ArticleThe EMBO journal1987
The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins.
Article in The EMBO journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 136 citations in OpenAlex.
- Annexin A4 self-association modulates general membrane protein mobility in living cells.Molecular biology of the cell · 2006Article
- Activated protein kinase C alpha associates with annexin VI from skeletal muscle.The Biochemical journal · 1998Article
- Ca2+ concentration during binding determines the manner in which annexin V binds to membranes.The Biochemical journal · 1995Article
- Expression and characterization of a Dictyostelium discoideum annexin.Molecular and cellular biochemistry · 1994Article
- Distinct cellular expression pattern of annexins in Hydra vulgaris.The Journal of cell biology · 1992Article
- A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin.The Journal of cell biology · 1992Article
- Purification and partial sequence analysis of plant annexins.The Biochemical journal · 1990Article
- Monoclonal antibodies specific to a Ca2(+)-bound form of lipocortin I distinguish its Ca2(+)-dependent phospholipid-binding ability from its ability to inhibit phospholipase A2.The Biochemical journal · 1990Article
- Synexin (annexin VII): a cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes.The Journal of membrane biology · 1990Review
- Expression of annexins as a function of cellular growth state.The Journal of cell biology · 1990Article
- Identification of the 32 kDa components of bovine lens EDTA-extractable protein as endonexins I and II.The Biochemical journal · 1990Article
- Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins.The Biochemical journal · 1990Article
- A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation.The Biochemical journal · 1989Article
- Calcium channel activity of purified human synexin and structure of the human synexin gene.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix.The EMBO journal · 1988Article
- Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family.The EMBO journal · 1988Article
- A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties.The Biochemical journal · 1988Article
- Primary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein family.The EMBO journal · 1988Article
- Annexin II tetramer: structure and function.Molecular and cellular biochemistryReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein II isolated from porcine intestinal epithelium is a Ca2+-modulated lipid-binding protein. The amino acid sequence of porcine protein II reported here sheds new light on the properties of a multigene protein family which includes the tyrosine kinase substrates of the sarc gene (p36) and of the EGF-receptor (p35). The sequence consolidates the structural principle in which an amino-terminal tailpiece of variable length is followed by a core built from four internally homologous segments for those proteins in the 35-40 kd range. Sequence data also show that the core can now be described as two domains each containing one low and one high homology segment. This view accounts for two Ca2+ sites, lipid aggregation and F-actin bundling--when present--and suggests that properties of the cores in which protein II differs from p36 and p35 arise primarily from segments 1 and 2. The protease-sensitive tailpiece of protein II is very short and lacks the phosphorylatable tyrosine present in the larger tail domains of p36 and p35. It harbors, however, like the p36 domain, the major site for in vitro phosphorylation by the Ca2+- and lipid-activated protein kinase C. In protein II this site is most likely threonine 6. The sequence alignment also explains why protein II does not interact with a unique p11, a property probably specific for p36. Our results further suggest that liver endonexin may reflect two protein species both closely related to protein II.
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