Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
A putative blue-light receptor from Drosophila melanogaster.
An extraretinally expressed insect cryptochrome with similarity to the blue light photoreceptors of mammals and plants.
Light-dependent sequestration of TIMELESS by CRYPTOCHROME.
Drosophila CRY is a deep brain circadian photoreceptor.
A new role for cryptochrome in a Drosophila circadian oscillator.
Light-dependent interaction between Drosophila CRY and the clock protein PER mediated by the carboxy terminus of CRY.
Identification of genes involved in Drosophila melanogaster geotaxis, a complex behavioral trait.
The extraretinal eyelet of Drosophila: development, ultrastructure, and putative circadian function.
Novel features of cryptochrome-mediated photoreception in the brain circadian clock of Drosophila.
A constitutively active cryptochrome in Drosophila melanogaster.
Serotonin modulates circadian entrainment in Drosophila.
Disruption of Cryptochrome partially restores circadian rhythmicity to the arrhythmic period mutant of Drosophila.
Functional analysis of circadian pacemaker neurons in Drosophila melanogaster.
Drosophila CRYPTOCHROME is a circadian transcriptional repressor.
JETLAG resets the Drosophila circadian clock by promoting light-induced degradation of TIMELESS.
Veela defines a molecular link between Cryptochrome and Timeless in the light-input pathway to Drosophila's circadian clock.
A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome.
The Drosophila circadian network is a seasonal timer.
Light activates output from evening neurons and inhibits output from morning neurons in the Drosophila circadian clock.
Animal type 1 cryptochromes. Analysis of the redox state of the flavin cofactor by site-directed mutagenesis.
Cryptochrome is present in the compound eyes and a subset of Drosophila's clock neurons.
Human and Drosophila cryptochromes are light activated by flavin photoreduction in living cells.
The blue-light photoreceptor CRYPTOCHROME is expressed in a subset of circadian oscillator neurons in the Drosophila CNS.
Cryptochrome mediates light-dependent magnetosensitivity in Drosophila.
Cryptochrome mediates light-dependent magnetosensitivity of Drosophila's circadian clock.
Animal cryptochromes mediate magnetoreception by an unconventional photochemical mechanism.
Reaction mechanism of Drosophila cryptochrome.
Structure of full-length Drosophila cryptochrome.
Cryptochrome-positive and -negative clock neurons in Drosophila entrain differentially to light and temperature.
Rhodopsin 5- and Rhodopsin 6-mediated clock synchronization in Drosophila melanogaster is independent of retinal phospholipase C-β signaling.
Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function.
Flavin reduction activates Drosophila cryptochrome.
Effects of light interruption on sleep and viability of Drosophila melanogaster.
A rhodopsin in the brain functions in circadian photoentrainment in Drosophila.
A New Rhodopsin Influences Light-dependent Daily Activity Patterns of Fruit Flies.
Cryptochrome-Timeless structure reveals circadian clock timing mechanisms.
CRY, a Drosophila clock and light-regulated cryptochrome, is a major contributor to circadian rhythm resetting and photosensitivity.
The cryb mutation identifies cryptochrome as a circadian photoreceptor in Drosophila.
CRY is activated by light and binds to phosphorylated nuclear TIM
Nuclear JET binds CRY, facilitating its ubiquitination
JET binds cytosolic TIM, facilitating its ubiquitination
JET binds phosphorylated nuclear TIM, facilitating its ubiquitination
CRY is activated by light and binds to cytosolic TIM
Cytosolic CRY is degraded by the 26S proteasome
Cytosolic JET binds to CRY, facilitating its ubiquitination
Nuclear CRY is degraded by the 26S proteasome
CRY is phosphorylated by SGG
Deep research on Drosophila cry via Cyberian
Falcon deep research report on Drosophila melanogaster cry (CRY, O77059)
-
DmCRY (UniProt O77059, CG3772) is a Drosophila-type/type I cryptochrome in the DNA
photolyase/cryptochrome family that binds FAD and functions primarily as a blue-light
photoreceptor for circadian clock entrainment.
