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. 2004 Apr 12;101(16):5922–5927. doi: 10.1073/pnas.0401600101

Fig. 3.

Fig. 3.

A second hydrophobic patch within the ZP domain is also involved in secretion and assembly of ZP3. (A) Comparison of EHP and IHP sequences of ZP1–3 and (B) schematic representation of their position within a minimal ZP domain protein. Amino acid numbers and sequences refer to human and mouse ZP proteins; secondary structure predictions and consensus sequences for individual ZP protein subfamilies (ZP1–3) were obtained as in Fig. 1B. The IHP is depicted as a yellow rectangle, with all other elements as in Fig. 1, except for the CP, which was omitted. Amino acid F171 within the IHP of ZP3 is indicated by a red dot. (C) IHP mutation F171S does not affect secretion of full-length ZP3 (ZP3-FLAG-F171S; lanes 1 and 2) but abolishes secretion of protein constructs lacking a TMD (ZP3-FLAG-370-F171S; lanes 3 and 4). (D and E) The IHP mutant ZP3-FLAG-F171S is packaged into secretory vesicles by microinjected oocytes (E) but is not assembled into the ZP (D). Red crosses mark mutated IHPs.