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. 1999 Mar;154(3):813–822. doi: 10.1016/S0002-9440(10)65328-X

Figure 6.

Figure 6.

Amino acid sequence alignment of rat podocalyxin (derived from clone 51A) and the previously published podocalyxin-like proteins of rabbit, human, and chicken (gallus). Note the identical or highly homologous structure of the putative transmembrane (double underlining) and intracellular domains of all species. The intracellular domain of rat podocalyxin shows one protein kinase C(*) and two casein kinase II (○) consensus phosphorylation sites, and its partially cloned extracellular domain extends to include two of the four conserved cysteins (arrows). The extracellular seven-amino-acid sequence (aa 50 to 56, line above) was found independently by amino acid sequencing of tryptic peptides of isolated rat glomerular podocalyxin. The probes used for Northern blotting or in situ hybridization covered the whole area shown. Numbering is according to the sequences in GenBank. Accession numbers are U35239 rabbit PCPL-1, U97519 human PCLP, Y13978 Gallus gallus thrombomucin.