The evolution fo rhodopsins and neurotransmitter receptors

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Abstract
Rhodopsins share a limited number of amino acid identities with a variety of other integral membrane proteins. Most of these proteins have seven putative transmembrane segments and are likely to play a role in transmembrane signaling. We have undertaken a systematic series of comparisons of primary and secondary structure in order to clarify the functional and evolutionary significance of these sequence similarities. On the basis of consistently high similarity scores, we find that the most internally consistent definition of the rhodopsis gene family would ionclude vertebrate rhodospins, α- and β-adrenergic receptors, M1 and M2 muscarinic acetylcholine receptors, substance K receptors and insect rhodopsins, while excluding bacterirhodopsin, themas human oncogene, vertebrate and insect nicotinic acetylcholine receptors, and the yeast STE2 and STE3 peptide receptors. The rhodopsin gene family is highly diverged at the primary sequence level but has maintained a conserved secondary structure, including a previosuly unidentified hierarchy of transmembrane segment hydrophobicity. We have deevelope new computer alogithms for progressive multiple sequence alignment and the analysis of local conservation of protein domains, and we have used these algorithms to examined the phylogeny of the rhodopsin gene family and the changing domains of sequence conservation. The results show striking diffiierences and similarities in the conserved domains in each of the three main branches of the rhodopsin gene family, and indicte that color vision arose independently in the lines of descent leading to modern humans and fruit flies.