significant presence of α1(I) or α3(I) homotrimers could be excluded in all three tissues"
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The alpha3(I)/alpha1(I) ratio is higher in skin and scales than in bone.
"SRM and spectral counting mass spectrometry data shows a statistically significant higher α3(I)/α1(I) ratio in external (skin and scales) versus internal (bone) tissues"
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col1a1b is co-expressed with col1a1a and col1a2 but not in the fin fold.
"Interestingly, only col1a1a was shown to be expressed in the median fin fold and in the apical ectodermal ridge of the pectoral fin at 48, 72 and 96 hpf"
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pro-alpha3(I) lacks one inter-chain C-propeptide cysteine and has a more divergent chain recognition region.
"Also, the chain recognition region is more divergent in proα3 than in proα1 when compared to mammalian proα1"
Zebrafish type I collagen mutants faithfully recapitulate human type I collagenopathies.
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col1a1b nonsense mutants lack alpha3(I) and are viable; single heterozygotes are normal; double heterozygotes with col1a1a are fragile.
"Homozygous mutant col1a1b−/− mutants [loss of α3(I)] were present by the age of 3 mo, however at reduced numbers if combined with heterozygous loss of col1a1a (col1a1a+/−;col1a1b−/−)."
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The authors interpret alpha1(I) as more abundant, i.e. a dosage asymmetry.
"This suggests a gene/protein dosage effect, where α1(I) is more abundant than α3(I), as hypothesized in our previous work (19)."
Phylogenetic analysis of vertebrate fibrillar collagen locates the position of zebrafish alpha3(I) and suggests an evolutionary link between collagen alpha chains and hox clusters.
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Zebrafish alpha3(I) cDNA cloned; alpha3(I) is phylogenetically closest to alpha1(I) and likely arose by its duplication.
"support the hypothesis that the alpha3(I) chain arose from a duplication of the alpha1(I) gene"
Complete primary structure of rainbow trout type I collagen consisting of alpha1(I)alpha2(I)alpha3(I) heterotrimers.
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In trout, skin collagen is alpha1alpha2alpha3 and muscle collagen is (alpha1)2alpha2; alpha3(I) has many Gly-Gly doublets.
"The subunit compositions of skin and muscle type I collagens from rainbow trout were found to be alpha1(I)alpha2(I)alpha3(I) and [alpha1(I)](2)alpha2(I), respectively."
Fish skin type I collagen: wide distribution of an alpha 3 subunit in teleosts.
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alpha3 is found in skin collagen of many but not all teleosts.
"The skin collagen seems to exist as an alpha 1 alpha 2 alpha 3 heterotrimer in many teleosts and as an (alpha 1)2 alpha 2 heterotrimer in some teleosts."
Wide distribution of the skin type I collagen alpha 3 chain in bony fish.
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An alpha3(I)-like chain was detected in white sturgeon skin collagen.
"The present study, however, has revealed the occurrence of alpha 3(I) in a chondrostean fish, white sturgeon."
Phylogenetic analyses of ray-finned fishes (Actinopterygii) using collagen type I protein sequences.
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alpha3(I) evolves fastest of the three chains and is absent from some teleosts (two cyprinid genera, herring).
"This chain is, however, apparently absent from two of the five genera of cyprinids"
C-propeptide cysteine comparison of col1a1a and col1a1b