The human homologue of the recently cloned murine IL-13 binding protein (IL-13Ral) was cloned from a cDNA library derived from the carcinoma cell line CAKI-1. The cloned cDNA encodes a 427 amino acid protein with two consensus patterns characteristic of the hematopoietic cytokine receptor family and a short cytoplasmic tail. The human protein is 74% identical to the murine IL-13Ral, and 27% identical to the human IL-13Ra2. CHO cells expressing recombinant hlL13Ral specifically bind IL-13 (Äd~4 nM) but not IL-4. Coexpression of the cloned cDNA with that of IL-4Ra resulted in a receptor complex that displayed high affinity for IL-13 (Κ^ ~ 30 pM), and that allowed cross-competition of IL-13 and IL-4. Electrophoretic mobility shift assay showed that IL-13 and IL-4 were able to activate Stat6 in cells expressing both IL-4Roc and IL-13Ral, while no activation was observed in cells expressing either one or the other alone.

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In the fission yeast, four genes (rpaP1-1, rpaP1-3, rpaP2-2, and rpaP2-4) encoding two variants of the RpaP1 and RpaP2 ribosomal proteins (rp) have been characterized. We have identified cDNA for additional variants called RpaP1.5 and RpaP2.6. Sequence comparison suggests that RpaP1.5 diverged before RpaP1.1 and RpaP1.3 and that RpaP2.6 is closer to RpaP2.2 than to RpaP2.4. The corresponding genes, rpaP1-5 and rpaP2-6, are transcribed coordinately with other rp genes.

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