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J. Biol. Chem., Vol. 264, Issue 14, 8126-8134, 05, 1989
I Kiss, F Deak, RG Holloway Jr, H Delius, KA Mebust, E Frimberger, WS Argraves, PA Tsonis, N Winterbottom and PF Goetinck
The entire gene for chicken cartilage matrix protein (CMP) has been
isolated and characterized by restriction mapping, electron microscopy,
nuclease S1 mapping, and sequence analysis. The gene, which is present in a
single copy in the chicken genome, is 18 kilobase pairs long and comprises
eight exons and seven introns. It has two transcription initiation sites, 8
base pairs from each other. A sequence very homologous to the consensus
nuclear factor III binding-site sequence, a CAT- and a TATA-like sequence
are found in the promoter region and ATTAAA is used as a polyadenylation
signal. The nucleotide sequence defines a primary translation product of
493 amino acids which consists of a 23-amino acid signal peptide and two
large repeated domains connected by an epidermal growth factor module.
Amino acid sequences homologous to those of the repeated domains are
present in the type A repeats of von Willebrand factor, complement factors
B and C2, and in the alpha chains of the integrins Mac-1, p150,95, and
LFA-1. The exon- intron structure indicates that the CMP gene may have
arisen by exon duplication and exon shuffling during evolution. The GT-AG
splice rule cannot be applied for the excision of the last intron of the
CMP pre- mRNA. The donor splice site of intron G is basically different
from the consensus sequence indicating that a novel type of splicing
mechanism might exist in cartilage.
Structure of the gene for cartilage matrix protein, a modular protein of the extracellular matrix. Exon/intron organization, unusual splice sites, and relation to alpha chains of beta 2 integrins, von Willebrand factor, complement factors B and C2, and epidermal growth factor
Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged.
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