Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cryptochrome-1

Gene

cry

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry. Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate. 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.9 Publications

Cofactori

FAD4 PublicationsNote: 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.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei237FAD2 Publications1
Binding sitei265FAD2 Publications1
Binding sitei267FAD; via amide nitrogenBy similarity1
Binding sitei311FAD2 Publications1
Binding sitei378FAD2 Publications1
Binding sitei416FAD2 Publications1
Binding sitei419FAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi410 – 412FAD2 Publications3

GO - Molecular functioni

  • blue light photoreceptor activity Source: UniProtKB
  • FAD binding Source: UniProtKB
  • flavin adenine dinucleotide binding Source: UniProtKB
  • G-protein coupled photoreceptor activity Source: FlyBase
  • photoreceptor activity Source: UniProtKB

GO - Biological processi

  • blue light signaling pathway Source: FlyBase
  • circadian rhythm Source: FlyBase
  • detection of light stimulus involved in magnetoreception Source: UniProtKB
  • entrainment of circadian clock Source: FlyBase
  • entrainment of circadian clock by photoperiod Source: FlyBase
  • gravitaxis Source: FlyBase
  • locomotor rhythm Source: FlyBase
  • magnetoreception Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • phototransduction Source: FlyBase
  • protein-chromophore linkage Source: UniProtKB-KW
  • protein import into nucleus, translocation Source: UniProtKB
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of circadian sleep/wake cycle, sleep Source: FlyBase
  • response to blue light Source: FlyBase
  • response to light stimulus Source: FlyBase
  • response to magnetism Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • UV-A, blue light phototransduction Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Photoreceptor protein, Receptor, Repressor

Keywords - Biological processi

Biological rhythms, Sensory transduction, Transcription, Transcription regulation

Keywords - Ligandi

Chromophore, FAD, Flavoprotein, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cryptochrome-1
Short name:
DmCRY1Imported
Short name:
dcryImported
Alternative name(s):
Blue light photoreceptorImported
Gene namesi
Name:cryImported
ORF Names:CG3772
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0025680. cry.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • nuclear envelope lumen Source: FlyBase
  • nucleus Source: FlyBase
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi337C → A: Accelerates formation and decay of the FAD radical. 1 Publication1
Mutagenesisi397W → F: Abolishes formation of the FAD radical. 1 Publication1
Mutagenesisi410D → N in cryb: Loss of accumulation. 1 Publication1
Mutagenesisi416C → A: Accelerates decay of the FAD radical. 1 Publication1
Mutagenesisi420W → A: Abolishes formation of the FAD radical. 1 Publication1
Mutagenesisi523C → A: Accelerates formation and decay of the FAD radical. 1 Publication1
Mutagenesisi526S → A: Slows down the decay of the FAD radical. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003485971 – 542Cryptochrome-1Add BLAST542

Proteomic databases

PaxDbiO77059.
PRIDEiO77059.

Expressioni

Tissue specificityi

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.3 Publications

Inductioni

Expression is regulated by light and circadian rhythms. Under circadian regulation, expression is influenced by the clock pacemaker genes period, timeless, Clock and cycle.1 Publication

Gene expression databases

BgeeiFBgn0025680.
GenevisibleiO77059. DM.

Interactioni

Subunit structurei

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).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
sggP184312EBI-94117,EBI-242141

Protein-protein interaction databases

BioGridi67302. 6 interactors.
DIPiDIP-29424N.
IntActiO77059. 1 interactor.
MINTiMINT-1328097.
STRINGi7227.FBpp0083150.

Structurei

Secondary structure

1542
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Beta strandi17 – 19Combined sources3
Helixi21 – 27Combined sources7
Helixi30 – 32Combined sources3
Beta strandi35 – 42Combined sources8
Turni46 – 48Combined sources3
Helixi54 – 74Combined sources21
Turni75 – 77Combined sources3
Beta strandi82 – 86Combined sources5
Helixi88 – 98Combined sources11
Beta strandi101 – 107Combined sources7
Helixi112 – 114Combined sources3
Helixi115 – 128Combined sources14
Beta strandi131 – 135Combined sources5
Beta strandi138 – 141Combined sources4
Helixi143 – 149Combined sources7
Turni150 – 152Combined sources3
Helixi158 – 168Combined sources11
Helixi190 – 195Combined sources6
Helixi205 – 208Combined sources4
Beta strandi212 – 214Combined sources3
Helixi227 – 247Combined sources21
Turni252 – 254Combined sources3
Helixi267 – 271Combined sources5
Helixi277 – 288Combined sources12
Beta strandi296 – 301Combined sources6
Helixi303 – 305Combined sources3
Helixi306 – 322Combined sources17
Turni326 – 329Combined sources4
Helixi347 – 354Combined sources8
Helixi361 – 373Combined sources13
Helixi378 – 388Combined sources11
Turni389 – 393Combined sources5
Helixi397 – 407Combined sources11
Helixi413 – 425Combined sources13
Helixi430 – 433Combined sources4
Helixi435 – 438Combined sources4
Helixi440 – 447Combined sources8
Helixi452 – 457Combined sources6
Helixi459 – 461Combined sources3
Beta strandi462 – 464Combined sources3
Helixi466 – 469Combined sources4
Helixi472 – 474Combined sources3
Helixi477 – 482Combined sources6
Turni487 – 489Combined sources3
Helixi498 – 516Combined sources19
Helixi528 – 535Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GU5X-ray2.30A/B1-539[»]
4JZYX-ray2.34A/B1-540[»]
4K03X-ray3.20A/B1-542[»]
ProteinModelPortaliO77059.
SMRiO77059.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 140Photolyase/cryptochrome alpha/betaAdd BLAST136

Domaini

FAD-binding region regulates cry stability, cry-tim interaction, and circadian photosensitivity.1 Publication
Photolyase/cryptochrome alpha/beta domain is sufficient for light detection and phototransduction.

