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The cell matrix adhesion regulator (CMAR) gene has been suggested to be a signal transduction molecule influencing cell adhesion to collagen and, through this, possibly involved in tumor suppression. The originally reported CMAR cDNA was 464 bp long with a tyrosine phosphorylation site at the extreme 3' end, which mutagenesis studies had shown to be central to the function of this gene. Since the discovery of a 4-bp insertion polymorphism within the originally reported coding region, further sequence information has been obtained. The cDNA has been extended 5' by approximately 2 kb revealing a 559-bp region showing strong homology to the proposed 5' untranslated sequence of a murine protein kinase receptor family member, variant in kinase (vik). CMAR genomic sequencing has shown the presence of an intron, the intron/exon boundary lying within this region of homology. An RNA transcript for CMAR of approximately 2.5 kb has also been identified. The data suggest complex mechanisms for control of expression of two closely associated genes, CMAR and the vik- associated sequence.

Type

Journal article

Journal

Proc Natl Acad Sci U S A

Publication Date

23/12/1997

Volume

94

Pages

14578 - 14583

Keywords

ATPases Associated with Diverse Cellular Activities, Animals, Base Sequence, Cell Adhesion Molecules, Cell Line, DNA, Complementary, Genome, Human, Humans, Metalloendopeptidases, Molecular Sequence Data, Receptors, Virus, Sequence Alignment, Sequence Analysis, DNA