Protein spanning

http://www.chembio.uoguelph.ca/educmat/phy456/456lec03.htm

It states: Polytopic membrane proteins appear to be derived by a modification of this basic mechanism. Instead of the signal appearing as a single leader, multiple signal sequences occur internally in the polypeptide, alternating with stop transfer sequences. Unlike the N-terminal signal, the internal signal/anchor sequences are not cleaved by the signal peptidase that acts on N-terminal-signals. Internal signals are characterized by occurrence of charged amino acids at the helix boundary. The charges govern the orientation such that the end retained in the cytoplasm is positively charged, while the translocated end may be negative. Some bitopic membrane proteins lack N-terminal signal sequences, and may be inserted by the action of an internal signal/anchor sequence. This can account for bitopic transmembrane proteins with the wrong orientation, i.e. N-terminal on the cytoplasmic side.

So, I could either be 1 or 2... I'm gearing more towards 1.