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Abstract

Pineal opsin (P-opsin), an opsin from chick that is highly expressed in pineal but is not detectable in retina, was cloned by the polymerase chain reaction. It is likely that the P-opsin lineage diverged from the retinal opsins early in opsin evolution. The amino acid sequence of P-opsin is 42 to 46 percent identical to that of the retinal opsins. P-opsin is a seven-membrane spanning, G protein-linked receptor with a Schiff-base lysine in the seventh membrane span and a Schiff-base counterion in the third membrane span. The primary sequence of P-opsin suggests that it will be maximally sensitive to ∼500-nanometer light and produce a slow and prolonged phototransduction response consistent with the nonvisual function of pineal photoreception.

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Science
Volume 267 | Issue 5203
10 March 1995

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Published in print: 10 March 1995

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Marianna Max
Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.
National Science Foundation Center for Biological Timing, Department of Neurobiology and Physiology, Northwestem University, Evanston, IL 60208, USA.
Peter J. McKinnon
Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.
Kenneth J. Seidenman
National Science Foundation Center for Biological Timing, Department of Neurobiology and Physiology, Northwestem University, Evanston, IL 60208, USA.
R. Keith Barrett
National Science Foundation Center for Biological Timing, Department of Neurobiology and Physiology, Northwestem University, Evanston, IL 60208, USA.
Meredithe L. Applebury
Harvard Medical School, Howe Laboratories, Boston, MA 02114, USA.
Joseph S. Takahashi
National Science Foundation Center for Biological Timing, Department of Neurobiology and Physiology, Northwestem University, Evanston, IL 60208, USA.
Robert F. Margolskee
Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.

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