Open AccessStructure of the chicken link protein gene: exons correlate with the protein domains.
Author(s) -
Ibolya Kiss,
F. Deák,
S. Mestric,
Hajo Delius,
J. Soós,
Katalin Dekany,
W. Scott Argraves,
Kenneth J. Sparks,
Paul F. Goetinck
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.18.6399
Subject(s) - exon , exon shuffling , tandem exon duplication , biology , gene , exon trapping , genetics , intron , untranslated region , gene duplication , coding region , snap23 , microbiology and biotechnology , alternative splicing , hspa2 , peptide sequence , rna
The structure of the chicken link protein gene has been determined from a series of genomic clones that cover the entire coding region as well as the complete 3'-untranslated region and a small portion of the 5'-untranslated region. The gene is greater than 80 kilobase pairs long and is present in a single copy in the chicken genome. The link protein gene contains at least five exons with four encoding the entire protein. The domain of link protein that has homologies with immunoglobulin-like proteins and the tandemly repeated hyaluronic acid binding domains are each encoded by separate exons. The exon-intron structure indicates that the link protein gene may have arisen by exon duplication and exon shuffling.