Primary structure of human, chicken, and Xenopus laevis p11, a cellular ligand of the Src-kinase substrate, annexin II.
The p11 protein is a member of the S-100 family of Ca(2+)-binding proteins and serves within the cell as a ligand of the tyrosine kinase substrate, annexin II. To obtain more structural information on this molecule, we have isolated and characterized p11 cDNA clones from several different species. A comparison of the deduced amino acid (aa) sequences reveals that mammalian and avian p11 are highly similar (at least 90% identical at the aa level), whereas p11 from Xenopus laevis shows a considerable degree of sequence variation (the aa sequence identity drops to approx. 60% when compared to mammalian or chicken p11). Interestingly, the C-terminal 18 aa, which are unique to p11 within the S-100 family, show a relatively high conservation among species. This high evolutionary conservation is in line with a structurally and/or functionally important role of this C terminus, e.g., in annexin II binding.
Kube
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Department of Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, F.R.G.
Weber
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Gerke
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D000595:Amino Acid Sequence; D000818:Animals; D017306:Annexin A2; D017302:Annexins; D001483:Base Sequence; D015152:Blotting, Northern; D002135:Calcium-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D002645:Chickens; D004247:DNA; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics* / Q000378:metabolism; D009418:S100 Proteins; D016415:Sequence Alignment; D014982:Xenopus laevis; D000099248:S100 Calcium Binding Protein A10
D017306:Annexin A2; D017302:Annexins; D002135:Calcium-Binding Proteins; D004247:DNA; D008024:Ligands; D010455:Peptides; D009418:S100 Proteins; D000099248:S100 Calcium Binding Protein A10