CRY1_DROME
ID CRY1_DROME Reviewed; 542 AA.
AC O77059; Q9TYA0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cryptochrome-1;
DE Short=DmCRY1 {ECO:0000312|EMBL:BAA33787.1};
DE Short=dcry {ECO:0000312|EMBL:BAA35000.1};
DE AltName: Full=Blue light photoreceptor {ECO:0000312|EMBL:BAA35000.1};
GN Name=cry {ECO:0000312|EMBL:AAF55649.1, ECO:0000312|FlyBase:FBgn0025680};
GN ORFNames=CG3772;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC83828.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9845369; DOI=10.1016/s0092-8674(00)81637-2;
RA Emery P., So W.V., Kaneko M., Hall J.C., Rosbash M.;
RT "CRY, a Drosophila clock and light-regulated cryptochrome, is a major
RT contributor to circadian rhythm resetting and photosensitivity.";
RL Cell 95:669-679(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA33787.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, LACK OF PHOTOLYASE ACTIVITY, TISSUE
RP SPECIFICITY, AND FAD-BINDING.
RC STRAIN=Berkeley {ECO:0000269|PubMed:10063806};
RC TISSUE=Head {ECO:0000269|PubMed:10063806};
RX PubMed=10063806; DOI=10.1562/0031-8655(1999)069<0108:apblrf>2.3.co;2;
RA Okano S., Kanno S., Takao M., Eker A.P.M., Isono K., Tsukahara Y.,
RA Yasui A.;
RT "A putative blue-light receptor from Drosophila melanogaster.";
RL Photochem. Photobiol. 69:108-113(1999).
RN [3] {ECO:0000312|EMBL:BAA35000.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Head {ECO:0000312|EMBL:BAA35000.1};
RA Todo T., Ishikawa T.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAF55649.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAF55649.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6] {ECO:0000312|EMBL:AAK92938.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK92938.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7] {ECO:0000305}
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF
RP ASP-410, AND DISRUPTION PHENOTYPE.
RX PubMed=9845370; DOI=10.1016/s0092-8674(00)81638-4;
RA Stanewsky R., Kaneko M., Emery P., Beretta B., Wager-Smith K., Kay S.A.,
RA Rosbash M., Hall J.C.;
RT "The cryb mutation identifies cryptochrome as a circadian photoreceptor in
RT Drosophila.";
RL Cell 95:681-692(1998).
RN [8] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10233998; DOI=10.1523/jneurosci.19-10-03665.1999;
RA Egan E.S., Franklin T.M., Hilderbrand-Chae M.J., McNeil G.P., Roberts M.A.,
RA Schroeder A.J., Zhang X., Jackson F.R.;
RT "An extraretinally expressed insect cryptochrome with similarity to the
RT blue light photoreceptors of mammals and plants.";
RL J. Neurosci. 19:3665-3673(1999).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TIM, AND SUBCELLULAR LOCATION.
RX PubMed=10417378; DOI=10.1126/science.285.5427.553;
RA Ceriani M.F., Darlington T.K., Staknis D., Mas P., Petti A.A., Weitz C.J.,
RA Kay S.A.;
RT "Light-dependent sequestration of TIMELESS by CRYPTOCHROME.";
RL Science 285:553-556(1999).
RN [10]
RP INTERACTION WITH PER.
RX PubMed=11448767; DOI=10.1016/s0960-9822(01)00259-7;
RA Rosato E., Codd V., Mazzotta G., Piccin A., Zordan M., Costa R.,
RA Kyriacou C.P.;
RT "Light-dependent interaction between Drosophila CRY and the clock protein
RT PER mediated by the carboxy terminus of CRY.";
RL Curr. Biol. 11:909-917(2001).
RN [11] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND C-TERMINAL DOMAIN.
RX PubMed=15258584; DOI=10.1038/nn1285;
RA Dissel S., Codd V., Fedic R., Garner K.J., Costa R., Kyriacou C.P.,
RA Rosato E.;
RT "A constitutively active cryptochrome in Drosophila melanogaster.";
RL Nat. Neurosci. 7:834-840(2004).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=16527739; DOI=10.1016/j.cub.2006.01.034;
RA Collins B., Mazzoni E.O., Stanewsky R., Blau J.;
RT "Drosophila CRYPTOCHROME is a circadian transcriptional repressor.";
RL Curr. Biol. 16:441-449(2006).
RN [13] {ECO:0000305}
RP FUNCTION, AND FAD-BINDING.
RX PubMed=17298948; DOI=10.1074/jbc.m608872200;
RA Berndt A., Kottke T., Breitkreuz H., Dvorsky R., Hennig S., Alexander M.,
RA Wolf E.;
RT "A novel photoreaction mechanism for the circadian blue light photoreceptor
RT Drosophila cryptochrome.";
RL J. Biol. Chem. 282:13011-13021(2007).
RN [14] {ECO:0000305}
RP FUNCTION.
RX PubMed=18641630; DOI=10.1038/nature07183;
RA Gegear R.J., Casselman A., Waddell S., Reppert S.M.;
RT "Cryptochrome mediates light-dependent magnetosensitivity in Drosophila.";
RL Nature 454:1014-1018(2008).
RN [15] {ECO:0000305}
RP FUNCTION, AND FAD-BINDING.
RX PubMed=18597555; DOI=10.1371/journal.pbio.0060160;
RA Hoang N., Schleicher E., Kacprzak S., Bouly J.-P., Picot M., Wu W.,
RA Berndt A., Wolf E., Bittl R., Ahmad M.;
RT "Human and Drosophila cryptochromes are light activated by flavin
RT photoreduction in living cells.";
RL PLoS Biol. 6:E160-E160(2008).
RN [16]
RP INTERACTION WITH L(1)G0136.
RX PubMed=26569474; DOI=10.1038/nmat4484;
RA Qin S., Yin H., Yang C., Dou Y., Liu Z., Zhang P., Yu H., Huang Y.,
RA Feng J., Hao J., Hao J., Deng L., Yan X., Dong X., Zhao Z., Jiang T.,
RA Wang H.W., Luo S.J., Xie C.;
RT "A magnetic protein biocompass.";
RL Nat. Mater. 15:217-226(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, AND
RP MUTAGENESIS OF CYS-337; TRP-397; CYS-416; TRP-420; CYS-523 AND SER-526.
RX PubMed=23746849; DOI=10.1016/j.cell.2013.05.011;
RA Czarna A., Berndt A., Singh H.R., Grudziecki A., Ladurner A.G.,
RA Timinszky G., Kramer A., Wolf E.;
RT "Structures of Drosophila cryptochrome and mouse cryptochrome1 provide
RT insight into circadian function.";
RL Cell 153:1394-1405(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-539 IN COMPLEX WITH FAD.
RX PubMed=23518567; DOI=10.1038/nature11995;
RA Levy C., Zoltowski B.D., Jones A.R., Vaidya A.T., Top D., Widom J.,
RA Young M.W., Scrutton N.S., Crane B.R., Leys D.;
RT "Updated structure of Drosophila cryptochrome.";
RL Nature 495:E3-E4(2013).
CC -!- FUNCTION: Blue light-dependent regulator that is the input of the
CC circadian feedback loop. Has no photolyase activity for cyclobutane
CC pyrimidine dimers or 6-4 photoproducts. Regulation of expression by
CC light suggests a role in photoreception for locomotor activity rhythms.
CC Functions, together with per, as a transcriptional repressor required
CC for the oscillation of peripheral circadian clocks and for the correct
CC specification of clock cells. Genes directly activated by the
CC transcription factors Clock (Clk) and cycle (cyc) are repressed by cry.
CC Necessary for light-dependent magnetosensitivity, an intact circadian
CC system is not required for the magnetoreception mechanism to operate.
CC Required for both the naive and trained responses to magnetic field,
CC consistent with the notion that cry is in the input pathway of magnetic
CC sensing. {ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:10233998,
CC ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:16527739,
CC ECO:0000269|PubMed:17298948, ECO:0000269|PubMed:18597555,
CC ECO:0000269|PubMed:18641630, ECO:0000269|PubMed:9845369,
CC ECO:0000269|PubMed:9845370}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:17298948,
CC ECO:0000269|PubMed:18597555, ECO:0000269|PubMed:23746849};
CC Note=Binds 1 FAD per subunit. The bound form of FAD in the inactive
CC state of cry is oxidized FAD, not reduced. After activation by blue
CC light the FAD is in an anionic radical state, which would be
CC paramagnetic. Green light, which reduces levels of radical
CC intermediate, has an antagonistic effect on function.
CC {ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:17298948,
CC ECO:0000269|PubMed:18597555, ECO:0000269|PubMed:23746849};
CC -!- SUBUNIT: Interacts with tim and per; promoted by light conditions
CC (PubMed:10417378, PubMed:11448767). Interaction with tim irreversibly
CC commits tim to proteasomal degradation (PubMed:10417378). Interacts
CC with l(1)G0136/CG8198 (PubMed:26569474). {ECO:0000269|PubMed:10417378,
CC ECO:0000269|PubMed:11448767, ECO:0000269|PubMed:23518567,
CC ECO:0000269|PubMed:23746849, ECO:0000269|PubMed:26569474}.
CC -!- INTERACTION:
CC O77059; P18431: sgg; NbExp=2; IntAct=EBI-94117, EBI-242141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10417378,
CC ECO:0000269|PubMed:15258584}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Nucleus
CC {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}.
