Biomaterial Database

Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins. 1978

J R Dedman, and R L Jackson, and W E Schreiber, and A R Means

A Ca2+-dependent regulator protein of cyclic 3':5'-nucleotide phosphodiesterase (EC 3.1.4.17) has previously been isolated from rat testis and shown to be a heat-stable, Ca2+-binding protein with a molecular weight of approximately 17,000. The Ca2+-dependent regulator protein is also structurally similar to troponin-C, the Ca2+-binding component of muscle troponin and Ca2+ mediator of muscle contraction. The present report describes a partial amino acid sequence of the Ca2+-dependent regulator. The protein (148 amino acids) is 50% homologous with skeletal muscle troponin-C, but is 11 residues shorter than the muscle protein. The Ca2+-dependent regulator protein has an NH2-terminal sequence of acetyl-Ala-Asp-Glu, a COOH-terminal sequence of Thr-Ala-Lys and 1 residue of epsilon-trimethyllysine located at position 115. All of these properties are distinct from those of other homologous Ca2+-binding proteins. These properties may account for the biological specificities demonstrated by these proteins as compared to the Ca2+-dependent regulator protein. Based on the sequence and a comparison of the Ca2+-dependent regulator protein to other calcium-binding proteins, our data support the view that all of these moecules contain common sequences, especially at their proposed metal-binding sites.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D002118	Calcium	A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.	Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
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
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013737	Testis	The male gonad containing two functional parts: the SEMINIFEROUS TUBULES for the production and transport of male germ cells (SPERMATOGENESIS) and the interstitial compartment containing LEYDIG CELLS that produce ANDROGENS.	Testicles,Testes,Testicle
D014336	Troponin	One of the minor protein components of skeletal and cardiac muscles. It functions as the calcium-binding component in a complex with BETA-TROPOMYOSIN; ACTIN; and MYOSIN and confers calcium sensitivity to the cross-linked actin and myosin filaments. Troponin itself is a complex of three regulatory proteins (TROPONIN C; TROPONIN I; and TROPONIN T).	Troponin Complex,Troponins
D015105	3',5'-Cyclic-AMP Phosphodiesterases	Enzymes that catalyze the hydrolysis of CYCLIC AMP to form adenosine 5'-phosphate. The enzymes are widely distributed in animal tissue and control the level of intracellular cyclic AMP. Many specific enzymes classified under this heading demonstrate additional spcificity for 3',5'-cyclic IMP and CYCLIC GMP.	3',5'-Cyclic AMP 5'-Nucleotidohydrolase,3',5'-Cyclic-Nucleotide Phosphodiesterase,CAMP Phosphodiesterase,3',5' Cyclic AMP Phosphodiesterase,3',5'-Cyclic AMP Phosphodiesterase,3',5'-Cyclic Nucleotide Phosphodiesterase,3',5'-Cyclic-AMP Phosphodiesterase,3',5'-Nucleotide Phosphodiesterase,3,5-Cyclic AMP 5-Nucleotidohydrolase,3,5-Cyclic AMP Phosphodiesterase,3',5' Cyclic AMP 5' Nucleotidohydrolase,3',5' Cyclic AMP Phosphodiesterases,3',5' Cyclic Nucleotide Phosphodiesterase,3',5' Nucleotide Phosphodiesterase,3,5 Cyclic AMP 5 Nucleotidohydrolase,3,5 Cyclic AMP Phosphodiesterase,5'-Nucleotidohydrolase, 3',5'-Cyclic AMP,5-Nucleotidohydrolase, 3,5-Cyclic AMP,AMP 5'-Nucleotidohydrolase, 3',5'-Cyclic,AMP 5-Nucleotidohydrolase, 3,5-Cyclic,AMP Phosphodiesterase, 3',5'-Cyclic,AMP Phosphodiesterase, 3,5-Cyclic,Nucleotide Phosphodiesterase, 3',5'-Cyclic,Phosphodiesterase, 3',5'-Cyclic AMP,Phosphodiesterase, 3',5'-Cyclic Nucleotide,Phosphodiesterase, 3',5'-Cyclic-AMP,Phosphodiesterase, 3',5'-Cyclic-Nucleotide,Phosphodiesterase, 3',5'-Nucleotide,Phosphodiesterase, 3,5-Cyclic AMP,Phosphodiesterase, CAMP,Phosphodiesterases, 3',5'-Cyclic-AMP