"The UniProt accession **O77059** corresponds to **Drosophila melanogaster Cryptochrome-1 (DmCRY; gene symbol cry; ORF CG3772)**, a **Drosophila-type/type I cryptochrome** within the **DNA photolyase/cryptochrome family** that **binds FAD** and functions primarily as a **blue-light photoreceptor** for circadian clock entrainment."
-
In the canonical pathway, light-activated CRY binds TIMELESS (TIM) and triggers TIM
degradation via recruitment of the E3 ubiquitin ligase Jetlag (JET), resetting the
circadian oscillator.
"In the canonical pathway, light-activated CRY **binds Timeless (TIM)** and triggers **TIM degradation** via recruitment of the **E3 ubiquitin ligase Jetlag (JET)**, thereby resetting the circadian oscillator."
-
The Drosophila CRY light-sensing role is mechanistically distinct from mammalian-type
(type II) cryptochromes, which are light-independent transcriptional repressors in the
core clock feedback loop.
"This Drosophila light-sensing role is mechanistically distinct from **vertebrate/mammalian-type (type II) cryptochromes**, which are described primarily as **light-independent transcriptional repressors** in the core clock feedback loop."
-
Cryptochromes are structurally related to DNA photolyases but generally lack DNA repair
activity and instead serve as sensory/signaling proteins; DmCRY is a cell-autonomous
circadian photoreceptor.
"Cryptochromes are structurally related to UV/blue-sensitive **DNA photolyases** but generally lack DNA repair activity and instead serve as **sensory/signaling proteins**."
-
A quantitative binding study supports CTT-gated TIM recognition: WT CRY binds TIM more
strongly in light than dark (KD,dark ~32 uM vs KD,light ~9 uM), while CTT deletion gives
constitutive high-affinity binding (KD ~1.7 uM).
"WT CRY binds TIM more strongly in light than dark (**KD,dark ≈ 32 µM** vs **KD,light ≈ 9 µM**), while CTT deletion yields **constitutive high-affinity binding** (**KD ≈ 1.7 µM**)."
-
A 2023 cryo-EM CRY-TIM structure (3.3 A; PDB 8DD7 / EMDB-27335) shows TIM inserts its
N-terminus into the CRY flavin pocket, replacing the CRY CTT.
"For the peer-reviewed Nature cryo-EM dataset (Apr 2023), the reported reconstruction statistics include **3.3 Å map resolution (2.4–5.5 Å range)** and deposition **PDB 8DD7 / EMDB-27335**, supporting confidence in residue-level interface interpretation."
-
FAD binding is not only photochemical but also a structural requirement for CRY to reach
a signaling-competent native fold.
"These data support a functional-annotation view in which **FAD binding is not only photochemical but also a structural requirement** to reach a signaling-competent native fold."
-
In compound eyes, CRY can act as a structural/assembling factor in rhabdomeres,
interacting with actin; this rhabdomeric pool is not degraded by light, consistent with
a stable scaffolding role.
"In compound eyes, CRY can act as a **structural/assembling factor** in rhabdomeres: it interacts with **actin** and is proposed to maintain the phototransduction “signalplex” near the membrane, enhancing light sensitivity and thereby contributing to eye-mediated clock light input. This rhabdomeric CRY pool is reported as **not degraded by light**, consistent with a stable scaffolding role."
-
Beyond entrainment, Drosophila CRY contributes to non-canonical roles including
arousal/UV avoidance, visual photoreception, and magnetic field detection.
"Drosophila CRY contributes to **arousal/UV avoidance**, **visual photoreception**, and **magnetic field detection**, and can influence circadian amplitude through light-independent mechanisms in a tissue-dependent fashion."
-
Loss of CRY (cry01) alters metabolic physiology, including triglyceride dynamics,
starvation resistance, and lifespan.
"A 2024 peer-reviewed study reports that loss of CRY (cry01) alters metabolic physiology, including triglyceride dynamics, starvation resistance, and lifespan."
PANTHER family PTHR11455 (CRYPTOCHROME) summary
Structure of full-length Drosophila cryptochrome
Cry-Timeless complex (Drosophila) by cryo-EM