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Mapping of functional domains in the plasma membrane Ca2+ pump using trypsin proteolysis. 1990

E Zvaritch, and P James, and T Vorherr, and R Falchetto, and N Modyanov, and E Carafoli
Laboratory for Biohemistry, Swiss Federal Institute of Technology (ETH), Zurich.

The purified erythrocyte Ca2+ pump has been exposed to trypsin under conditions designed to enrich the fragments of molecular mass 90, 85, 81, and 76 kDa, respectively. In SDS-polyacrylamide gels, these fragments are accompanied by a product of molecular mass about 33 kDa. N- and C-terminal sequencing of the fragments blotted on PVDF membranes has located the four high molecular mass fragments and the 33-kDa fragment within the pump structure. The work has extended previous work on the organization of the calmodulin-interacting domain of the pump (Zurini et al., 1984; Benaim et al., 1984) and has tentatively placed the domain of the pump which interacts with acidic phospholipids between transmembrane helices 2 and 3.

UI MeSH Term Description Entries
D008563 Membrane Lipids Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation. Cell Membrane Lipid,Cell Membrane Lipids,Membrane Lipid,Lipid, Cell Membrane,Lipid, Membrane,Lipids, Cell Membrane,Lipids, Membrane,Membrane Lipid, Cell,Membrane Lipids, Cell
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
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
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010743 Phospholipids Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system. Phosphatides,Phospholipid
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002147 Calmodulin A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels. Calcium-Dependent Activator Protein,Calcium-Dependent Regulator,Bovine Activator Protein,Cyclic AMP-Phosphodiesterase Activator,Phosphodiesterase Activating Factor,Phosphodiesterase Activator Protein,Phosphodiesterase Protein Activator,Regulator, Calcium-Dependent,AMP-Phosphodiesterase Activator, Cyclic,Activating Factor, Phosphodiesterase,Activator Protein, Bovine,Activator Protein, Calcium-Dependent,Activator Protein, Phosphodiesterase,Activator, Cyclic AMP-Phosphodiesterase,Activator, Phosphodiesterase Protein,Calcium Dependent Activator Protein,Calcium Dependent Regulator,Cyclic AMP Phosphodiesterase Activator,Factor, Phosphodiesterase Activating,Protein Activator, Phosphodiesterase,Protein, Bovine Activator,Protein, Calcium-Dependent Activator,Protein, Phosphodiesterase Activator,Regulator, Calcium Dependent
D004910 Erythrocyte Membrane The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS. Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D006180 Proton-Translocating ATPases Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane. ATP Dependent Proton Translocase,ATPase, F0,ATPase, F1,Adenosinetriphosphatase F1,F(1)F(0)-ATPase,F1 ATPase,H(+)-Transporting ATP Synthase,H(+)-Transporting ATPase,H(+)ATPase Complex,Proton-Translocating ATPase,Proton-Translocating ATPase Complex,Proton-Translocating ATPase Complexes,ATPase, F(1)F(0),ATPase, F0F1,ATPase, H(+),Adenosine Triphosphatase Complex,F(0)F(1)-ATP Synthase,F-0-ATPase,F-1-ATPase,F0F1 ATPase,F1-ATPase,F1F0 ATPase Complex,H(+)-ATPase,H(+)-Transporting ATP Synthase, Acyl-Phosphate-Linked,H+ ATPase,H+ Transporting ATP Synthase,H+-Translocating ATPase,Proton-Translocating ATPase, F0 Sector,Proton-Translocating ATPase, F1 Sector,ATPase Complex, Proton-Translocating,ATPase Complexes, Proton-Translocating,ATPase, H+,ATPase, H+-Translocating,ATPase, Proton-Translocating,Complex, Adenosine Triphosphatase,Complexes, Proton-Translocating ATPase,F 0 ATPase,F 1 ATPase,F0 ATPase,H+ Translocating ATPase,Proton Translocating ATPase,Proton Translocating ATPase Complex,Proton Translocating ATPase Complexes,Proton Translocating ATPase, F0 Sector,Proton Translocating ATPase, F1 Sector,Triphosphatase Complex, Adenosine
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

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