O77059 · CRY1_DROME
- ProteinCryptochrome-1
- Genecry
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids542 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Blue light-dependent regulator that is the input of the circadian feedback loop (PubMed:10063806, PubMed:10233998, PubMed:10417378, PubMed:16527739, PubMed:17298948, PubMed:18597555, PubMed:36994075, PubMed:9845369).
Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts (PubMed:10063806).
Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms (PubMed:10063806, PubMed:10233998, PubMed:9845369).
Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells (PubMed:10417378, PubMed:16527739, PubMed:36994075, PubMed:9845370).
Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry (PubMed:10417378, PubMed:16527739).
Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate (PubMed:18641630).
Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing (PubMed:18641630).
Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts (PubMed:10063806).
Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms (PubMed:10063806, PubMed:10233998, PubMed:9845369).
Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells (PubMed:10417378, PubMed:16527739, PubMed:36994075, PubMed:9845370).
Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry (PubMed:10417378, PubMed:16527739).
Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate (PubMed:18641630).
Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing (PubMed:18641630).
Miscellaneous
Unstable upon light exposure. Light induces the degradation of cry, likely due to conformational change in the photoreceptor leading to targeting to the proteasome.
Appears to bind 5,10-methenyltetrahydrofolate at substoichiometric levels.
Cofactor
Note: Binds 1 FAD per subunit. The bound form of FAD in the inactive state of cry is oxidized FAD, not reduced. After activation by blue light the FAD is in an anionic radical state, which would be paramagnetic. Green light, which reduces levels of radical intermediate, has an antagonistic effect on function.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 237 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 265 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 267 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 311 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 378 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 410-412 | FAD (UniProtKB | ChEBI) | ||||
Sequence: DAD | ||||||
Binding site | 416 | FAD (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 419 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCryptochrome-1
- Short namesDmCRY1 ; dcry
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionO77059
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear translocation initiates after the perception of a light signal. Accumulates in the perinuclear region about one hour before translocation into the nucleus. Translocation occurs through interaction with other Clock proteins such as tim and per.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Flies exhibit poor synchronization to light-dark cycles and show no response to brief light pulses. Mutant abolishes rhythmic tim and per expression in photoreceptor and glial cells, but not within certain pacemaker neurons of adult brain.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 337 | Accelerates formation and decay of the FAD radical. | ||||
Sequence: C → A | ||||||
Mutagenesis | 397 | Abolishes formation of the FAD radical. | ||||
Sequence: W → F | ||||||
Mutagenesis | 410 | In cryb: Loss of accumulation. In photoreceptors, leads to an equivalent distribution of per in the nuclei in both day and night ultimately resulting in a slight decrease in Bdbt foci development. | ||||
Sequence: D → N | ||||||
Mutagenesis | 416 | Accelerates decay of the FAD radical. | ||||
Sequence: C → A | ||||||
Mutagenesis | 420 | Abolishes formation of the FAD radical. | ||||
Sequence: W → A | ||||||
Mutagenesis | 523 | Accelerates formation and decay of the FAD radical. | ||||
Sequence: C → A | ||||||
Mutagenesis | 526 | Slows down the decay of the FAD radical. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000348597 | 1-542 | Cryptochrome-1 | |||
Sequence: MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV |
Proteomic databases
Expression
Tissue specificity
Expressed at higher levels in the head than in body and it is more expressed in antennae than in legs, wings and mouth appendages. Prominent expression is seen in cells of the lateral brain, which are close to or coincident with the clock neurons. Abundance oscillates in a circadian manner.
Induction
Expression is regulated by light and circadian rhythms. Under circadian regulation, expression is influenced by the clock pacemaker genes period, timeless, Clock and cycle.
Gene expression databases
Interaction
Subunit
Interacts with tim and per; promoted by light conditions (PubMed:10417378, PubMed:11448767).
Interaction with tim irreversibly commits tim to proteasomal degradation (PubMed:10417378).
Interacts with l1G0136/CG8198 (PubMed:26569474).
Interaction with tim irreversibly commits tim to proteasomal degradation (PubMed:10417378).
Interacts with l1G0136/CG8198 (PubMed:26569474).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O77059 | sgg P18431 | 2 | EBI-94117, EBI-242141 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-140 | Photolyase/cryptochrome alpha/beta | ||||
Sequence: GANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTL |
Domain
FAD-binding region regulates cry stability, cry-tim interaction, and circadian photosensitivity.
Photolyase/cryptochrome alpha/beta domain is sufficient for light detection and phototransduction.
Sequence similarities
Belongs to the DNA photolyase class-1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length542
- Mass (Da)62,513
- Last updated1998-11-01 v1
- ChecksumAB0019E5447BF56E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 232 | in Ref. 3; BAA35000 | ||||
Sequence: L → H | ||||||
Sequence conflict | 335 | in Ref. 3; BAA35000 | ||||
Sequence: D → E | ||||||
Sequence conflict | 348 | in Ref. 3; BAA35000 | ||||
Sequence: N → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF099734 EMBL· GenBank· DDBJ | AAC83828.1 EMBL· GenBank· DDBJ | mRNA | ||
AB018400 EMBL· GenBank· DDBJ | BAA33787.1 EMBL· GenBank· DDBJ | mRNA | ||
AB019389 EMBL· GenBank· DDBJ | BAA35000.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF55649.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY051514 EMBL· GenBank· DDBJ | AAK92938.1 EMBL· GenBank· DDBJ | mRNA |