caa a22 4500 397557957 CHVBK 20180308164808.0 cr unu---uuuuu 161202e199610 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021485 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021485 Identification and Cloning of a Novel cDNA Belonging to Tetratricopeptide Repeat Gene Family from Down Syndrome-Critical Region 21q22.2 [Elektronische Daten] [Fujiko Tsukahara, Masahira Hattori, Takamura Muraki, Yoshiyuki Sakaki] We identified and cloned a novel 9,078-bp cDNA, designated TPRDI, from the Down syndrome-critical region by exon trapping. The cDNA encodes a putative protein (TPRDI) of 2,025 amino acid residues. Two isoforms, TPRDII (8,992 bp) and TPRDIII (7,416 bp), were also isolated. TPRDII, which is probably an alternative splicing product from the TPRD gene transcript, encodes two large open reading frames (ORFs) of 200 amino acid residues and 1,792 amino acid residues, respectively. TPRDIII, which is probably generated by transcription from an alternative start site of the TPRD gene, encodes a putative protein of 1,715 amino acid residues (TPRDIII). Northern blot analysis revealed that TPRDI and its isoforms are present in 7-17 day mouse embryo and in all the human adult and fetal tissues examined. TPRDI has three units of a 34-amino-acid repeat similar to the tetratricopeptide repeat (TPR) motif, which may mediate interaction with various proteins. A larger ORF encoded by TPRDII also has three units of TPR motif, but TPRDIII has only two-thirds of this motif unit. Thus, the TPRD gene may belong to the TPR gene family. Near-central and C terminal regions of TPRDs showed some homology to several matrix proteins such as trichohyalin and bullous pemphigoid antigen. It is possible that the TPRD gene is one of the genes whose overexpression causes several morphological anomalies observed in Down syndrome. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence cDNA cloning nationallicence Down syndrome nationallicence exon trapping nationallicence tetratricopeptide repeat nationallicence Tsukahara Fujiko Department of Pharmacology, Tokyo Women's Medical College 8-1 Kawada-cho, Shinjuku-ku Tokyo 162 aut Hattori Masahira Human Genome Center, Institute of Medical Science, The University of Tokyo 4-6-1 Shiroganedai, Minato-ku Tokyo 108 aut Muraki Takamura Department of Pharmacology, Tokyo Women's Medical College 8-1 Kawada-cho, Shinjuku-ku Tokyo 162 aut Sakaki Yoshiyuki Human Genome Center, Institute of Medical Science, The University of Tokyo 4-6-1 Shiroganedai, Minato-ku Tokyo 108 aut The Journal of Biochemistry Oxford University Press 120/4(1996-10), 820-827 0021-924X 120:4<820 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021485 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021485 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tsukahara Fujiko Department of Pharmacology, Tokyo Women's Medical College 8-1 Kawada-cho, Shinjuku-ku Tokyo 162 aut NATIONALLICENCE 700 1- Hattori Masahira Human Genome Center, Institute of Medical Science, The University of Tokyo 4-6-1 Shiroganedai, Minato-ku Tokyo 108 aut NATIONALLICENCE 700 1- Muraki Takamura Department of Pharmacology, Tokyo Women's Medical College 8-1 Kawada-cho, Shinjuku-ku Tokyo 162 aut NATIONALLICENCE 700 1- Sakaki Yoshiyuki Human Genome Center, Institute of Medical Science, The University of Tokyo 4-6-1 Shiroganedai, Minato-ku Tokyo 108 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/4(1996-10), 820-827 0021-924X 120:4<820 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford