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An orphan nuclear receptor lacking a zinc-finger DNA-binding domain: interaction with several nuclear receptors1

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Abstract

The yeast two-hybrid screening was applied to cloning cDNAs of proteins that interact with peroxisome proliferator-activated receptor α (PPARα). We obtained from a rat liver cDNA library a clone encoding a protein related to the ligand-binding domain of the members of nuclear hormone receptor superfamily, whereas apparently lacking the zinc-finger DNA-binding domain. This protein interacted with the activated forms of several nuclear receptors, and thus is a novel type of heterodimer-forming nuclear receptor.

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    SHP is also detected in mouse mesenteric, epididymal, and subcutaneous fat tissues by reverse transcriptase polymerase chain reaction (RT‐PCR) (Nishizawa et al., 2002). Rat SHP mRNA was detected in the liver, heart, and to a lesser extent in skeletal muscle, kidney, testis, lung, and spleen by Northern analysis (Masuda et al., 1997). It was also detected in the epididymis, prostate, testis, uterus, colon, small intestine, bladder, stomach, spleen, lung, liver, thymus, heart, adrenal, spinal cord, olfactory lobes, and cerebellum (Johansson et al., 1999).

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1

The present nucleotide sequences are available on the DDBJ/EMBL/GenBank databases with the accession numbers D86580 (cDNA), D86745 (genomic sequence around exon 1), and D86839 (genomic sequence around exon 2).

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