1. cDNA cloning, genomic structure, chromosomal mapping, and expression analysis of parotid secretory protein in pig
- Author
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Ning Li, Zhao Liang Liu, Wei Lu, Bao Liang Fan, HaiFang Yin, Zhi Hui Zhao, and Yu Fang Liu
- Subjects
Models, Molecular ,Leucine zipper ,DNA, Complementary ,Sequence analysis ,Molecular Sequence Data ,Sus scrofa ,Dot blot ,Sequence alignment ,Biology ,Synteny ,Protein Structure, Secondary ,Rapid amplification of cDNA ends ,Complementary DNA ,Genetics ,Consensus sequence ,Animals ,Humans ,Parotid Gland ,Amino Acid Sequence ,Cloning, Molecular ,Salivary Proteins and Peptides ,Peptide sequence ,Base Sequence ,Sequence Homology, Amino Acid ,Gene Expression Profiling ,Chromosome Mapping ,DNA ,Exons ,Sequence Analysis, DNA ,Chromosomes, Mammalian ,Molecular biology ,Introns ,Genes ,Sequence Alignment - Abstract
A novel cDNA has been isolated from pig parotid glands by 3' and 5' rapid amplification of cDNA ends and designated parotid secretory protein (PSP). The open reading frame of this cDNA covers 714 bases, encoding 238 amino acids, which show 56% identity with human PSP at the level of the primary protein structure. The PSP genomic sequence comprises eight exons and seven introns, is approximately 22 kb in size, determined by sequencing, and maps to pig chromosome 17q21-q23. RT-PCR, dot blot, and Northern blot analyses demonstrated that PSP is strongly expressed in parotid glands, but is not present in heart, liver, lung, kidney, muscle, or stomach. A search for functionally significant protein motifs revealed consensus sequences for casein kinase II phosphorylation and N-myristoylation. We observed a unique amino acid sequence pattern consisting of the residues Leu-X(6)-Leu-X(6)-Leu-X(7)-Leu-X(6)-Leu-X(6)-Leu near the amino-terminal portion of the protein, which is similar to the leucine zipper.
- Published
- 2004
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