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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei237 – 2371FAD2 Publications
Binding sitei265 – 2651FAD2 Publications
Binding sitei267 – 2671FAD; via amide nitrogenBy similarity
Binding sitei311 – 3111FAD2 Publications
Binding sitei378 – 3781FAD2 Publications
Binding sitei416 – 4161FAD2 Publications
Binding sitei419 – 4191FAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi410 – 4123FAD2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi337 – 3371C → A: Accelerates formation and decay of the FAD radical. 1 Publication
Mutagenesisi397 – 3971W → F: Abolishes formation of the FAD radical. 1 Publication
Mutagenesisi410 – 4101D → N in cryb: Loss of accumulation. 1 Publication
Mutagenesisi416 – 4161C → A: Accelerates decay of the FAD radical. 1 Publication
Mutagenesisi420 – 4201W → A: Abolishes formation of the FAD radical. 1 Publication
Mutagenesisi523 – 5231C → A: Accelerates formation and decay of the FAD radical. 1 Publication
Mutagenesisi526 – 5261S → A: Slows down the decay of the FAD radical. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Cryptochrome-1PRO_0000348597Add
BLAST

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

BgeeiO77059.
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 interactions.
DIPiDIP-29424N.
IntActiO77059. 1 interaction.
MINTiMINT-1328097.
STRINGi7227.FBpp0083150.

Structurei

Secondary structure

1
542
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138Combined sources
Beta strandi17 – 193Combined sources
Helixi21 – 277Combined sources
Helixi30 – 323Combined sources
Beta strandi35 – 428Combined sources
Turni46 – 483Combined sources
Helixi54 – 7421Combined sources
Turni75 – 773Combined sources
Beta strandi82 – 865Combined sources
Helixi88 – 9811Combined sources
Beta strandi101 – 1077Combined sources
Helixi112 – 1143Combined sources
Helixi115 – 12814Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi138 – 1414Combined sources
Helixi143 – 1497Combined sources
Turni150 – 1523Combined sources
Helixi158 – 16811Combined sources
Helixi190 – 1956Combined sources
Helixi205 – 2084Combined sources
Beta strandi212 – 2143Combined sources
Helixi227 – 24721Combined sources
Turni252 – 2543Combined sources
Helixi267 – 2715Combined sources
Helixi277 – 28812Combined sources
Beta strandi296 – 3016Combined sources
Helixi303 – 3053Combined sources
Helixi306 – 32217Combined sources
Turni326 – 3294Combined sources
Helixi347 – 3548Combined sources
Helixi361 – 37313Combined sources
Helixi378 – 38811Combined sources
Turni389 – 3935Combined sources
Helixi397 – 40711Combined sources
Helixi413 – 42513Combined sources
Helixi430 – 4334Combined sources
Helixi435 – 4384Combined sources
Helixi440 – 4478Combined sources
Helixi452 – 4576Combined sources
Helixi459 – 4613Combined sources
Beta strandi462 – 4643Combined sources
Helixi466 – 4694Combined sources
Helixi472 – 4743Combined sources
Helixi477 – 4826Combined sources
Turni487 – 4893Combined sources
Helixi498 – 51619Combined sources
Helixi528 – 5358Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GU5X-ray2.30A/B1-539[»]
4JZYX-ray2.34A/B1-540[»]
4K03X-ray3.20A/B1-542[»]
ProteinModelPortaliO77059.
SMRiO77059. Positions 2-539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 140136Photolyase/cryptochrome alpha/betaAdd
BLAST

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.
OMAiANVIWFR.
OrthoDBiEOG7QG43M.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321L → H in BAA35000 (Ref. 3) Curated
Sequence conflicti335 – 3351D → E in BAA35000 (Ref. 3) Curated
Sequence conflicti348 – 3481N → D in BAA35000 (Ref. 3) Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4GU5X-ray2.30A/B1-539[»]
4JZYX-ray2.34A/B1-540[»]
4K03X-ray3.20A/B1-542[»]
ProteinModelPortaliO77059.
SMRiO77059. Positions 2-539.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67302. 6 interactions.
DIPiDIP-29424N.
IntActiO77059. 1 interaction.
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.
OMAiANVIWFR.
OrthoDBiEOG7QG43M.
PhylomeDBiO77059.

