Cryptochrome 4: Difference between revisions

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== Description ==

Cryptochrome 4 is believed to be a crucial protein involved in magentoreception, a function that allows birds to visualize magnetic fields. In most animals where it is present, it is located within both the outer segments of the double cones and long-wavelength cones in the eye <ref name="B"/>. It is evolutionarily related to DNA Photolyase proteins, however is shows no DNA repair activity. It shows a weak circadian oscillation and has strong up regulation during migratory seasons (2.2x upregulated) <ref name="B"/>. It binds FAD at physiological conditions; a necessary function for its photochemical function<ref name="A">DOI 10.1073/pnas.1907875116</ref>. It has “a construct truncated at the C terminus by 28 residues that contains the photolyase homology region (PHR) that demonstrates spectra consistent with bound FAD^ox in the ground state”<ref name="A"/>. There is high efficiency of conversion of FAD^ox to FADH^rad as well as the conversions of FADH^rad to FADH^-, indicating that it is sensitive to low light intensity<ref name="B">DOI 10.1016/j.cub.2017.12.003</ref>.

'''Cryptochrome 4''' is believed to be a crucial protein involved in magentoreception, a function that allows birds to visualize magnetic fields. In most animals where it is present, it is located within both the outer segments of the double cones and long-wavelength cones in the eye <ref name="B"/>. It is evolutionarily related to DNA Photolyase proteins, however is shows no DNA repair activity. It shows a weak circadian oscillation and has strong up regulation during migratory seasons (2.2x upregulated) <ref name="B"/>. It binds FAD at physiological conditions; a necessary function for its photochemical function<ref name="A">DOI 10.1073/pnas.1907875116</ref>. It has “a construct truncated at the C terminus by 28 residues that contains the photolyase homology region (PHR) that demonstrates spectra consistent with bound FAD^ox in the ground state”<ref name="A"/>. There is high efficiency of conversion of FAD^ox to FADH^rad as well as the conversions of FADH^rad to FADH^-, indicating that it is sensitive to low light intensity<ref name="B">DOI 10.1016/j.cub.2017.12.003</ref>.

== Purpose ==

Cryptochrome 4: Difference between revisions

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 == Description ==
-Cryptochrome 4 is believed to be a crucial protein involved in magentoreception, a function that allows birds to visualize magnetic fields. In most animals where it is present, it is located within both the outer segments of the double cones and long-wavelength cones in the eye <ref name="B"/>. It is evolutionarily related to DNA Photolyase proteins, however is shows no DNA repair activity. It shows a weak circadian oscillation and has strong up regulation during migratory seasons (2.2x upregulated) <ref name="B"/>. It binds FAD at physiological conditions; a necessary function for its photochemical function<ref name="A">DOI 10.1073/pnas.1907875116</ref>. It has “a construct truncated at the C terminus by 28 residues that contains the photolyase homology region (PHR) that demonstrates spectra consistent with bound FAD^ox in the ground state”<ref name="A"/>. There is high efficiency of conversion of FAD^ox to FADH^rad as well as the conversions of FADH^rad to FADH^-, indicating that it is sensitive to low light intensity<ref name="B">DOI 10.1016/j.cub.2017.12.003</ref>.
+'''Cryptochrome 4''' is believed to be a crucial protein involved in magentoreception, a function that allows birds to visualize magnetic fields. In most animals where it is present, it is located within both the outer segments of the double cones and long-wavelength cones in the eye <ref name="B"/>. It is evolutionarily related to DNA Photolyase proteins, however is shows no DNA repair activity. It shows a weak circadian oscillation and has strong up regulation during migratory seasons (2.2x upregulated) <ref name="B"/>. It binds FAD at physiological conditions; a necessary function for its photochemical function<ref name="A">DOI 10.1073/pnas.1907875116</ref>. It has “a construct truncated at the C terminus by 28 residues that contains the photolyase homology region (PHR) that demonstrates spectra consistent with bound FAD^ox in the ground state”<ref name="A"/>. There is high efficiency of conversion of FAD^ox to FADH^rad as well as the conversions of FADH^rad to FADH^-, indicating that it is sensitive to low light intensity<ref name="B">DOI 10.1016/j.cub.2017.12.003</ref>.
 == Purpose ==