Two Membrane-Associated Tyrosine Phosphatase Homologs Potentiate C. elegans AKT-1/PKB Signaling (original) (raw)
Figure 2
Predicted Primary Amino Acid Sequence of EAK-6 and Similarity with PTPs
(A) EAK-6 amino acid sequence. EAK-6 sequence was derived from full-length cDNA amplified by RT-PCR from wild-type C. elegans total RNA. The PTP domain is denoted in boldface. The residue mutated in eak-6(mg329) is boxed and the predicted change indicated above the mutated residue. Amino acids encoded by an alternatively spliced exon present in EAK-6L but not in EAK-6S (see Materials and Methods) are underlined.
(B) EAK-6 homology with PTPs. The PTP domain of EAK-6 is aligned with that of SDF-9 and 3 human PTPs. Sequences used in the alignment are based on domains defined by Pfam [101] and correspond to amino acids 40 to 276 of PTPN1 (PTP1B), 57 to 308 of EAK-6, 31 to 283 of SDF-9, 265 to 500 of PTPRA (receptor-type PTPĪ±), and 273 to 520 of PTPN11 (SHP-2). Alignment was performed using ClustalX 1.8 and MacBoxshade 2.15. Conserved and identical residues are shaded. Ten motifs conserved among 37 vertebrate PTPs [68] are underlined, and 19 residues that are invariant among 113 vertebrate PTP domains are boxed. The four invariant residues that are not identical in EAK-6 (R45, Q85, H214, and G220, numbered according to the PTPN1 primary sequence) are denoted with dots. The catalytic cysteine residue [69] is denoted by an asterisk. Two conserved residues that are not conserved in EAK-6, D181 and Q262, are denoted by arrowheads.