CC Note=Nuclear translocation initiates after the perception of a light
CC signal. Accumulates in the perinuclear region about one hour before
CC translocation into the nucleus. Translocation occurs through
CC interaction with other Clock proteins such as tim and per.
CC {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}.
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in the head than in body
CC and it is more expressed in antennae than in legs, wings and mouth
CC appendages. Prominent expression is seen in cells of the lateral brain,
CC which are close to or coincident with the clock neurons. Abundance
CC oscillates in a circadian manner. {ECO:0000269|PubMed:10063806,
CC ECO:0000269|PubMed:10233998, ECO:0000269|PubMed:9845369}.
CC -!- INDUCTION: Expression is regulated by light and circadian rhythms.
CC Under circadian regulation, expression is influenced by the clock
CC pacemaker genes period, timeless, Clock and cycle.
CC {ECO:0000269|PubMed:9845369}.
CC -!- DOMAIN: FAD-binding region regulates cry stability, cry-tim
CC interaction, and circadian photosensitivity.
CC {ECO:0000269|PubMed:15258584}.
CC -!- DOMAIN: Photolyase/cryptochrome alpha/beta domain is sufficient for
CC light detection and phototransduction.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit poor synchronization to light-dark
CC cycles and show no response to brief light pulses. Mutant abolishes
CC rhythmic tim and per expression in photoreceptor and glial cells, but
CC not within certain pacemaker neurons of adult brain.
CC {ECO:0000269|PubMed:9845370}.
CC -!- MISCELLANEOUS: Unstable upon light exposure. Light induces the
CC degradation of cry, likely due to conformational change in the
CC photoreceptor leading to targeting to the proteasome.
CC -!- MISCELLANEOUS: Appears to bind 5,10-methenyltetrahydrofolate at
CC substoichiometric levels. {ECO:0000269|PubMed:17298948}.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000255}.
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DR EMBL; AF099734; AAC83828.1; -; mRNA.
DR EMBL; AB018400; BAA33787.1; -; mRNA.
DR EMBL; AB019389; BAA35000.1; -; mRNA.
DR EMBL; AE014297; AAF55649.1; -; Genomic_DNA.
DR EMBL; AY051514; AAK92938.1; -; mRNA.
DR RefSeq; NP_732407.1; NM_169852.2.
DR PDB; 4GU5; X-ray; 2.30 A; A/B=1-539.
DR PDB; 4JZY; X-ray; 2.34 A; A/B=1-540.
DR PDB; 4K03; X-ray; 3.20 A; A/B=1-542.
DR PDB; 6WTB; X-ray; 2.58 A; A/B=1-539.
DR PDBsum; 4GU5; -.
DR PDBsum; 4JZY; -.
DR PDBsum; 4K03; -.
DR PDBsum; 6WTB; -.
DR AlphaFoldDB; O77059; -.
DR SMR; O77059; -.
DR BioGRID; 67302; 28.
DR DIP; DIP-29424N; -.
DR IntAct; O77059; 1.
DR STRING; 7227.FBpp0083150; -.
DR PaxDb; O77059; -.
DR PRIDE; O77059; -.
DR DNASU; 42305; -.
DR EnsemblMetazoa; FBtr0083736; FBpp0083150; FBgn0025680.
DR GeneID; 42305; -.
DR KEGG; dme:Dmel_CG3772; -.
DR UCSC; CG3772-RA; d. melanogaster.
DR CTD; 42305; -.
DR FlyBase; FBgn0025680; cry.
DR VEuPathDB; VectorBase:FBgn0025680; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_3_4_1; -.
DR InParanoid; O77059; -.
DR OMA; IWFRHGL; -.
DR OrthoDB; 378952at2759; -.
DR PhylomeDB; O77059; -.
DR Reactome; R-DME-432395; Degradation of TIM.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-538864; Degradation of CRY.
DR SignaLink; O77059; -.
DR BioGRID-ORCS; 42305; 0 hits in 3 CRISPR screens.
DR ChiTaRS; cry; fly.
DR GenomeRNAi; 42305; -.
DR PRO; PR:O77059; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0025680; Expressed in adult Malpighian tubule (Drosophila) and 34 other tissues.
DR Genevisible; O77059; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009882; F:blue light photoreceptor activity; IMP:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:FlyBase.
DR GO; GO:0009881; F:photoreceptor activity; IDA:FlyBase.
DR GO; GO:0009785; P:blue light signaling pathway; IMP:FlyBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:FlyBase.
DR GO; GO:0048512; P:circadian behavior; IMP:FlyBase.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0050980; P:detection of light stimulus involved in magnetoreception; IMP:UniProtKB.
DR GO; GO:0009649; P:entrainment of circadian clock; IDA:FlyBase.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:FlyBase.
