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. 2004 Jan;78(2):595–602. doi: 10.1128/JVI.78.2.595-602.2004

FIG. 5.

FIG. 5.

Amino acid sequence comparison of putative ECD1 and TM2 of PiT1 and PiT2. (A) Replacement of PiT1 ECD1 with that of PiT2 renders PiT1 functional as an A-MuLV receptor. The amino acid sequence identity between ECD1 of PiT1 and PiT2 is approximately 70% and includes conservation of the N-linked glycosylation site (*). (B) Alignment of PiT1 and PiT2 TM2 reveals approximately 89% residue identity between the two domains. The bold text represents the difference between PiT1 (valine) and PiT2 (threonine) at PiT1 position 72, which is thought to play a role in determining receptor topology. Numbers indicate where the respective domains begin and end.