Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes. 1988

E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
Department of Oral Biochemistry, School of Dentistry at Niigata, Nippon Dental University.

Human saliva contains at least three molecular species of cystatin S-type cysteine proteinase inhibitor (cystatin S, cystatin SN and cystatin SA), which have similar but distinct amino-acid sequences. The nucleotide sequences of the CST 1 gene for cystatin SN and the CST 2 gene for cystatin SA are highly homologous to each other and to the corresponding regions of the cDNA for cystatin C and the EcoRI-PstI fragment from the cystatin C gene. Three cystatin-like domains in the kininogen gene and the salivary cystatin genes share the same gene organizations. These data demonstrate that family II cystatin genes are evolutionarily related to family III cystatin genes.

UI MeSH Term Description Entries
D007525 Isoelectric Focusing Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point. Electrofocusing,Focusing, Isoelectric
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D005075 Biological Evolution The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics. Evolution, Biological
D005810 Multigene Family A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed) Gene Clusters,Genes, Reiterated,Cluster, Gene,Clusters, Gene,Families, Multigene,Family, Multigene,Gene Cluster,Gene, Reiterated,Multigene Families,Reiterated Gene,Reiterated Genes
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D012463 Saliva The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin. Salivas
D012471 Salivary Proteins and Peptides Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals. Salivary Gland Protein,Salivary Gland Proteins,Salivary Peptide,Salivary Protein,Salivary Proteins,Salivary Peptides,Gland Protein, Salivary,Peptide, Salivary,Protein, Salivary,Protein, Salivary Gland
D015853 Cysteine Proteinase Inhibitors Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES. Acid Cysteine Proteinase Inhibitor,Cysteine Protease Inhibitor,Cysteine Protease Inhibitors,Cysteine Proteinase Antagonist,Cysteine Proteinase Antagonists,Cysteine Proteinase Inhibitor,Cysteine Proteinase Inhibitors, Endogenous,Cysteine Proteinase Inhibitors, Exogenous,alpha-Cysteine Protease Inhibitor,Acid Cysteine Proteinase Inhibitors,alpha-Cysteine Protease Inhibitors,Antagonist, Cysteine Proteinase,Antagonists, Cysteine Proteinase,Inhibitor, Cysteine Protease,Inhibitor, Cysteine Proteinase,Inhibitor, alpha-Cysteine Protease,Inhibitors, Cysteine Protease,Inhibitors, Cysteine Proteinase,Inhibitors, alpha-Cysteine Protease,Protease Inhibitor, Cysteine,Protease Inhibitor, alpha-Cysteine,Protease Inhibitors, Cysteine,Protease Inhibitors, alpha-Cysteine,Proteinase Antagonist, Cysteine,Proteinase Antagonists, Cysteine,Proteinase Inhibitor, Cysteine,Proteinase Inhibitors, Cysteine,alpha Cysteine Protease Inhibitor,alpha Cysteine Protease Inhibitors

Related Publications

E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
May 1987, FEBS letters,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
June 2009, Cancer genetics and cytogenetics,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
April 1990, Nucleic acids research,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
March 1993, Gene,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
December 2023, Insects,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
November 1998, Protein science : a publication of the Protein Society,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
October 1995, FEMS microbiology letters,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
March 2022, Journal of molecular endocrinology,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
February 2008, Virology journal,
E Saitoh, and S Isemura, and K Sanada, and H S Kim, and O Smithies, and N Maeda
April 1989, Journal of molecular biology,
Copied contents to your clipboard!