DR GO; GO:0042332; P:gravitaxis; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0050958; P:magnetoreception; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0042752; P:regulation of circadian rhythm; IDA:FlyBase.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0009637; P:response to blue light; IMP:FlyBase.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR GO; GO:0071000; P:response to magnetism; IMP:FlyBase.
DR GO; GO:0009588; P:UV-A, blue light phototransduction; ISS:FlyBase.
DR Gene3D; 3.40.50.620; -; 1.
DR IDEAL; IID50267; -.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; PTHR11455; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; SSF48173; 1.
DR SUPFAM; SSF52425; SSF52425; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Chromophore; Cytoplasm; FAD;
KW Flavoprotein; Nucleotide-binding; Nucleus; Photoreceptor protein; Receptor;
KW Reference proteome; Repressor; Sensory transduction; Transcription;
KW Transcription regulation.
FT CHAIN 1..542
FT /note="Cryptochrome-1"
FT /id="PRO_0000348597"
FT DOMAIN 5..140
FT /note="Photolyase/cryptochrome alpha/beta"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23518567,
FT ECO:0000269|PubMed:23746849"
FT BINDING 265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23518567,
FT ECO:0000269|PubMed:23746849"
FT BINDING 267
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23518567,
FT ECO:0000269|PubMed:23746849"
FT BINDING 378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23518567,
FT ECO:0000269|PubMed:23746849"
FT BINDING 410..412
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23518567,
FT ECO:0000269|PubMed:23746849"
FT BINDING 416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23518567,
FT ECO:0000269|PubMed:23746849"
FT BINDING 419
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23518567,
FT ECO:0000269|PubMed:23746849"
FT MUTAGEN 337
FT /note="C->A: Accelerates formation and decay of the FAD
FT radical."
FT /evidence="ECO:0000269|PubMed:23746849"
FT MUTAGEN 397
FT /note="W->F: Abolishes formation of the FAD radical."
FT /evidence="ECO:0000269|PubMed:23746849"
FT MUTAGEN 410
FT /note="D->N: In cryb: Loss of accumulation."
FT /evidence="ECO:0000269|PubMed:9845370"
FT MUTAGEN 416
FT /note="C->A: Accelerates decay of the FAD radical."
FT /evidence="ECO:0000269|PubMed:23746849"
FT MUTAGEN 420
FT /note="W->A: Abolishes formation of the FAD radical."
FT /evidence="ECO:0000269|PubMed:23746849"
FT MUTAGEN 523
FT /note="C->A: Accelerates formation and decay of the FAD
FT radical."
FT /evidence="ECO:0000269|PubMed:23746849"
FT MUTAGEN 526
FT /note="S->A: Slows down the decay of the FAD radical."
FT /evidence="ECO:0000269|PubMed:23746849"
FT CONFLICT 232
FT /note="L -> H (in Ref. 3; BAA35000)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="D -> E (in Ref. 3; BAA35000)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="N -> D (in Ref. 3; BAA35000)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:4GU5"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:4GU5"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:4GU5"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:4JZY"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4JZY"
FT HELIX 227..247
FT /evidence="ECO:0007829|PDB:4GU5"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:6WTB"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 306..322
FT /evidence="ECO:0007829|PDB:4GU5"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 361..373
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:4GU5"
FT TURN 389..393
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 440..447
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 452..457
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4GU5"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:4K03"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:4GU5"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 498..516
FT /evidence="ECO:0007829|PDB:4GU5"
FT HELIX 528..535
FT /evidence="ECO:0007829|PDB:4GU5"
SQ SEQUENCE 542 AA; 62513 MW; AB0019E5447BF56E CRC64;
MATRGANVIW FRHGLRLHDN PALLAALADK DQGIALIPVF IFDGESAGTK NVGYNRMRFL
LDSLQDIDDQ LQAATDGRGR LLVFEGEPAY IFRRLHEQVR LHRICIEQDC EPIWNERDES
IRSLCRELNI DFVEKVSHTL WDPQLVIETN GGIPPLTYQM FLHTVQIIGL PPRPTADARL
EDATFVELDP EFCRSLKLFE QLPTPEHFNV YGDNMGFLAK INWRGGETQA LLLLDERLKV
EQHAFERGFY LPNQALPNIH DSPKSMSAHL RFGCLSVRRF YWSVHDLFKN VQLRACVRGV
QMTGGAHITG QLIWREYFYT MSVNNPNYDR MEGNDICLSI PWAKPNENLL QSWRLGQTGF
PLIDGAMRQL LAEGWLHHTL RNTVATFLTR GGLWQSWEHG LQHFLKYLLD ADWSVCAGNW
MWVSSSAFER LLDSSLVTCP VALAKRLDPD GTYIKQYVPE LMNVPKEFVH EPWRMSAEQQ
EQYECLIGVH YPERIIDLSM AVKRNMLAMK SLRNSLITPP PHCRPSNEEE VRQFFWLADV
VV
