RGD Reference Report - Rat lens beta-crystallins are internally duplicated and homologous to gamma-crystallins. - Rat Genome Database

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Rat lens beta-crystallins are internally duplicated and homologous to gamma-crystallins.

Authors: Den Dunnen, JT  Moormann, RJ  Schoenmakers, JG 
Citation: den Dunnen JT, etal., Biochim Biophys Acta 1985 Apr 19;824(4):295-303.
RGD ID: 61560
Pubmed: PMID:3879970   (View Abstract at PubMed)

The nucleotide sequence of two cloned rat lens beta-crystallin cDNAs pRL beta B3-2 and pRL beta B1-3 has been determined. pRL beta B3-2 contains the complete coding information for a beta-crystallin, designated beta B3, of 210 amino acid residues. pRL beta B1-3 is incomplete at its 5' end; the 5' codogenic information which is not present in this cDNA clone was deduced from the cloned gene. pRL beta B1-3 codes for a beta-crystallin polypeptide, designated beta B1, whose full length is 247 amino acid residues. Considerable sequence homology is noted between the amino- and carboxy-terminal halves of each protein. The two rat beta-crystallins show a substantial sequence homology with each other (60%) as well as with the published sequences of rat gamma-crystallin (37%) and bovine and murine beta-crystallins (55 and 45%). All these proteins have a two-domain structure which, like the bovine gamma II-crystallin, might be folded into four remarkably similar protein motifs. Our data further indicate that the beta-crystallins can be subdivided into two groups which are evolutionarily related. Both groups are, although more distantly, also related to the gamma-crystallins.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Crybb3Ratstructural constituent of eye lens  TAS  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Crybb3  (crystallin, beta B3)

Objects referenced in this article
Gene Crybb1 crystallin, beta B1 Rattus norvegicus

Additional Information