Organization of the human CD9 gene.

Abstract

The CD9 antigen was originally described as a 24-kDa molecule present on B-lineage-derived acute lymphoblastic leukemia cells and developing B lymphocytes. Platelets also express a large amount of CD9 antigen and can be activated by CD9 antibodies. We report here the structure of the CD9 gene, which is composed of 8 exons spanning more than 20 kb. There is no TATA or CAAT box in the 5'-flanking domain of the CD9 gene, but a 120-bp region extremely rich in C and G (88%) contains several Sp 1 binding sites and a consensus site for the binding of zinc-finger proteins of the Krox/EGR family. The CD9 antigen belongs to a new cell surface protein family. The organization of its gene closely resembles the organization of the genes for two other members of this protein family, TAPA1 and CD63, which share with CD9 respectively 45 and 25% identity at the amino acid level.

• Authors: E Rubinstein, P Benoit, M Billard, S Plaisance, M Prenant, G Uzan, C Boucheix
• Journal: Genomics (Genomics) Vol. 16 Issue 1 Pg. 132-8 (Apr 1993) ISSN: 0888-7543 [Print] United States
• PMID: 8486348 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antigens, CD
• CD9 protein, human
• Cd9 protein, mouse
• Membrane Glycoproteins
• Tetraspanin 29
• DNA

Topics

• Amino Acid Sequence
• Animals
• Antigens, CD (genetics)
• Base Sequence
• Chromosome Mapping
• Cloning, Molecular
• Consensus Sequence
• DNA (genetics)
• Exons
• Humans
• Introns
• Membrane Glycoproteins
• Mice
• Molecular Sequence Data
• Sequence Homology, Amino Acid
• Sequence Homology, Nucleic Acid
• Tetraspanin 29
• Transcription, Genetic