
doi: 10.1271/bbb.63.243
pmid: 10052151
We cloned a cDNA encoding the NH2-terminal portion of mouse SREBP-1. The deduced amino acid sequence was 76% and 90% identical to human and hamster SREBP-1, respectively. We found out a novel splicing isoform of mouse SREBP-1 that lacks 42 amino acid residues composing a PEST sequence observed in unstable proteins. It has been reported that SREBP-1 is rapidly turned over in the nucleus. Although this isoform was not a dominant isoform, it might be possible that the produced protein functions differently from other isoforms including a complete PEST sequence.
DNA, Complementary, Base Sequence, Sequence Homology, Amino Acid, Helix-Loop-Helix Motifs, Molecular Sequence Data, Nuclear Proteins, DNA, DNA-Binding Proteins, Alternative Splicing, Mice, Species Specificity, Cricetinae, CCAAT-Enhancer-Binding Proteins, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Sterol Regulatory Element Binding Protein 1, Transcription Factors
DNA, Complementary, Base Sequence, Sequence Homology, Amino Acid, Helix-Loop-Helix Motifs, Molecular Sequence Data, Nuclear Proteins, DNA, DNA-Binding Proteins, Alternative Splicing, Mice, Species Specificity, Cricetinae, CCAAT-Enhancer-Binding Proteins, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Sterol Regulatory Element Binding Protein 1, Transcription Factors
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