Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine-specific protein kinases.
Biochemical and partial sequence data reveal the two-domain structure of p36. A loose structure of some 30 residues at the amino-terminus contains the phosphorylatable tyrosine and the binding site for the p11 regulatory chain. The following p33 domain retains the lipid-binding site as well as the Ca2+ site which influences the spectral properties of the single tryptophan and one tyrosine. The combined sequence data covering about 25% of the molecule identify p36 as a unique polypeptide.
D000595:Amino Acid Sequence; D000818:Animals; D017306:Annexin A2; D017302:Annexins; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D050356:Lipid Metabolism; D008565:Membrane Proteins / Q000032:analysis*; D010455:Peptides / Q000378:metabolism*; D010766:Phosphorylation; D012190:Retroviridae / Q000201:enzymology*; D009418:S100 Proteins; D013552:Swine; D014364:Tryptophan / Q000032:analysis; D014443:Tyrosine / Q000378:metabolism; D000099248:S100 Calcium Binding Protein A10
D017306:Annexin A2; D017302:Annexins; D002118:Calcium; D002135:Calcium-Binding Proteins; D008565:Membrane Proteins; D010455:Peptides; D009418:S100 Proteins; D014364:Tryptophan; D014443:Tyrosine; D000099248:S100 Calcium Binding Protein A10; C044504:protein I, intestinal