Sequence similaritiesi

Belongs to the DNA photolyase class-1 family.Sequence analysis

Phylogenomic databases

eggNOGiKOG0133. Eukaryota.
COG0415. LUCA.
GeneTreeiENSGT00500000044813.
InParanoidiO77059.
KOiK02295.
OMAiRACVRGV.
OrthoDBiEOG091G07M3.
PhylomeDBiO77059.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR005101. Cryptochr/Photolyase_FAD-bd.
IPR002081. Cryptochrome/DNA_photolyase_1.
IPR006050. DNA_photolyase_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00875. DNA_photolyase. 1 hit.
PF03441. FAD_binding_7. 1 hit.
[Graphical view]
PRINTSiPR00147. DNAPHOTLYASE.
SUPFAMiSSF48173. SSF48173. 1 hit.
SSF52425. SSF52425. 1 hit.
PROSITEiPS51645. PHR_CRY_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O77059-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATRGANVIW FRHGLRLHDN PALLAALADK DQGIALIPVF IFDGESAGTK
60 70 80 90 100
NVGYNRMRFL LDSLQDIDDQ LQAATDGRGR LLVFEGEPAY IFRRLHEQVR
110 120 130 140 150
LHRICIEQDC EPIWNERDES IRSLCRELNI DFVEKVSHTL WDPQLVIETN
160 170 180 190 200
GGIPPLTYQM FLHTVQIIGL PPRPTADARL EDATFVELDP EFCRSLKLFE
210 220 230 240 250
QLPTPEHFNV YGDNMGFLAK INWRGGETQA LLLLDERLKV EQHAFERGFY
260 270 280 290 300
LPNQALPNIH DSPKSMSAHL RFGCLSVRRF YWSVHDLFKN VQLRACVRGV
310 320 330 340 350
QMTGGAHITG QLIWREYFYT MSVNNPNYDR MEGNDICLSI PWAKPNENLL
360 370 380 390 400
QSWRLGQTGF PLIDGAMRQL LAEGWLHHTL RNTVATFLTR GGLWQSWEHG
410 420 430 440 450
LQHFLKYLLD ADWSVCAGNW MWVSSSAFER LLDSSLVTCP VALAKRLDPD
460 470 480 490 500
GTYIKQYVPE LMNVPKEFVH EPWRMSAEQQ EQYECLIGVH YPERIIDLSM
510 520 530 540
AVKRNMLAMK SLRNSLITPP PHCRPSNEEE VRQFFWLADV VV
Length:542
Mass (Da):62,513
Last modified:November 1, 1998 - v1
Checksum:iAB0019E5447BF56E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti232L → H in BAA35000 (Ref. 3) Curated1
Sequence conflicti335D → E in BAA35000 (Ref. 3) Curated1
Sequence conflicti348N → D in BAA35000 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099734 mRNA. Translation: AAC83828.1.
AB018400 mRNA. Translation: BAA33787.1.
AB019389 mRNA. Translation: BAA35000.1.
AE014297 Genomic DNA. Translation: AAF55649.1.
AY051514 mRNA. Translation: AAK92938.1.
RefSeqiNP_732407.1. NM_169852.2.
UniGeneiDm.4579.

Genome annotation databases

EnsemblMetazoaiFBtr0083736; FBpp0083150; FBgn0025680.
GeneIDi42305.
KEGGidme:Dmel_CG3772.
UCSCiCG3772-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099734 mRNA. Translation: AAC83828.1.
AB018400 mRNA. Translation: BAA33787.1.
AB019389 mRNA. Translation: BAA35000.1.
AE014297 Genomic DNA. Translation: AAF55649.1.
AY051514 mRNA. Translation: AAK92938.1.
RefSeqiNP_732407.1. NM_169852.2.
UniGeneiDm.4579.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GU5X-ray2.30A/B1-539[»]
4JZYX-ray2.34A/B1-540[»]
4K03X-ray3.20A/B1-542[»]
ProteinModelPortaliO77059.
SMRiO77059.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67302. 6 interactors.
DIPiDIP-29424N.
IntActiO77059. 1 interactor.
MINTiMINT-1328097.
STRINGi7227.FBpp0083150.

Proteomic databases

PaxDbiO77059.
PRIDEiO77059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083736; FBpp0083150; FBgn0025680.
GeneIDi42305.
KEGGidme:Dmel_CG3772.
UCSCiCG3772-RA. d. melanogaster.

Organism-specific databases

CTDi42305.
FlyBaseiFBgn0025680. cry.

Phylogenomic databases

eggNOGiKOG0133. Eukaryota.
COG0415. LUCA.
GeneTreeiENSGT00500000044813.
InParanoidiO77059.
KOiK02295.
OMAiRACVRGV.
OrthoDBiEOG091G07M3.
PhylomeDBiO77059.

Miscellaneous databases

GenomeRNAii42305.
PROiO77059.

Gene expression databases

BgeeiFBgn0025680.
GenevisibleiO77059. DM.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR005101. Cryptochr/Photolyase_FAD-bd.
IPR002081. Cryptochrome/DNA_photolyase_1.
IPR006050. DNA_photolyase_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00875. DNA_photolyase. 1 hit.
PF03441. FAD_binding_7. 1 hit.
[Graphical view]
PRINTSiPR00147. DNAPHOTLYASE.
SUPFAMiSSF48173. SSF48173. 1 hit.
SSF52425. SSF52425. 1 hit.
PROSITEiPS51645. PHR_CRY_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCRY1_DROME
AccessioniPrimary (citable) accession number: O77059
Secondary accession number(s): Q9TYA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.