Miscellaneous databases

GenomeRNAii42305.
PROiO77059.

Gene expression databases

BgeeiO77059.
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...

Publicationsi

« Hide 'large scale' publications
  1. "CRY, a Drosophila clock and light-regulated cryptochrome, is a major contributor to circadian rhythm resetting and photosensitivity."
    Emery P., So W.V., Kaneko M., Hall J.C., Rosbash M.
    Cell 95:669-679(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, LACK OF PHOTOLYASE ACTIVITY, TISSUE SPECIFICITY, FAD-BINDING.
    Strain: Berkeley1 Publication.
    Tissue: Head1 Publication.
  3. Todo T., Ishikawa T.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: HeadImported.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    Tissue: Head1 Publication.
  7. "The cryb mutation identifies cryptochrome as a circadian photoreceptor in Drosophila."
    Stanewsky R., Kaneko M., Emery P., Beretta B., Wager-Smith K., Kay S.A., Rosbash M., Hall J.C.
    Cell 95:681-692(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF ASP-410, DISRUPTION PHENOTYPE.
  8. "An extraretinally expressed insect cryptochrome with similarity to the blue light photoreceptors of mammals and plants."
    Egan E.S., Franklin T.M., Hilderbrand-Chae M.J., McNeil G.P., Roberts M.A., Schroeder A.J., Zhang X., Jackson F.R.
    J. Neurosci. 19:3665-3673(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "Light-dependent sequestration of TIMELESS by CRYPTOCHROME."
    Ceriani M.F., Darlington T.K., Staknis D., Mas P., Petti A.A., Weitz C.J., Kay S.A.
    Science 285:553-556(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TIM, SUBCELLULAR LOCATION.
  10. "Light-dependent interaction between Drosophila CRY and the clock protein PER mediated by the carboxy terminus of CRY."
    Rosato E., Codd V., Mazzotta G., Piccin A., Zordan M., Costa R., Kyriacou C.P.
    Curr. Biol. 11:909-917(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PER.
  11. "A constitutively active cryptochrome in Drosophila melanogaster."
    Dissel S., Codd V., Fedic R., Garner K.J., Costa R., Kyriacou C.P., Rosato E.
    Nat. Neurosci. 7:834-840(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, C-TERMINAL DOMAIN.
  12. "Drosophila CRYPTOCHROME is a circadian transcriptional repressor."
    Collins B., Mazzoni E.O., Stanewsky R., Blau J.
    Curr. Biol. 16:441-449(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome."
    Berndt A., Kottke T., Breitkreuz H., Dvorsky R., Hennig S., Alexander M., Wolf E.
    J. Biol. Chem. 282:13011-13021(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FAD-BINDING.
  14. "Cryptochrome mediates light-dependent magnetosensitivity in Drosophila."
    Gegear R.J., Casselman A., Waddell S., Reppert S.M.
    Nature 454:1014-1018(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Human and Drosophila cryptochromes are light activated by flavin photoreduction in living cells."
    Hoang N., Schleicher E., Kacprzak S., Bouly J.-P., Picot M., Wu W., Berndt A., Wolf E., Bittl R., Ahmad M.
    PLoS Biol. 6:E160-E160(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FAD-BINDING.
  16. Cited for: INTERACTION WITH L(1)G0136.
  17. "Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function."
    Czarna A., Berndt A., Singh H.R., Grudziecki A., Ladurner A.G., Timinszky G., Kramer A., Wolf E.
    Cell 153:1394-1405(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, MUTAGENESIS OF CYS-337; TRP-397; CYS-416; TRP-420; CYS-523 AND SER-526.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-539 IN COMPLEX WITH FAD.

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: July 6, 2016
This is version 129 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.