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. 2008 Jun 17;84(3):842–851. doi: 10.1189/jlb.0208087

Fig. 1.

Fig. 1.

Comparison of GAPT with LAT family adaptor proteins. (A) Comparison of conserved tyrosine residues between GAPT and other LAT family members. Similar to LAT, GAPT has a short, extracellular domain, a transmembrane (TM) domain, and multiple cytoplasmic tyrosine residues. Among these tyrosine residues, four of them are within a Grb2-binding motif (YxN; gray). (B) Sequence alignment of hGAPT and mGAPT, which share 58% homology of amino acid sequences. The conserved transmembrane domain is labeled, and potential palmitoylation sites are boxed. Potential Grb2-binding motifs are underlined. Arrows show the conserved prolines. The molecular weights of hGAPT and mGAPT are estimated to be 17.8 and 17.6 kDa, respectively.