Biomaterial Database

Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase. 1989

K Watanabe, and T Senshu

Department of Biochemistry, Tokyo Metropolitan Institute of Gerontology, Japan.

Various mammalian tissues contain protein-arginine deiminases (EC 3.5.3.15), which convert the arginine residues in normal peptide bonds to the citrulline residues in calcium ion-dependent manners. Here, we describe the complete primary structure of rat skeletal muscle peptidylarginine deiminase deduced from the sequences of its cDNA clones isolated by recombinant DNA technology. We have isolated three overlapping cDNA clones which constitute a 4,507-base pair cDNA sequence including a 2,452-base pair 3'-untranslated region. The coding region consists of 1,995 base pairs encoding 665 amino acid residues. A potential N-linked glycosylation site is present at asparagine-534. The molecular weight of the enzyme calculated from the deduced amino acid sequence is 75,122. Direct repeat sequences resembling the rodent B2 type repetitive sequences appear in the 3'-untranslated region (nucleotides 3,090-3,198 and 3,270-3,391). Northern hybridization demonstrated the presence of its mRNA in poly(A)+ fractions of spinal cord, cerebrum, cerebellum, and submaxillary gland as well as skeletal muscle. The sizes of peptidylarginine deiminase mRNAs in these tissues were estimated to be 4.5-5.0 kilobases. No positive bands were detected on the blots of the corresponding RNA fractions of liver and kidney. Possible similarity of the amino acid sequence of peptidylarginine deiminase to those of other calcium binding proteins is discussed.

UI	MeSH Term	Description	Entries
D007256	Information Systems	Integrated set of files, procedures, and equipment for the storage, manipulation, and retrieval of information.	Ancillary Information Systems,Emergency Care Information Systems,Information Retrieval Systems,Perinatal Information System,Ancillary Information System,Information Retrieval System,Information System,Information System, Ancillary,Information System, Perinatal,Perinatal Information Systems,Systems, Information Retrieval
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
D009132	Muscles	Contractile tissue that produces movement in animals.	Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D003001	Cloning, Molecular	The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.	Molecular Cloning
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
D005796	Genes	A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.	Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
D006867	Hydrolases	Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.	Hydrolase
D000076342	Protein-Arginine Deiminases	A family of ENZYMES that, in the presence of calcium ion, converts ARGININE to CITRULLINE in proteins. There are five PAD isotypes in mammals. In humans: they include PAD1, 2, 3, 4 and 6. They are encoded by five paralogous genes named PADI and clustered on human chromosome 1.	Peptidylarginine Deiminase,Peptidylarginine Deiminases,Protein-Arginine Deiminase,Protein-L-Arginine Iminohydrolase,Protein-L-Arginine Iminohydrolases,Deiminase, Peptidylarginine,Deiminase, Protein-Arginine,Deiminases, Peptidylarginine,Deiminases, Protein-Arginine,Iminohydrolase, Protein-L-Arginine,Iminohydrolases, Protein-L-Arginine,Protein Arginine Deiminase,Protein Arginine Deiminases,Protein L Arginine Iminohydrolase,Protein L Arginine Iminohydrolases
D000080002	Protein-Arginine Deiminase Type 4	A histone modification enzyme, which converts both ARGININE and monomethyl-arginine to CITRULLINE. It is one of several protein-arginine deiminase isoenzymes. It is a gene regulator involved in APOPTOSIS and CELL DIFFERENTIATION and a potential therapeutic target for the treatment of a variety of diseases.	PAD V Enzyme,PADI4 Protein,PADI5 Protein,Peptidyl Arginine Deiminase Type 4,Peptidyl Arginine Deiminase Type IV,Peptidylarginine Deiminase IV,Peptidylarginine Deiminase Type 4,Peptidylarginine Deiminase Type IV,Peptidylarginine Deiminase V,Protein Arginine Deiminase 4,Protein Arginine Deiminase Type 4,Protein Arginine Deiminase Type IV,Protein-Arginine Deiminase Type IV
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