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The extramembraneous segments in a large collection of G-protein coupled receptors (GPCRs) have been analysed in terms of amino acid composition and length. It is shown that this family of multi-spanning integral membrane proteins conforms well to the 'positive inside' rule. Further, the extracellular N-terminal tails of GPCRs lacking a cleavable signal peptide are shown to be considerably shorter and to have a reduced content of positively charged amnio acids compared with the N-terminal tails of GPCRs endowed with a signal peptide. This suggests that extracellular N-terminal tails of eukaryotic plasma membrane proteins may be translocated by different mechanisms depending on whether or not they are preceded by a signal peptide.
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Wallin et al. (1995) studied this question.
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