Abstract
The RFP-TM protein family was first described in Caenorhabditis elegans as hypothetical transmembrane proteins containing a conserved 350–400 amino acid domain including the invariant peptide motif RFP. The VMD2 gene underlying Best disease was shown to represent the first human member of the RFP-TM protein family. More than 97% of the disease-causing mutations are located in the N-terminal RFP-TM domain implying important functional properties. Here, we have identified three novel VMD2-related human genes (VMD2L1, VMD2L2 and VMD2L3) demonstrating a high degree of conservation in their respective RFP-TM domains. Each of the VMD2-like proteins has a unique C-terminus that lack similarity to other proteins or motifs. By FISH analysis, VMD2L1 was localised to chromosome 19p13.2-p13.12, VMD2L2 to 1p32.3-p33 and VMD2L3 to 12q14.2-q15. RT–PCR analyses revealed tissue-restricted expression of the three genes with both VMD2L1 and VMD2L2 abundantly transcribed in colon. VMD2L1 is present in the retinal pigment epithelium while VMD2L3 shows predominant expression in skeletal muscle.
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References
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Acknowledgements
This work was supported in part by a grant from the Bundesministerium für Bildung und Forschung (BMBF) under 01KW9921 and the Deutsche Forschungsgemeinschaft (DFG) (WE 1259/13-1). The sequence data reported in this paper have been submitted to GenBank and have been assigned the accession numbers AF440756 (cDNA sequence for VMD2L1), AF440757 (cDNA sequence for VMD2L2) and AF440758 (cDNA sequence for VMD2L3).
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Stöhr, H., Marquardt, A., Nanda, I. et al. Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family. Eur J Hum Genet 10, 281–284 (2002). https://doi.org/10.1038/sj.ejhg.5200796
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DOI: https://doi.org/10.1038/sj.ejhg.5200796
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