Characterization of a novel protein (FGFRL1) from human cartilage related to FGF receptors.
Utilizing a subtractive cDNA cloning approach we have identified a novel protein from human cartilage. This protein represents an integral membrane protein with 504 amino acids and a molecular mass of 55 kDa. It is composed of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. The extracellular domain is closely related to the extracellular domain of FGF receptors. The intracellular domain, however, does not show any similarity to the protein tyrosine kinase domain of FGF receptors. The novel gene (FGFRL1) is located on human chromosome 4 band p16 in close proximity to the gene for FGFR3. Its mRNA is preferentially expressed in cartilaginous tissues. Owing to the structural similarity, it is conceivable that the novel protein plays a role in the modulation of FGF receptor activity.
Wiedemann
M
M
M. E. Müller-Institute, University of Bern, Bern, CH-3010, Switzerland.
Trueb
B
B
D020121:5' Untranslated Regions; D000595:Amino Acid Sequence; D002356:Cartilage / Q000502:physiology*; D002894:Chromosomes, Human, Pair 4; D005091:Exons; D020869:Gene Expression Profiling; D006801:Humans; D007438:Introns; D008969:Molecular Sequence Data; D012326:RNA Splicing; D051500:Receptor, Fibroblast Growth Factor, Type 5; D017468:Receptors, Fibroblast Growth Factor / Q000235:genetics* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D020121:5' Untranslated Regions; C417531:FGFRL1 protein, human; D051500:Receptor, Fibroblast Growth Factor, Type 5; D017468:Receptors, Fibroblast Growth Factor