Identification of a Novel Human Ankyrin-Repeated Protein Homologous to CARP

• Published in: Biochemical and biophysical research communications 2001-07, Vol.285 (3), p.715-723
• Main Authors: Moriyama, Masatsugu, Tsukamoto, Yoshiyuki, Fujiwara, Masahiko, Kondo, Gento, Nakada, Chisato, Baba, Takeshi, Ishiguro, Naoko, Miyazaki, Akiko, Nakamura, Kyoko, Hori, Naohiro, Sato, Kenzo, Shomori, Kohei, Takeuchi, Kengo, Satoh, Hitoshi, Mori, Shigeo, Ito, Hisao
• Format: Article
• Language: English
• Subjects: 10q24; Ankyrin Repeat - genetics; ankyrin-repeat; Arpp protein; Base Sequence; C-193; Carcinoma - genetics; cardiac muscle; CARP; Cell Line; Cell Nucleus - metabolism; Chromosomes, Human, Pair 10 - genetics; Cloning, Molecular; Cytoplasm - metabolism; DNA, Complementary - genetics; DNA, Complementary - isolation & purification; esophageal carcinoma; Esophageal Neoplasms - genetics; Gene Library; heart; Heart Ventricles - metabolism; Humans; In Situ Hybridization, Fluorescence; MARP; Molecular Sequence Data; Muscle Proteins; Muscle, Skeletal - metabolism; Myocardium - metabolism; Neoplasm Proteins - genetics; Neoplasm Proteins - metabolism; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Organ Specificity; PEST; Physical Chromosome Mapping; Repressor Proteins - genetics; Repressor Proteins - metabolism; Sequence Homology, Amino Acid; skeletal muscle
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.2001.5216

We cloned a novel ankyrin repeat protein, Arpp, by immunoscreening a cDNA library constructed from a human esophageal carcinoma cell line, TE1, with an antibody directed to a hypothetical protein encoded by antisense p53 mRNA. Arpp protein is composed of 333 amino acids and contains four ankyrin-like repeat motifs in the middle portion of the protein, a PEST-like sequence and a lysine-rich sequence similar to a nuclear localization signal in the N-terminal region, and a proline-rich region containing consensus phosphorylation sites in the C-terminal region. Protein sequence analysis revealed that Arpp is homologous (52.7% identity) to Carp which is shown to be involved in the regulation of the transcription of the cardiac ventricular myosin light chain 2 gene. Arpp mRNA was found to be expressed in normal skeletal and cardiac muscle. Interestingly, Arpp expression was detectable in bilateral ventricles, but undetectable in bilateral atria and large vessels, suggesting that Arpp may play a specific function in cardiac ventricles as well as skeletal muscles.