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The deduced amino acid sequence of rat and human rhodopsin kinases have 84% sequence similarity to the earlier reported sequence of the bovine retinal enzyme, with complete conservation of the topological regions containing the position of the catalytic domain and sites of posttranslational modifications. Rat pineal also expresses rod opsin and putative blue cone opsin. Using immunocytochemistry, rod opsin and rhodopsin kinase were found to be co-localized in pinealocytes in the human tissue. These data demonstrate that the mammalian pineal contains light-sensitive opsins and a kinase involved in their inactivation. These findings correlate with an earlier report that neonatal rats show extraretinal light sensitivity, and suggest that a functional photoreceptive system may be present in the adult mammalian pineal.<\/jats:p>","DOI":"10.1017\/s0952523800011366","type":"journal-article","created":{"date-parts":[[2009,6,2]],"date-time":"2009-06-02T11:12:54Z","timestamp":1243941174000},"page":"225-232","update-policy":"https:\/\/doi.org\/10.1017\/policypage","source":"Crossref","is-referenced-by-count":38,"title":["Molecular cloning and localization of rhodopsin kinase in the mammalian pineal"],"prefix":"10.48130","volume":"14","author":[{"given":"Xinyu","family":"Zhao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fran\u00e7oise","family":"Haeseleer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert N.","family":"Fariss","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang","family":"Baehr","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ann H.","family":"Milam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krzysztof","family":"Palczewski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"27968","published-online":{"date-parts":[[2009,6,2]]},"reference":[{"key":"S0952523800011366_ref014","doi-asserted-by":"publisher","DOI":"10.1006\/geno.1996.0399"},{"key":"S0952523800011366_ref036","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.56.2.515"},{"key":"S0952523800011366_ref033","doi-asserted-by":"publisher","DOI":"10.1126\/science.272.5260.419"},{"key":"S0952523800011366_ref031","doi-asserted-by":"publisher","DOI":"10.1016\/0014-4835(92)90090-F"},{"key":"S0952523800011366_ref028","doi-asserted-by":"crossref","first-page":"6004","DOI":"10.1016\/S0021-9258(18)53419-0","article-title":"Identification of the N-terminal region in rhodopsin kinase involved in its interaction with rhodopsin","volume":"268","author":"Palczewski","year":"1993","journal-title":"Journal of Biological Chemistry"},{"key":"S0952523800011366_ref026","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6989(90)90170-P"},{"key":"S0952523800011366_ref024","doi-asserted-by":"publisher","DOI":"10.1038\/372094a0"},{"key":"S0952523800011366_ref023","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.13.5932"},{"key":"S0952523800011366_ref022","doi-asserted-by":"crossref","first-page":"5215","DOI":"10.1074\/jbc.271.9.5215","article-title":"Structural and enzymatic aspects of rhodopsin phosphorylation","volume":"271","author":"Ohguro","year":"1996","journal-title":"Journal of Biological Chemistry"},{"key":"S0952523800011366_ref021","doi-asserted-by":"publisher","DOI":"10.1126\/science.2937147"},{"key":"S0952523800011366_ref032","doi-asserted-by":"publisher","DOI":"10.1006\/exer.1993.1153"},{"key":"S0952523800011366_ref013","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1016\/S0021-9258(18)45960-1","article-title":"Isoprenylation of a protein kinase. 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