The characterization of a human RHAMM cDNA: conservation of the hyaluronan-binding domains.
A full-length human RHAMM cDNA clone was isolated by a combination of screening a human breast cDNA expression library with the murine RHAMM 2 cDNA as well as 5' RACE and RT-PCR using messenger RNA from human breast cell line (MCF-10A). The full-length cDNA contained 725 aa that encoded an 84 kDa protein. Although the coding region of the human RHAMM cDNA resembles the murine RHAMM v4, it has additional unique N-terminal (489 bp) and C-terminal (33 bp) regions. Also, only 1 of 5 repeat sequences encoded in the murine cDNA are present in human cDNA. The overall homology between the overlapping region of human and mouse RHAMM v4 cDNA clone is 85%, but the HA binding motif (B[X7]B), shown to be critical for the signaling capability of this receptor, is 100% conserved.[1]References
- The characterization of a human RHAMM cDNA: conservation of the hyaluronan-binding domains. Wang, C., Entwistle, J., Hou, G., Li, Q., Turley, E.A. Gene (1996) [Pubmed]
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